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   A2A653_MOUSE            Unreviewed;       289 AA.
AC   A2A653;
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=Bromodomain PHD finger transcription factor;
DE   Flags: Fragment;
GN   Name=Bptf; ORFNames=RP23-317F9.3-003;
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   Beasley H.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL596116; CAM20630.1; -; Genomic_DNA.
DR   IPI; IPI00828260; -.
DR   UniGene; Mm.343986; -.
DR   Ensembl; ENSMUST00000041145; ENSMUSP00000042085; ENSMUSG00000040481.
DR   Ensembl; ENSMUST00000149486; ENSMUSP00000122575; ENSMUSG00000040481.
DR   MGI; MGI:2444008; Bptf.
DR   GeneTree; ENSGT00430000030976; -.
DR   Bgee; A2A653; -.
DR   Genevestigator; A2A653; -.
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.
PE   4: Predicted;
FT   NON_TER       1      1
FT   NON_TER     289    289
SQ   SEQUENCE   289 AA;  30606 MW;  AD2B76AD557ED4CE CRC64;
     VGPYGIRSEY CIRKIICPIG VPEAPKETPT PQRKGLRSSA LRPKRPETPK QTGPVIIESW
     VAEEELELWE IRAFAERVEK EKAQAAEQQT KKRLEQQKPA VIAASTTSPA NNTSSTVSPA
     QKVMVAPLSG SVTPGTKMVL ATKVGSPATV TFQQNKNFHQ TFATWVKQGQ SNSATSTAAT
     SATTIASTGQ TFQITGSPVT MAGKVITKLP LPANSKIVAV NVPATQGGMV QVQQKVLGII
     PSTTGPSQQT FTSFQPRTAT VTIRPNTSAS AGTTTTSQVI TGPQIRPGM
//
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.
CC   -----------------------------------------------------------------------
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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   A2A6S2_MOUSE            Unreviewed;      1239 AA.
AC   A2A6S2;
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=Glutamate receptor, ionotropic, NMDA2C (Epsilon 3);
DE   SubName: Full=Grin2c protein;
GN   Name=Grin2c; ORFNames=RP23-117K15.2-001, mCG_6611;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; 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.
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; BC137849; AAI37850.1; -; mRNA.
DR   EMBL; AL603828; CAM13800.1; -; Genomic_DNA.
DR   EMBL; CH466558; EDL34470.1; -; Genomic_DNA.
DR   IPI; IPI00321321; -.
DR   RefSeq; NP_034480.2; NM_010350.2.
DR   UniGene; Mm.39090; -.
DR   ProteinModelPortal; A2A6S2; -.
DR   SMR; A2A6S2; 27-390, 401-799.
DR   STRING; A2A6S2; -.
DR   PRIDE; A2A6S2; -.
DR   Ensembl; ENSMUST00000003351; ENSMUSP00000003351; ENSMUSG00000020734.
DR   Ensembl; ENSMUST00000106554; ENSMUSP00000102164; ENSMUSG00000020734.
DR   GeneID; 14813; -.
DR   KEGG; mmu:14813; -.
DR   CTD; 14813; -.
DR   MGI; MGI:95822; Grin2c.
DR   eggNOG; roNOG06546; -.
DR   HOVERGEN; HBG052636; -.
DR   InParanoid; A2A6S2; -.
DR   OMA; HYSSFPR; -.
DR   PhylomeDB; A2A6S2; -.
DR   NextBio; 287007; -.
DR   Bgee; A2A6S2; -.
DR   Genevestigator; A2A6S2; -.
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-KW.
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   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   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   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   A2AA49_MOUSE            Unreviewed;       377 AA.
AC   A2AA49;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   11-JAN-2011, entry version 42.
DE   SubName: Full=Guanine nucleotide binding protein, alpha 13;
DE   SubName: Full=Guanine nucleotide binding protein, alpha 13, isoform CRA_b;
GN   Name=Gna13; ORFNames=RP23-465A12.1-001, mCG_19634;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; 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   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   Pearce A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL645583; CAM14525.1; -; Genomic_DNA.
DR   EMBL; AL645791; CAM14525.1; JOINED; Genomic_DNA.
DR   EMBL; AL645791; CAM25209.1; -; Genomic_DNA.
DR   EMBL; AL645583; CAM25209.1; JOINED; Genomic_DNA.
DR   EMBL; CH466558; EDL34354.1; -; Genomic_DNA.
DR   IPI; IPI00118569; -.
DR   RefSeq; NP_034433.3; NM_010303.3.
DR   UniGene; Mm.193925; -.
DR   ProteinModelPortal; A2AA49; -.
DR   SMR; A2AA49; 47-369.
DR   STRING; A2AA49; -.
DR   PRIDE; A2AA49; -.
DR   Ensembl; ENSMUST00000020930; ENSMUSP00000020930; ENSMUSG00000020611.
DR   GeneID; 14674; -.
DR   KEGG; mmu:14674; -.
DR   CTD; 14674; -.
DR   MGI; MGI:95768; Gna13.
DR   eggNOG; roNOG10942; -.
DR   HOVERGEN; HBG063184; -.
DR   InParanoid; A2AA49; -.
DR   OMA; RVFLQYL; -.
DR   PhylomeDB; A2AA49; -.
DR   NextBio; 286562; -.
DR   Bgee; A2AA49; -.
DR   Genevestigator; A2AA49; -.
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:InterPro.
DR   GO; GO:0007189; P:activation of adenylate cyclase activity by G-protein signaling pathway; IGI:MGI.
DR   GO; GO:0030154; P:cell differentiation; IDA:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR   GO; GO:0007243; P:intracellular protein kinase cascade; IDA:MGI.
DR   GO; GO:0001569; P:patterning of blood vessels; IMP:MGI.
DR   GO; GO:0030168; P:platelet activation; IMP:MGI.
DR   GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; IDA:MGI.
DR   GO; GO:0007266; P:Rho protein signal transduction; IDA:MGI.
DR   InterPro; IPR000469; Gprotein_alpha12.
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; PR00440; GPROTEINA12.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF47895; Transducn_insert; 1.
PE   4: Predicted;
KW   GTP-binding; Nucleotide-binding.
SQ   SEQUENCE   377 AA;  44055 MW;  45A6A6DB47C707BB CRC64;
     MADFLPSRSV LSVCFPGCVL TNGEAEQQRK SKEIDKCLSR EKTYVKRLVK ILLLGAGESG
     KSTFLKQMRI IHGQDFDQRA REEFRPTIYS NVIKGMRVLV DAREKLHIPW GDNKNQLHGD
     KLMAFDTRAP MAAQGMVETR VFLQYLPAIR ALWEDSGIQN AYDRRREFQL GESVKYFLDN
     LDKLGVPDYI PSQQDILLAR RPTKGIHEYD FEIKNVPFKM VDVGGQRSER KRWFECFDSV
     TSILFLVSSS EFDQVLMEDR QTNRLTESLN IFETIVNNRV FSNVSIILFL NKTDLLEEKV
     QVVSIKDYFL EFEGDPHCLR DVQKFLVECF RGKRRDQQQR PLYHHFTTAI NTENIRLVFR
     DVKDTILHDN LKQLMLQ
//
ID   A2AC70_MOUSE            Unreviewed;       679 AA.
AC   A2AC70;
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=TAF4A RNA polymerase II, TATA box binding protein (TBP)-associated factor;
DE   Flags: Fragment;
GN   Name=Taf4a; ORFNames=RP23-23G3.2-001;
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   Tracey A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL663067; CAM18347.1; -; Genomic_DNA.
DR   IPI; IPI00853742; -.
DR   UniGene; Mm.235542; -.
DR   STRING; A2AC70; -.
DR   Ensembl; ENSMUST00000041618; ENSMUSP00000038610; ENSMUSG00000039117.
DR   Ensembl; ENSMUST00000131358; ENSMUSP00000118917; ENSMUSG00000039117.
DR   MGI; MGI:2152346; Taf4a.
DR   eggNOG; roNOG10763; -.
DR   HOGENOM; HBG505913; -.
DR   HOVERGEN; HBG058585; -.
DR   InParanoid; A2AC70; -.
DR   OrthoDB; EOG4CJVH7; -.
DR   Bgee; A2AC70; -.
DR   Genevestigator; A2AC70; -.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0016251; F:general RNA polymerase II transcription factor activity; TAS:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR007900; TAF4.
DR   InterPro; IPR003894; TAFH_NHR1.
DR   Gene3D; G3DSA:1.10.20.10; Histone-fold; 1.
DR   Pfam; PF05236; TAF4; 1.
DR   Pfam; PF07531; TAFH; 1.
DR   SMART; SM00549; TAFH; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
DR   PROSITE; PS51119; TAFH; 1.
PE   4: Predicted;
FT   NON_TER       1      1
SQ   SEQUENCE   679 AA;  73137 MW;  2DC341B5020E0D60 CRC64;
     AAATPSLPRT PAATTGAIRA TLTPTVLAPR LPQPPQNPTN IQNFQLPPGM VLVRSENGQL
     LMIPQQALAQ MQAHAQAQPQ STMAPRPATP TGAPPVQIST VQAPGTPIIA RQVTPTTIIK
     QVSQAQTTVQ PTTTLQRSPG VQPQLVLGGS AQPASLGTAT AVQTGTPQRT VPGASTTSTA
     ATETMENVKK CKSFLSTLIK LASSGKQSTE TAANVKDLVQ NLLDGKIEAE DFTSRLYREL
     NSSPQPYLVP FLKRSLPALR QLTPDSAAFI QQSQQQQPPA SQATTALTAV VLSSSVQRTA
     GKTAASVTSA LQPPVISLTQ PTQVGVGKQA PPTPLVIQQP PKPGALIRPP QVTLTQTPMV
     ALRQPHNRIM LTTPQQIQLN QLQPVPVVKP TVLPGTKALS TVSAQAAAAQ KNKLKEPGGG
     SFRDDDDIND VASMAGVNLS EESARILATN SELVGTLTRS CKDDTFLLPA PLQRRILEIG
     KKHGITELHP DVVSYVSHAT QQRLQNLVEK ISETAQQKNF SYKDDDRYEQ ASDVRAQLKF
     FEQLDQIEKQ RKDEQEREIL MRAAKSRSRQ EDPEQLRLKQ KAKEMQQQEL AQMRQRDANL
     TALAAIGPRK KRKVDCTGPG SGAEGSGPGA AVPGGSGVGT PRQFTRQRIT RVNLRDLIFC
     LENERETSHS LLLYKAFLK
//
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   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   AMRA1_MOUSE             Reviewed;        1300 AA.
AC   A2AH22; A2AH21; A2AH24; Q3TF60; Q3U239; Q3UF70; Q6ZPJ1; Q8BJJ8;
AC   Q8BYW8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Activating molecule in BECN1-regulated autophagy protein 1;
GN   Name=Ambra1; Synonyms=Kiaa1736;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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/6J, and NOD; 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   [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] OF 126-1300.
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, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE
RP   SPECIFICITY, AND INTERACTION WITH BECN1 AND PIK3C3.
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).
RN   [5]
RP   REVIEW.
RX   PubMed=17603510; DOI=10.1038/ncb0707-741;
RA   Le Bot N.;
RT   "Autophagy: a new regulator of development.";
RL   Nat. Cell Biol. 9:741-741(2007).
CC   -!- FUNCTION: Regulates autophagy and development of the nervous
CC       system. Involved in autophagy in controlling protein turnover
CC       during neuronal development, and in regulating normal cell
CC       survival and proliferation.
CC   -!- SUBUNIT: Interacts with BECN1. Probably forms a complex with BECN1
CC       and PIK3C3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome
CC       (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=1;
CC         IsoId=A2AH22-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AH22-2; Sequence=VSP_030658;
CC       Name=3;
CC         IsoId=A2AH22-3; Sequence=VSP_030661;
CC       Name=4;
CC         IsoId=A2AH22-4; Sequence=VSP_030659, VSP_030661;
CC       Name=5;
CC         IsoId=A2AH22-5; Sequence=VSP_030658, VSP_030659, VSP_030662,
CC                                  VSP_030663;
CC       Name=6;
CC         IsoId=A2AH22-6; Sequence=VSP_030660;
CC       Name=7;
CC         IsoId=A2AH22-7; Sequence=VSP_030658, VSP_030659;
CC   -!- DEVELOPMENTAL STAGE: At E8.5, it is detected throughout the
CC       neuroepithelium. At E11.5, it is highly expressed in the ventral-
CC       most part of the spinal cord, the encephalic vesicles, the neural
CC       retina, the limbs and the dorsal root ganglia. Later, it is
CC       expressed in the entire developing nervous system as well as in
CC       other tissues. In brain, strong expression is observed in the
CC       cortex, hippocampus and striatum of postnatal brain.
CC   -!- DISRUPTION PHENOTYPE: Mice display severe neural tube defects
CC       associated with autophagy impairment, accumulation of
CC       ubiquitinated proteins, unbalanced cell proliferation and
CC       excessive apoptotic cell death.
CC   -!- SIMILARITY: Contains 3 WD repeats.
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DR   EMBL; AK037516; BAC29823.1; -; mRNA.
DR   EMBL; AK083596; BAC38965.1; -; mRNA.
DR   EMBL; AK148887; BAE28691.1; -; mRNA.
DR   EMBL; AK155513; BAE33303.1; -; mRNA.
DR   EMBL; AK169280; BAE41038.1; -; mRNA.
DR   EMBL; AL714023; CAM14517.1; -; Genomic_DNA.
DR   EMBL; AL731772; CAM14517.1; JOINED; Genomic_DNA.
DR   EMBL; AL714023; CAM14518.1; -; Genomic_DNA.
DR   EMBL; AL731772; CAM14518.1; JOINED; Genomic_DNA.
DR   EMBL; AL714023; CAM14519.1; -; Genomic_DNA.
DR   EMBL; AL731772; CAM14519.1; JOINED; Genomic_DNA.
DR   EMBL; AL714023; CAM14520.1; -; Genomic_DNA.
DR   EMBL; AL731772; CAM14520.1; JOINED; Genomic_DNA.
DR   EMBL; AL731772; CAM19280.1; -; Genomic_DNA.
DR   EMBL; AL714023; CAM19280.1; JOINED; Genomic_DNA.
DR   EMBL; AL731772; CAM19281.1; -; Genomic_DNA.
DR   EMBL; AL714023; CAM19281.1; JOINED; Genomic_DNA.
DR   EMBL; AL731772; CAM19282.1; -; Genomic_DNA.
DR   EMBL; AL714023; CAM19282.1; JOINED; Genomic_DNA.
DR   EMBL; AL731772; CAM19283.1; -; Genomic_DNA.
DR   EMBL; AL714023; CAM19283.1; JOINED; Genomic_DNA.
DR   EMBL; AK129433; BAC98243.1; -; mRNA.
DR   IPI; IPI00261808; -.
DR   IPI; IPI00622790; -.
DR   IPI; IPI00653387; -.
DR   IPI; IPI00654077; -.
DR   IPI; IPI00752741; -.
DR   IPI; IPI00880527; -.
DR   IPI; IPI00881898; -.
DR   RefSeq; NP_001074223.1; NM_001080754.1.
DR   RefSeq; NP_766257.3; NM_172669.3.
DR   UniGene; Mm.436667; -.
DR   ProteinModelPortal; A2AH22; -.
DR   SMR; A2AH22; 49-209, 1011-1036.
DR   PhosphoSite; A2AH22; -.
DR   PRIDE; A2AH22; -.
DR   Ensembl; ENSMUST00000045705; ENSMUSP00000049258; ENSMUSG00000040506.
DR   Ensembl; ENSMUST00000099712; ENSMUSP00000097299; ENSMUSG00000040506.
DR   Ensembl; ENSMUST00000111316; ENSMUSP00000106948; ENSMUSG00000040506.
DR   Ensembl; ENSMUST00000111317; ENSMUSP00000106949; ENSMUSG00000040506.
DR   GeneID; 228361; -.
DR   KEGG; mmu:228361; -.
DR   CTD; 228361; -.
DR   MGI; MGI:2443564; Ambra1.
DR   eggNOG; roNOG07312; -.
DR   GeneTree; ENSGT00390000016223; -.
DR   HOVERGEN; HBG103818; -.
DR   InParanoid; A2AH22; -.
DR   OMA; YPDPARD; -.
DR   OrthoDB; EOG40S0DX; -.
DR   NextBio; 378972; -.
DR   Bgee; A2AH22; -.
DR   CleanEx; MM_AMBRA1; -.
DR   Genevestigator; A2AH22; -.
DR   GO; GO:0005776; C:autophagic vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0006914; P:autophagy; IMP:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0021915; P:neural tube development; IMP:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptosis; 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; 2.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00320; WD40; 3.
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   Alternative splicing; Autophagy; Cytoplasmic vesicle;
KW   Developmental protein; Differentiation; Neurogenesis; Phosphoprotein;
KW   Repeat; WD repeat.
FT   CHAIN         1   1300       Activating molecule in BECN1-regulated
FT                                autophagy protein 1.
FT                                /FTId=PRO_0000315704.
FT   REPEAT       51     90       WD 1.
FT   REPEAT       93    133       WD 2.
FT   REPEAT      135    175       WD 3.
FT   COMPBIAS    268    277       Poly-Pro.
FT   COMPBIAS    756    763       Poly-Ser.
FT   COMPBIAS   1120   1125       Poly-Glu.
FT   MOD_RES     640    640       Phosphoserine (By similarity).
FT   VAR_SEQ     255    345       Missing (in isoform 2, isoform 5 and
FT                                isoform 7).
FT                                /FTId=VSP_030658.
FT   VAR_SEQ     692    720       Missing (in isoform 4, isoform 5 and
FT                                isoform 7).
FT                                /FTId=VSP_030659.
FT   VAR_SEQ     722    781       Missing (in isoform 6).
FT                                /FTId=VSP_030660.
FT   VAR_SEQ     782   1300       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_030661.
FT   VAR_SEQ    1010   1016       VSINSAR -> QRSTSLK (in isoform 5).
FT                                /FTId=VSP_030662.
FT   VAR_SEQ    1017   1300       Missing (in isoform 5).
FT                                /FTId=VSP_030663.
FT   CONFLICT    111    111       I -> T (in Ref. 1; BAE33303).
FT   CONFLICT    492    492       N -> K (in Ref. 1; BAE33303).
SQ   SEQUENCE   1300 AA;  142879 MW;  081C4E14166B4985 CRC64;
     MKVVPEKNAV RILWGRERGT RAMGAQRLLQ ELVEDKTRWM KWEGKRVELP DSPRSTFLLA
     FSPDRTLLAS THVNHNIYIT EVKTGKCVHS LIGHRRTPWC VTFHPTISGL IASGCLDGEV
     RIWDLHGGSE SWFTDSNNAI ASLAFHPTAQ LLLIATANEI HFWDWSRREP FAVVKTASEM
     ERVRLVRFDP LGHYLLTAIV NPSNQQGDDE PEIPIDGTEL SHYRQRALLQ SQPVRRTPLL
     HNFLHMLSSR SSGIQVGEQS TVQDSATPSP PPPPPQPSTE RPRTSAYIRL RQRVSYPTTV
     ECCQHPGILC LCSRCAGTRV PSLLPHQDSV PPASARATTP SFSFVQTEPF HPPEQASSTQ
     QDQGLLNRPS AFSTVQSSTA GNTLRNLSLG PTRRSLGGPL SSHPSRYHRE LAPGLTGSEW
     TRTVLTLNSR SEVESMPPPR TSASSVSLLS VLRQQEGGSQ ASVYTSATEG RGFPSSGLAT
     ESDGGNGSSQ NNSGSIRHEL QCDLRRFFLE YDRLQELDQS LSGETPQTQQ AQEMLNNNIE
     SERPGPSHLP TPHSSENNSN LSRGHLNRCR ACHNLLTFNN DTLRWERTTP NYSSGEASSS
     WHVSTTFEGM PPSGNQLPPL ERTEGQMPSS SRLELSSSAS SQEERTVGVA FNQETGHWER
     IYTQSSRSGT VSQEALHQDM PEESSEEDSL RRRLLESSLI SLSRYDGAGS REHPIYPDPA
     RLSPAAYYAQ RMIQYLSRRD SIRQRSMRYQ QNRLRSSTSS SSSDNQGPSV EGTDLEFEDF
     EDNGDRSRHR APRNARMSAP SLGRFVPRRF LLPEYLPYAG IFHERGQPGL ATHSSVNRVL
     AGAVIGDGQS AVASNIANTT YRLQWWDFTK FDLPEISNAS VNVLVQNCKI YNDASCDISA
     DGQLLAAFIP SSQRGFPDEG ILAVYSLAPH NLGEMLYTKR FGPNAISVSL SPMGRYVMVG
     LASRRILLHP STEHMVAQVF RLQQAHGGET SMRRVFNVLY PMPADQRRHV SINSARWLPE
     PGLGLAYGTN KGDLVICRPE ALNSGIEYYW DQLSETVFTV HSSSRSSERP GTSRATWRTD
     RDMGLMNAIG LQPRNPTTSV TSQGTQTLAL QLQNAETQTE REEEEPGAAS SGPGEGEGSE
     YGGSGEDALS RIQRLMAEGG MTAVVQREQS TTMASMGGFG NNIIVSHRIH RSSQTGTESG
     AARTSSPQPS TSRGLPSEPG QLAERALSPR TASWDQPSTS GRELPQPALS SSSPVPIPVP
     LASNEGPTMH CNVTNNSHLP EGDGSNRGEA AGPSGEPQNR
//
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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   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   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   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;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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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   -----------------------------------------------------------------------
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   D19L4_MOUSE             Reviewed;         722 AA.
AC   A2AJQ3; B2RW18; Q3T9A8;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 31.
DE   RecName: Full=Protein dpy-19 homolog 4;
DE   AltName: Full=Dpy-19-like protein 4;
GN   Name=Dpy19l4; Synonyms=Gm1023;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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 1-568 (ISOFORM 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).
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=A2AJQ3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AJQ3-2; Sequence=VSP_029632;
CC   -!- SIMILARITY: Belongs to the dpy-19 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL772170; CAM20811.1; -; Genomic_DNA.
DR   EMBL; AL840625; CAM20811.1; JOINED; Genomic_DNA.
DR   EMBL; AL953845; CAM20811.1; JOINED; Genomic_DNA.
DR   EMBL; AL840625; CAM21617.1; -; Genomic_DNA.
DR   EMBL; AL772170; CAM21617.1; JOINED; Genomic_DNA.
DR   EMBL; AL953845; CAM21617.1; JOINED; Genomic_DNA.
DR   EMBL; AL953845; CAM23148.1; -; Genomic_DNA.
DR   EMBL; AL772170; CAM23148.1; JOINED; Genomic_DNA.
DR   EMBL; AL840625; CAM23148.1; JOINED; Genomic_DNA.
DR   EMBL; BC147500; AAI47501.1; -; mRNA.
DR   EMBL; BC157932; AAI57933.1; -; mRNA.
DR   EMBL; BC157988; AAI57989.1; -; mRNA.
DR   EMBL; AK172656; BAE43116.1; -; mRNA.
DR   IPI; IPI00378635; -.
DR   IPI; IPI00404281; -.
DR   RefSeq; NP_001074670.1; NM_001081201.1.
DR   UniGene; Mm.331486; -.
DR   UniGene; Mm.355656; -.
DR   PRIDE; A2AJQ3; -.
DR   Ensembl; ENSMUST00000053522; ENSMUSP00000058639; ENSMUSG00000045205.
DR   Ensembl; ENSMUST00000084892; ENSMUSP00000081954; ENSMUSG00000045205.
DR   GeneID; 381510; -.
DR   KEGG; mmu:381510; -.
DR   CTD; 381510; -.
DR   MGI; MGI:2685869; Dpy19l4.
DR   GeneTree; ENSGT00530000063023; -.
DR   HOGENOM; HBG446819; -.
DR   HOVERGEN; HBG107792; -.
DR   InParanoid; A2AJQ3; -.
DR   OMA; STYTFMM; -.
DR   OrthoDB; EOG4FJ88G; -.
DR   NextBio; 402162; -.
DR   Bgee; A2AJQ3; -.
DR   CleanEx; MM_DPY19L4; -.
DR   Genevestigator; A2AJQ3; -.
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    722       Protein dpy-19 homolog 4.
FT                                /FTId=PRO_0000311882.
FT   TRANSMEM     51     71       Helical; (Potential).
FT   TRANSMEM    160    177       Helical; (Potential).
FT   TRANSMEM    183    201       Helical; (Potential).
FT   TRANSMEM    246    262       Helical; (Potential).
FT   TRANSMEM    268    284       Helical; (Potential).
FT   TRANSMEM    291    307       Helical; (Potential).
FT   TRANSMEM    313    331       Helical; (Potential).
FT   TRANSMEM    351    369       Helical; (Potential).
FT   TRANSMEM    420    440       Helical; (Potential).
FT   TRANSMEM    465    485       Helical; (Potential).
FT   TRANSMEM    487    507       Helical; (Potential).
FT   TRANSMEM    521    541       Helical; (Potential).
FT   VAR_SEQ     290    333       Missing (in isoform 2).
FT                                /FTId=VSP_029632.
SQ   SEQUENCE   722 AA;  83604 MW;  029C334E649396D5 CRC64;
     MAKEEGTSVE PRQRKKQRTS GSQEAKAEKI RRTPAPERAP KYVSFQRFAK IVIGCLAAVI
     SGMMHVFYLS AYHERKFWFS NRQELEREIT FQGDSAIYYS YYKDMLKAPS FERGVYELTH
     NNKTISLKTI NAMQQMSLYP ELIASVLYQA TGSNEVIEPV YFYIGIVFGL QGMYVTALFV
     TSWLMSGTWL AGMLTVAWFL INRVDTTRIE YSIPLRENWA LPYFACQVAA LTGYLKRNLN
     TYAERFCYLL LSTSTYTFMM VWEYSHYVLF LQAVSLLLLD IFSVEQSDKV YEVYKVYIFS
     LFLGYLLQFE NPALLVSPLL SLVGAFMLVK CLQLNGKKGT FVAKVIKVFE FYLLCTLPVT
     LNLIVKMFVP HKENEHVLKF LEVKFGLNMT KNFTLNWLLC QESLQAPSQD FFFRLTQSSL
     LPFYVLVLII CLLSMTQVFF RRMSGKSKKE TVTLEDGRIG ERPEIIYHVI HTLLLGSLAM
     LMEGLKFIWT PYVCMLAAFG VCSPELWMTL LKWLRLRTVH PMLLALILSM AVPTIIGLSL
     WKEFFPRLIT ELTELQEFYD PDTVELMTWI KRQAPVAAVF AGSPQLMGVI KLCTGWTVTS
     LPLYSDDDLL QRNENIYQIY SKRSAEDIYK ILTSYKANYL IVEDAICNEL GTTRGCRVKD
     LLDIANGHVV FEEGDKLTYS KYGRFCHEVK INYSPYVNYF TRVYWNRSYF VYKVNTVISF
     QS
//
ID   A2AKJ2_MOUSE            Unreviewed;       102 AA.
AC   A2AKJ2;
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=Vimentin;
DE   Flags: Fragment;
GN   Name=Vim; ORFNames=RP23-185P20.1-003;
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   Almeida-King J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL772303; CAM16857.1; -; Genomic_DNA.
DR   IPI; IPI00751833; -.
DR   UniGene; Mm.268000; -.
DR   STRING; A2AKJ2; -.
DR   PRIDE; A2AKJ2; -.
DR   Ensembl; ENSMUST00000028062; ENSMUSP00000028062; ENSMUSG00000026728.
DR   Ensembl; ENSMUST00000141365; ENSMUSP00000114742; ENSMUSG00000026728.
DR   MGI; MGI:98932; Vim.
DR   eggNOG; roNOG09368; -.
DR   GeneTree; ENSGT00560000076592; -.
DR   InParanoid; A2AKJ2; -.
DR   Bgee; A2AKJ2; -.
DR   Genevestigator; A2AKJ2; -.
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; IPR001664; IF.
DR   InterPro; IPR006821; Intermed_filament_DNA-bd.
DR   PANTHER; PTHR23239; IF; 1.
DR   Pfam; PF04732; Filament_head; 1.
PE   4: Predicted;
KW   Coiled coil; Intermediate filament.
FT   NON_TER     102    102
SQ   SEQUENCE   102 AA;  10961 MW;  72C5E2EC6B24780B CRC64;
     MSTRSVSSSS YRRMFGGSGT SSRPSSNRSY VTTSTRTYSL GSALRPSTSR SLYSSSPGGA
     YVTRSSAVRL RSSVPGVRLL QDSVDFSLAD AINTEFKNTR TN
//
ID   A2AL71_MOUSE            Unreviewed;        73 AA.
AC   A2AL71;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-FEB-2011, entry version 27.
DE   SubName: Full=Aspartate-beta-hydroxylase;
DE   Flags: Fragment;
GN   Name=Asph; ORFNames=RP23-152A20.3-015;
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.
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DR   EMBL; AL773548; CAM26682.1; -; Genomic_DNA.
DR   IPI; IPI00649726; -.
DR   UniGene; Mm.222206; -.
DR   UniGene; Mm.412008; -.
DR   STRING; A2AL71; -.
DR   Ensembl; ENSMUST00000131605; ENSMUSP00000118518; ENSMUSG00000028207.
DR   Ensembl; ENSMUST00000146441; ENSMUSP00000116899; ENSMUSG00000028207.
DR   MGI; MGI:1914186; Asph.
DR   eggNOG; roNOG11810; -.
DR   GeneTree; ENSGT00530000063281; -.
DR   Bgee; A2AL71; -.
DR   Genevestigator; A2AL71; -.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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: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   Pfam; PF05279; Asp-B-Hydro_N; 1.
PE   4: Predicted;
FT   NON_TER      73     73
SQ   SEQUENCE   73 AA;  8013 MW;  9EBE899EA6185C12 CRC64;
     MVIALLGVWT SVAVVWFDLV DYEEVLAKAK DFRYNLSEVL QGKLGVYDAD GDGDFDVDDA
     KVLLGLTKDG SNE
//
ID   A2AL83_MOUSE            Unreviewed;       163 AA.
AC   A2AL83;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   11-JAN-2011, entry version 23.
DE   SubName: Full=Aspartate-beta-hydroxylase;
DE   Flags: Fragment;
GN   Name=Asph; ORFNames=RP23-152A20.3-017;
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   Lovell J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Sycamore N.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL732508; CAM19152.1; -; Genomic_DNA.
DR   EMBL; AL773548; CAM19152.1; JOINED; Genomic_DNA.
DR   EMBL; AL773548; CAM26694.1; -; Genomic_DNA.
DR   EMBL; AL732508; CAM26694.1; JOINED; Genomic_DNA.
DR   IPI; IPI00649469; -.
DR   UniGene; Mm.222206; -.
DR   UniGene; Mm.412008; -.
DR   Ensembl; ENSMUST00000084912; ENSMUSP00000081975; ENSMUSG00000028207.
DR   MGI; MGI:1914186; Asph.
DR   HOVERGEN; HBG062244; -.
DR   InParanoid; A2AL83; -.
DR   Bgee; A2AL83; -.
DR   Genevestigator; A2AL83; -.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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: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   Pfam; PF05279; Asp-B-Hydro_N; 1.
PE   4: Predicted;
FT   NON_TER     163    163
SQ   SEQUENCE   163 AA;  16986 MW;  05DEB249CBC08BCB CRC64;
     MAPRKNAKGG GGNSSSSGSG SGSGSGSPST GSSGSSSSPG ARREAKHGGH KNGRRGGISG
     GSFFTWFMVI ALLGVWTSVA VVWFDLVDYE EVLAKAKDFR YNLSEVLQGK LGVYDADGDG
     DFDVDDAKVL LGLKERSPSE RTFPPEEEAE THAELEEQAP EGA
//
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   A2ALS4_MOUSE            Unreviewed;       729 AA.
AC   A2ALS4;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   11-JAN-2011, entry version 28.
DE   SubName: Full=Rap1 GTPase-activating protein;
GN   Name=Rap1gap; ORFNames=RP23-277N22.1-002;
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   Tromans A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL805954; CAM19420.1; -; Genomic_DNA.
DR   IPI; IPI00459745; -.
DR   UniGene; Mm.180763; -.
DR   ProteinModelPortal; A2ALS4; -.
DR   SMR; A2ALS4; 142-478.
DR   STRING; A2ALS4; -.
DR   PRIDE; A2ALS4; -.
DR   Ensembl; ENSMUST00000105835; ENSMUSP00000101461; ENSMUSG00000041351.
DR   MGI; MGI:109338; Rap1gap.
DR   HOGENOM; HBG445308; -.
DR   HOVERGEN; HBG016371; -.
DR   InParanoid; A2ALS4; -.
DR   Bgee; A2ALS4; -.
DR   Genevestigator; A2ALS4; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; 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   729 AA;  81252 MW;  C448A90021F3961C CRC64;
     MSGRKRSFTF GAYGGVDKSF SLRQSVWRSD GQKQSFPQAL NLLLVDSVPS HPASPYPKNT
     DLFEMIEKMQ GSRMDEQRCS FPPPLKTEED YIPYPSVHEV LGREGPFPLI LLPQFGGYWI
     EGTNHEISSL PETEPLQSPT TKVKLECNPT ARIYRKHFLG KEHFNYYSLD TALGHLVFSL
     KYDVIGDQEH LRLLLRTKCR THHDVIPISC LTEFPNVVQM AKLVCEDVNV DRFYPVLYPK
     ASRLIVTFDE HVISNNFKFG VIYQKLGQTS EEELFSTNEE SPAFVEFLEF LGQKVKLQDF
     KGFRGGLDVT HGQTGTESVY CNFRNKEIMF HVSTKLPYTE GDAQQLQRKR HIGNDIVAVV
     FQDENTPFVP DMIASNFLHA YVVVQAEGGG PDGPLYKVSV TARDDVPFFG PPLPDPAVFR
     KGPEFQEFLL TKLINAEYAC YKAEKFAKLE ERTRAALLET LYEELHIHSQ SMMGLGGDDD
     KMENGSGGGG FFESFKRVIR SRSQSMDAMG LSNKKPNTVS TSHSGSFTPN NPDLAKAAGI
     SLIVPGKSPT RKKSGPFGSR RSSAIGIENI QEVQEKRESP PAGQKTPDSG HVSQEPKSEN
     SSTQSSPEMP TTKNRVESAA QRTEVLQGFS RSSSSASSFT SVVEETEGVD GDDTGLHMAG
     RQREHHERGQ LPSEVAPSCP PSQASHGHPT QTSASRGTLR VPRSRSNWKH LSSTHPRWAA
     SCHLISRRD
//
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;
CC   -----------------------------------------------------------------------
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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   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   A2ARP8_MOUSE            Unreviewed;      3014 AA.
AC   A2ARP8;
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=Microtubule-associated protein 1 A;
GN   Name=Mtap1a; ORFNames=RP23-433P19.1-001;
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 (APR-2008) 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; AL845466; CAM24227.1; -; Genomic_DNA.
DR   EMBL; AL929059; CAM24227.1; JOINED; Genomic_DNA.
DR   EMBL; AL929059; CAM24375.1; -; Genomic_DNA.
DR   EMBL; AL845466; CAM24375.1; JOINED; Genomic_DNA.
DR   IPI; IPI00676243; -.
DR   RefSeq; NP_115769.1; NM_032393.2.
DR   UniGene; Mm.36501; -.
DR   STRING; A2ARP8; -.
DR   PRIDE; A2ARP8; -.
DR   Ensembl; ENSMUST00000094639; ENSMUSP00000092223; ENSMUSG00000027254.
DR   GeneID; 17754; -.
DR   KEGG; mmu:17754; -.
DR   CTD; 17754; -.
DR   MGI; MGI:1306776; Mtap1a.
DR   HOGENOM; HBG282794; -.
DR   HOVERGEN; HBG052408; -.
DR   InParanoid; A2ARP8; -.
DR   OMA; DERSFQY; -.
DR   NextBio; 292423; -.
DR   Bgee; A2ARP8; -.
DR   Genevestigator; A2ARP8; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; IDA:MGI.
PE   4: Predicted;
SQ   SEQUENCE   3014 AA;  325886 MW;  B3E61AC287B5AF18 CRC64;
     MATEAGTARP GSVAMETTPE LGLQSLGAPP AQNPAEPLCE AGAAVAAARW DLRKYSLLIV
     IGDIGTESQL RAVRAHLEQG ILSWNIDLSS FDLNQQLRLF ITRHLAHFSS EVKGQRTLCH
     QSETLETIIL VNPTADSISS EVHHLLSSPS AHKLLILSGQ TLEPEGDLIL QSGTYSYQNF
     AQVLHKPEIA QLLSNRDPGI QAFLTVSCLG EGDWSHLGLS SSQETLHLRL NPEPVLPTMD
     GVAEFSEYVS ETVDVPSPFD LLEPPTSGGF LKLSKPCCYI FPGGRGDSAL FAVNGFNILV
     DGGSDRKSCF WKLVRHLDRI DSVLLTHIGA DNLPGINGLL QRKVAELEEE QSQGSSSYSD
     WVKNLISPEL GVVFFNVPDK LRLPDASRKA KRSIEEACLT LQHLNRLGIQ AEPLYRVVSN
     TIEPLTLFHK MGVGRLDMYV LNPVKDSKEM QFLMQKWAGN SKAKTGIVLA NGKEAEISVP
     YLTSITALVV WLPANPTEKI VRVLFPGNAP QNKILEGLEK LRHLDFLRYP VATQKDLAAG
     AVPANLKPSK IKHRADSKES LKAAPKTAMS KLAKREEVLE EGAKEARSEL AKELAKSEKK
     AKEPSEKPPE KPSKPERVRT ESSEALKAEK RKLIKDKVGK KHLKEKISKL EEKRDKEKKE
     IKKERKELKK EEGRKEEKKD AKKDEKRKDT KPELKKFSKP DLKPFTPEVR KTLYKAKAPG
     RLKVDKGRAA RGEKELSSEP RTPPAQKGAA PPPAASGHRE LALSSPEDLT QDFEELKREE
     RGLLAEPRDT ELGEKPLPAD ASEQGRPSTA IQVTQPPASV LEQEQVEREK EVVPDFPEDK
     GSKNRAPDSG AEVEREKETW EERKPREAEL TPENIAAARE ESEPEVKEDV IEKAELEEME
     EVHPSDEEEE ETKAESFYQK HMQEALKVIP KGREALGGRE LGFQGKAPEK ETASFLSSLA
     TPAGAAEHVS YIQDETIPGY SETEQTISDE EIHDEPDERP APPRFPTSTY DLSGPEGPGP
     FEASQSAESA VPASSSKTYG APETELTYPP NMVAAPLAEE EHVSSATSIT ECDKLSSFAT
     SVAEDQSVAS LTAPQTEETG KSSLLLDTVT SIPSSRTEAT QGLDYVPSAG TISPTSSLEE
     DKGFKSPPCE DFSVTGESEK KGESVGRGLT GEKAVGKEEK NVTTSEKLSS QYAAVFGAPG
     HALHPGEPAL GEVEERCLSP DDSTVKMASP PPSGPPSAAH TPFHQSPVEE KSEPQDFQED
     SWGDTKHAPG VSKEDAEEQT VKPGPEEAMS EEGKVPLSRS PQAQDTLGSL AGGQTGCTIQ
     LLPEQDKAVV FETGEAGAAS GAGSLPGEVR TQEPAEPQKD ELLGFTDQSF SPEDAESLSV
     LSVVSPDTAK QEATPRSPCT PKEQQLHKDL WPMVSPEDTQ SLSFSEESPS KETSLDISSK
     QLSPESLGTL QFGELSLGKE EKGPLVKAED NSCHLAPVSI PEPHTATVSP PTDEAAGEAG
     LTDESPAGNL PGSSFSHSAL SGDRKHSPGE ITGPGGHFMT SDSSLTKSPE SLSSPAMEDL
     AMEWGGKAPG SEDRATEQKE KELERKSETL QQKDQILSEK AALVQRDSVM HQKDEALDEE
     NKPGGQQDKT SEQKGRDLDK KDTAVELGKG PEPKGKDLYL EDQGLAEKDK ALEQRGAALQ
     QTQAPEPRAR AQEHRDLEQK DEHLELRDKT PEEKDKVLVL EDRAPEHIIP QPTQTDRAPE
     HRSKVDKEQK DEASEEKEQV LEQKDWAREK EGAALDQDNR AAGQKDGTLK EDKTQGQKSS
     FLEDKSTTPK EMTLDQKSPE KAKGVEQQDG AVPEKTRALG LEESPEEEGK AREQEEKYWK
     EQDVVQGWRE TSPTRGEPVP AWEGKSPEQE VRYWRDRDIT LQQDAYWKEL SCERKVWFPH
     ELDGQGARPR YSEERESTFL DEGPNEQEIT PLQHTPRSPW ASDFKDFQEP LPQKGLEVER
     WLAESPVGLP PEEEDKLTRS PFEIISPPAS PPEMTGQRVP SAPGQESPVP DTKSTPPTRN
     EPTTPSWLAE IPPWVPKDRP LPPAPLSPAP APPTPAPDPH APAPFSWGIA EYDSVVAAVQ
     EGAAELEGGP YSPLGKDYRK AEGEREGEGG AGAPDSSSFS SKVPEVTESH TTRDAEQTEP
     EQREPTPYPD ERSFQYADIY EQMMLTGLGP ACPTREPPLG ASGDWPPHLS TKEEAAGRNK
     SAEKELSSAV SPPNLHSDTP TFSYASLAGP TIPPRQEPEP GPNVEPSFTP PAVPPRAPIS
     LSQDPSPPLN GSTTSCGPDR RTPSPKEAGR SHWDDGTNDS DLEKGAREQP EKETQSPSPH
     HPMPVGHPSL WPETEAHSSL SSDSHLGPVR PSLDFPASAF GFSSLQPAPP QLPSPAEPRS
     APCGSLAFSG DRALALVPGT PTRTRHDEYL EVTKAPSLDS SLPQLPSPSS PGAPLLSNLP
     RPASPALSEG SSSEATTPVI SSVAERFPPG LEVAEQSSGE LGPGNEPAAH SLWDLTPLSP
     APLASRDLAP APAPAPAPSL PGNLGDGTLS CRPECSGELT KKPSPFLSHS GDHEANGPGE
     TSLNPPGFAT ATAEKEEAEA LHAWERGSWP EGAERSSRPD TLLSSEQRPG KSSGGPPCSL
     SSEVEAGPQG CATDPRPHCG ELSPSFLNPP LPPSTDDSDL STEEARLAGK GGRRRAGRPG
     ATGGPCPMAD ETPPTSASDS GSSQSDSDVP PETEECPSIT AEAALDSDED GDFLPVDKAG
     GVSGTHHPRP GHDPPPAPLP DPRPPPPRPD VCMADPEGLS SESGRVERLR EKVQGRPGRK
     APGRAKPASP ARRLDIRGKR SPTPGKGPVD RTSRALPRPR STPSQVTSEE KDGHSPMSKG
     LVNGLKAGST ALGSKGSSGP PVYVDLAYIP NHCSGKTADQ DFFRRVRASY YVVSGNDPAN
     GEPSRAVLDA LLEGKAQWGE NLQVTLIPTH DTEVTREWYQ QTHEQQQQLN VLVLASSSTV
     VMQDESFPAC KIEF
//
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   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   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   A2AUE0_MOUSE            Unreviewed;       160 AA.
AC   A2AUE0;
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=Tumor protein D52-like 2;
DE   Flags: Fragment;
GN   Name=Tpd52l2; ORFNames=RP23-33L3.2-010;
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   Almeida-King J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL929094; CAM21504.1; -; Genomic_DNA.
DR   IPI; IPI00750947; -.
DR   UniGene; Mm.136648; -.
DR   Ensembl; ENSMUST00000108801; ENSMUSP00000104429; ENSMUSG00000000827.
DR   Ensembl; ENSMUST00000141825; ENSMUSP00000123627; ENSMUSG00000000827.
DR   MGI; MGI:1913564; Tpd52l2.
DR   GeneTree; ENSGT00390000015988; -.
DR   HOVERGEN; HBG058643; -.
DR   Bgee; A2AUE0; -.
DR   Genevestigator; A2AUE0; -.
DR   InterPro; IPR007327; TPD52.
DR   PANTHER; PTHR19307; TPD52; 1.
DR   Pfam; PF04201; TPD52; 1.
PE   4: Predicted;
FT   NON_TER       1      1
FT   NON_TER     160    160
SQ   SEQUENCE   160 AA;  17619 MW;  4E3F610F31130077 CRC64;
     INLNSPNKGV LSDFMTDVPV DPGVVHRTPV VEGLTEGEEE ELRAELAKVE EEIVTLRQVL
     AAKERHCGEL KRRLGLSTLG ELKQNLSRSW HDVQVSTAYK KTQETLSQAG QKTSAALSTM
     GSAISRKLGD MRAHPLSQSF SSYSIRHSIS MPVMRNSATF
//
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   A2BIE1_MOUSE            Unreviewed;      1698 AA.
AC   A2BIE1;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 2.
DT   08-MAR-2011, entry version 30.
DE   SubName: Full=Glutamine and serine rich 1;
GN   Name=Qser1; ORFNames=RP24-297H17.9-001;
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; BX908741; CAM16964.2; -; Genomic_DNA.
DR   IPI; IPI00808125; -.
DR   RefSeq; NP_001116799.1; NM_001123327.1.
DR   UniGene; Mm.274314; -.
DR   PRIDE; A2BIE1; -.
DR   Ensembl; ENSMUST00000117237; ENSMUSP00000114062; ENSMUSG00000074994.
DR   GeneID; 99003; -.
DR   KEGG; mmu:99003; -.
DR   CTD; 99003; -.
DR   MGI; MGI:2138986; Qser1.
DR   eggNOG; roNOG16206; -.
DR   HOGENOM; HBG444812; -.
DR   HOVERGEN; HBG089439; -.
DR   InParanoid; A2BIE1; -.
DR   OrthoDB; EOG4NGGM0; -.
DR   NextBio; 353745; -.
DR   Bgee; A2BIE1; -.
DR   Genevestigator; A2BIE1; -.
PE   4: Predicted;
SQ   SEQUENCE   1698 AA;  185380 MW;  456A11EDA6CDDFF5 CRC64;
     MHSSAATELF VAGPLPTTGT LPPPTLSAYQ HSSTFSNRNF ATTSPLVLQD SSFNTTSNGI
     LSPHDPLLQI KTSQGTVPTA LAFERLGSSA LSNSVPPQSS TYRSAQESAP HLLQPQFSLL
     PSTLGGAQQT PQAYNSALFP SSAASIERAL LRECSVIKHH QRPSVTQSIQ AQLTGSQHPL
     HSYLSSASIG NFQEPSRQSS LSCSSVRDST QVSNGVLPQK TPQVSAELAQ SYSSVIPSSG
     YLPSATKVDS CSTKQPLTST TIPKPQSVIP PVQTLNYSKP LHNQSSVISG QAQIYSTAQL
     PSLLSVSQSQ NYGLVQPHNV PSIVHSQVYR SSRVEKLPSL YKTLTFSGSS QPVTSENQTL
     SYSSNQQEVL SLVTNENYPA QTRDLPSVSE SQNYSSGQSQ GLSPVSQTQV SYSSQSQVLS
     VVSPSESYAS GQSLTLTAPS LSYSSASRGQ SLPVSTPTPS YTSMHPSPNA QTQGSSAQPQ
     EFLPAVQSSF ASSTRGQTLQ SSIPSPDPKS YAERKLDSSV YTSSKQDEFP VQKLQALQSQ
     ASLESSSQRL PDGEVNAQES VYKTSKADDR YSQSVTRNNS HLEDQVVGVA LQGSEQEENM
     VGSMTQLNQQ SGQSNNAVAT DLKKATNLMQ TPQVRLNTKD LNQQHSLMHK MHEAKVQQQH
     DQIMSASSQI QIPNPALGQS HQALPHTSVL LDSACDLQIL QQAGILQASL GQAKASLQVQ
     RVQSPQQIVH PFLQMDGHII QSNGEHPQQQ LHPHNSDIMK LDLPEPSKPL QQLTTKGPFS
     EANPHDSKNQ FVSLGSICFS EAMLLSDERN ILSNVDDILA ATAAACGVTP SDFSKSAANE
     TMQDIESSDS KSHYQQSLNV RHVNSDFNSI AASVGKPQSI NDISLNGNQV SVSLSSVPTL
     QSETVLDQPH METPSQTIPT KVPSAMVGLG QEIQEQSSDP FKKQLTINHE SKEDREIAVD
     SALSNNRNQE FVSNSRSISG DSVVSERDFT LVGDDTGVLV NPRRSTLALL AMPQPGDAAS
     GKTEDEKQDV TYFNLPKEKA KGKEQGKEEE DNQKQLKRSA QCKRQNPRGT DVYVPYTSPS
     LESCDEGFQH QEKMRQKIKE VEEKQPEVKT GFIASFLDFL KCGPKQQFST LAVRVPNRTR
     RSGIQTTRTF CPPPFAKTSP AAQAPSETGG VSLSEKVDSE LKTLEQLSSF SSDEEDPGSC
     GHDIYKNTSA PLTVLDATSD KTKKTVLEAL PVATPGASAE TAGVAPTAST AVATIKQDLH
     LTSLTVNTME NANSTESPTA IELDSLPSDQ LAKGQDTVAI EGFTDEENIE SGGEGQYRER
     DEFVVKIEDI ETFKEALNTG KEPPAIWKVQ KALLQKFVPE IRDGQREFAA TNSYLGYFGD
     AKTKYKRIYV KFIENANKKE YVRVCSKKPR NKPSQTIRNI PSKPSSISKT SDPPVSKTTT
     TKTPSTKPKA KQLKIKAEPP PKKRKKWKEE FSSSQSESSP EVRSSSSEDE GFEPPAPSVT
     RFLNTRAMKE TFKSYMELLV SIALDPDTMQ ALEKSNDELL LPHMKKIDGM LNDNRKRLLV
     NLHLDQPFKN ALESFPELTV ITRDSKAKSG GSAISKIKMN GKAYNKKTLR TSKTTTKSAQ
     EFAVDPEKIQ LYSLYHSLHH YKYHVYLICK NEISSVQKKN EDLGQEEIVQ LCMKNVKWVE
     DLFEKFGELL NHVQQKCS
//
ID   K1310_MOUSE             Reviewed;         903 AA.
AC   A2RSY1; Q6ZPU0; Q8C0P9;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   08-MAR-2011, entry version 27.
DE   RecName: Full=Uncharacterized protein KIAA1310;
GN   Name=Kiaa1310;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; 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 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=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, 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=A2RSY1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2RSY1-2; Sequence=VSP_025335;
CC       Name=3;
CC         IsoId=A2RSY1-3; Sequence=VSP_025334, VSP_025335;
CC         Note=No experimental confirmation available;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98139.1; Type=Erroneous initiation;
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DR   EMBL; AK129329; BAC98139.1; ALT_INIT; mRNA.
DR   EMBL; AK030079; BAC26771.1; -; mRNA.
DR   EMBL; BC132293; AAI32294.1; -; mRNA.
DR   IPI; IPI00223902; -.
DR   IPI; IPI00845576; -.
DR   IPI; IPI00845845; -.
DR   RefSeq; NP_766240.1; NM_172652.3.
DR   UniGene; Mm.24734; -.
DR   ProteinModelPortal; A2RSY1; -.
DR   PhosphoSite; A2RSY1; -.
DR   PRIDE; A2RSY1; -.
DR   Ensembl; ENSMUST00000010597; ENSMUSP00000010597; ENSMUSG00000010453.
DR   Ensembl; ENSMUST00000115018; ENSMUSP00000110670; ENSMUSG00000010453.
DR   GeneID; 226976; -.
DR   KEGG; mmu:226976; -.
DR   MGI; MGI:1918055; 4632411B12Rik.
DR   eggNOG; roNOG06399; -.
DR   GeneTree; ENSGT00390000007636; -.
DR   HOGENOM; HBG506321; -.
DR   HOVERGEN; HBG062095; -.
DR   InParanoid; A2RSY1; -.
DR   OMA; PVPLYDN; -.
DR   OrthoDB; EOG4Z0B53; -.
DR   Bgee; A2RSY1; -.
DR   CleanEx; MM_4632411B12RIK; -.
DR   Genevestigator; A2RSY1; -.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    903       Uncharacterized protein KIAA1310.
FT                                /FTId=PRO_0000287138.
FT   COMPBIAS    699    772       Ser-rich.
FT   MOD_RES     523    523       Phosphoserine (By similarity).
FT   MOD_RES     535    535       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     540    540       Phosphoserine (By similarity).
FT   MOD_RES     772    772       Phosphoserine (By similarity).
FT   VAR_SEQ       1     99       Missing (in isoform 3).
FT                                /FTId=VSP_025334.
FT   VAR_SEQ     581    606       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_025335.
SQ   SEQUENCE   903 AA;  96135 MW;  68D32C689768DB7D CRC64;
     MAHRGGERDF QTSARRMGTS LLFQLSVHER ELDLVFLDHS YAKPWSAHPD ASSARPTRML
     FVTPRRQQEN TIESDVPIDV ETVTATPVPL YDNQKARSVM NECERHVIFA RTDADAPPPP
     EDWEEHVNRT GWTVAQNKLF NKILKALQSD RLARLANEGA CNEPVLRRVA VDKCARRVRQ
     ALASVSWDTK LTQWLHTTLV ETLSLPMLAA YLDALQTLKG KIPTLIDRML VSSNTKTGAA
     GAEALSLLLK RPWDPAVGVL SHNKPSKLPG SPLILIVSSG PSSSVFPASR RHRFWQSQLS
     CLGKVIPVAT HLLNNGSGVG VLQCLEHMIG AVRSKVLEIH SHFPHKPIIL IGWNTGALVA
     CHVSVMEYVT AVVCLGFPLL TVDGPRGDVD DPLLDMKTPV LFVIGQNSLQ CHPEAMEDFR
     EKIRAENSLV VVGGADDNLR ISKAKKKSEG LTQSMVDRCI QDEIVDFLTG VLTRAEGHVG
     SEPRDQDAEK KKKPRDLTRR DLAFEIPERG SRPASPAARL PTSPSGSEDL SSVSSSPTSS
     PKTKVTTVTS TQKSSQIGTS QLLKRHVQRT EAVLTHRQAQ AQFAAFLKQN MLVRKAFPPG
     TSSCLFVPIS SESVEDIEKE ELRVQLKRHH SSSPLPGAKP SKRPKIKVSL ISQGDTVGGP
     CTLSQGGTPE AAGGKPITMT LGASAGAKEL TGLLTTAKSS SSEGGGTAST TPSVASSSAT
     PNAIHTLQSR LVATSPGSSL PGTASASSLL QGLSFSLQDI SSKTSGLPGS PSPGPAPQAT
     SVKLPTPMQS LGAITTGTST IVRTIPVATT LSSLGATPGG KPTAIHQLLT NGSLAKLASS
     LPGLAQISNQ ASGLKVPTTI TLTLRGQPSR ITTLSPMGSG ATPSEEPNSQ MLPSSSQRLP
     PAP
//
ID   A2VCP3_MOUSE            Unreviewed;       597 AA.
AC   A2VCP3;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   08-MAR-2011, entry version 32.
DE   RecName: Full=P2X purinoceptor;
DE   Flags: Fragment;
GN   Name=P2rx7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; 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   -!- SUBUNIT: Homo- or heteropolymers (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the P2X receptor family.
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DR   EMBL; BC128303; AAI28304.1; -; mRNA.
DR   EMBL; BC128304; AAI28305.1; -; mRNA.
DR   IPI; IPI00720080; -.
DR   UniGene; Mm.42026; -.
DR   STRING; A2VCP3; -.
DR   Ensembl; ENSMUST00000100737; ENSMUSP00000098303; ENSMUSG00000029468.
DR   MGI; MGI:1339957; P2rx7.
DR   eggNOG; roNOG09808; -.
DR   HOGENOM; HBG713324; -.
DR   HOVERGEN; HBG053086; -.
DR   InParanoid; A2VCP3; -.
DR   Bgee; A2VCP3; -.
DR   Genevestigator; A2VCP3; -.
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:0005887; C:integral to plasma membrane; IMP:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IMP:MGI.
DR   GO; GO:0004931; F:extracellular ATP-gated cation channel activity; IMP:MGI.
DR   GO; GO:0001530; F:lipopolysaccharide binding; IDA:MGI.
DR   GO; GO:0000187; P:activation of MAPK activity; IMP:MGI.
DR   GO; GO:0032060; P:bleb assembly; IMP:MGI.
DR   GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR   GO; GO:0006884; P:cell volume homeostasis; IDA:MGI.
DR   GO; GO:0031668; P:cellular response to extracellular stimulus; IMP:MGI.
DR   GO; GO:0046513; P:ceramide biosynthetic process; IDA:MGI.
DR   GO; GO:0032963; P:collagen metabolic process; IMP:MGI.
DR   GO; GO:0019835; P:cytolysis; IDA:MGI.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
DR   GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
DR   GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR   GO; GO:0006900; P:membrane budding; IMP:MGI.
DR   GO; GO:0006509; P:membrane protein ectodomain proteolysis; IMP:MGI.
DR   GO; GO:0007005; P:mitochondrion organization; IDA:MGI.
DR   GO; GO:0044254; P:multicellular organismal protein catabolic process; IDA:MGI.
DR   GO; GO:0043132; P:NAD transport; IMP:MGI.
DR   GO; GO:0045779; P:negative regulation of bone resorption; IMP:MGI.
DR   GO; GO:0043409; P:negative regulation of MAPKKK cascade; IDA:MGI.
DR   GO; GO:0006800; ?:oxygen and reactive oxygen species metabolic process; IMP:MGI.
DR   GO; GO:0001845; P:phagolysosome assembly; IMP:MGI.
DR   GO; GO:0006649; P:phospholipid transfer to membrane; IMP:MGI.
DR   GO; GO:0045332; P:phospholipid translocation; IDA:MGI.
DR   GO; GO:0007009; P:plasma membrane organization; IDA:MGI.
DR   GO; GO:0046931; P:pore complex assembly; IMP:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptosis; IMP:MGI.
DR   GO; GO:0030501; P:positive regulation of bone mineralization; IMP:MGI.
DR   GO; GO:0014054; P:positive regulation of gamma-aminobutyric acid secretion; IMP:MGI.
DR   GO; GO:0014049; P:positive regulation of glutamate secretion; IMP:MGI.
DR   GO; GO:0050717; P:positive regulation of interleukin-1 alpha secretion; IMP:MGI.
DR   GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IMP:MGI.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:MGI.
DR   GO; GO:0043410; P:positive regulation of MAPKKK cascade; IMP:MGI.
DR   GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IMP:MGI.
DR   GO; GO:0032308; P:positive regulation of prostaglandin secretion; IMP:MGI.
DR   GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IMP:MGI.
DR   GO; GO:0051259; P:protein oligomerization; IDA:MGI.
DR   GO; GO:0016485; P:protein processing; IMP:MGI.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:MGI.
DR   GO; GO:0033198; P:response to ATP; IDA:MGI.
DR   GO; GO:0051592; P:response to calcium ion; IDA:MGI.
DR   GO; GO:0042493; P:response to drug; IMP:MGI.
DR   GO; GO:0051602; P:response to electrical stimulus; IMP:MGI.
DR   GO; GO:0034405; P:response to fluid shear stress; IMP:MGI.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IDA:MGI.
DR   GO; GO:0009612; P:response to mechanical stimulus; IMP:MGI.
DR   GO; GO:0014070; P:response to organic cyclic compound; IDA:MGI.
DR   GO; GO:0051789; P:response to protein stimulus; IDA:MGI.
DR   GO; GO:0010043; P:response to zinc ion; IMP:MGI.
DR   GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR   GO; GO:0016079; P:synaptic vesicle exocytosis; IMP:MGI.
DR   GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
DR   GO; GO:0042098; P:T cell proliferation; IMP:MGI.
DR   InterPro; IPR003050; P2X7_purnocptor.
DR   InterPro; IPR001429; P2X_purnocptor.
DR   PANTHER; PTHR10125; ATP_P2X_rcpt; 1.
DR   Pfam; PF00864; P2X_receptor; 1.
DR   PRINTS; PR01314; P2X7RECEPTOR.
DR   PRINTS; PR01307; P2XRECEPTOR.
DR   TIGRFAMs; TIGR00863; P2X; 1.
DR   PROSITE; PS01212; P2X_RECEPTOR; 1.
PE   2: Evidence at transcript level;
KW   Ion transport; Ionic channel; Membrane; Receptor; Transmembrane;
KW   Transport.
FT   NON_TER       1      1
SQ   SEQUENCE   597 AA;  68573 MW;  79C866C8B2EF8457 CRC64;
     GLCRACCSWN DVLQYETNKV TRIQSTNYGT VKWVLHMIVF SYISFALVSD KLYQRKEPVI
     SSVHTKVKGI AEVTENVTEG GVTKLGHSIF DTADYTFPLQ GNSFFVMTNY VKSEGQVQTL
     CPEYPRRGAQ CSSDRRCKKG WMDPQSKGIQ TGRCVPYDKT RKTCEVSAWC PTEEEKEAPR
     PALLRSAENF TVLIKNNIHF PGHNYTTRNI LPTMNGSCTF HKTWDPQCSI FRLGDIFQEA
     GENFTEVAVQ GGIMGIEIYW DCNLDSWSHH CRPRYSFRRL DDKNTDESFV PGYNFRYAKY
     YKENNVEKRT LIKAFGIRFD ILVFGTGGKF DIIQLVVYIG STLSYFGLAT VCIDLLINTY
     SSAFCRSGVY PYCKCCEPCT VNEYYYRKKC ESIMEPKPTL KYVSFVDEPH IRMVDQQLLG
     KSLQVVKGQE VPRPQMDFSD LSRLSLSLHD SPPTPGQSEE IQLLHEEVAP KSGDSPSWCQ
     CGNCLPSRLP EQRRALEELC CRRKPGRCIT TSKLFHKLVL SRDTLQLLLL YQDPLLVLGE
     EATNSRLRHR AYRCYATWRF GSQDMADFAI LPSCCRWRIR KEFPKTEGQY SGFKYPY
//
ID   A2VCS7_MOUSE            Unreviewed;      1261 AA.
AC   A2VCS7;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   05-OCT-2010, entry version 16.
DE   SubName: Full=Armcx4 protein;
DE   Flags: Fragment;
GN   Name=Armcx4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; 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; BC128507; AAI28508.1; -; mRNA.
DR   IPI; IPI00756611; -.
DR   UniGene; Mm.31961; -.
DR   UniGene; Mm.391318; -.
DR   PRIDE; A2VCS7; -.
DR   Genevestigator; A2VCS7; -.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
FT   NON_TER    1261   1261
SQ   SEQUENCE   1261 AA;  128482 MW;  41A7970ACD9C4969 CRC64;
     AGREAETRVK TEPETGEGGE PVAEVDSKVP VLVRSSGNCQ AKTMLEEEIE TQSETSSLVE
     TMVMTEAVTL TESTSQAKEV TMKEAVTQTD AEAEAVGKKE AVTQTKAKAW AMAGRAEVKK
     EAMTQTKAEA RTLAEKETEI NRVTVTQSEV LAVTKEVVKI GTMNETGVVA EAMIRPLEET
     VSVTRTQSEA RLDAAVDTKE NLNDMSVVVT GVDTKSCAQS QAVAIIQNDD MAGAEADKED
     LKNMSKAGSG IDMKVPGQPH IAANNLAEAV PGAKNDAWDN AKDICEAEAD IRTCLIQSET
     VAKIETEATS SATMDGGKDA NAKAMTDVNV TDTQPQAVTS DQTEAMPDAK VKGKGNASAM
     AKAGAKANTK TSSQTDALPD AGDKNRSDNN VTAKAETGID MVSCTQTEPV AKDNANTTSK
     EGAQATGQSQ GEALPNTKGK ARGKAKAKCK AAAGTDTKTC AQPQAGTKTQ AEALSDSKVD
     SKSDSNGVSK AGAKADQKAS GQPQPVANCQ NEALPGTKNK VKGNPNPTPK TEAGTATTSS
     AQTNVTSSQG ETTPGAKNKA KGNRNSVPKA GAGPDTTGSA QSQTVANSHS EALPGAKNKV
     KSNSNVVPKA EAGVGACPQS VPASQGTALT GTKTKVKGNS SAVSKPDAGA GTMGSAHAKT
     AANSQGETLP GSKNKVKGNS NAVPKAEAGA GTTEPNQPQA EALLGARNKV KGNSNSVPKA
     ESGASTILAL ASSQAEALLG ARNKVRGSSN AAPKAEAGVG ARGSAQSQAV VSSQNEALLG
     ARNKIRSNAG TKSGARTGTR GSAQPQAVVS SQNEALLGAR DKGLSSSQVE ATGDNRVYAK
     PMVGAVPASE MVTVAGAQPN VHDYYWNGIG VEDWIAAERW IKFRFQTIDG DWENSVSWTE
     DESGATIGPW TGAANDKAGL VSSWAVACDE SSIKSWTGAR PENEVALGSW VSAGDQATGA
     IWAGAQTTDG TWVADKASAG SWTGAENQIS AGSWVVSGNQ AIAGPWAVSQ VTDGSWPAVQ
     ASGVSWVVDQ ATGTWTVAEN QTGAVSWAGA GNIVSIGYWT GAVDQTNAVS WTGTTDQVGV
     EVKPRFEDQA SEKGSWVVAG VQTSGETRLG SEDQSSGRSW TETVDQANAA SRLGTVDQAG
     GTSWAGTGDQ VGGVSTSGSA DQSSSGSWAG TRNLAGERSW TGTGDQSDGA AKPGFENQTS
     DEGSWAGTIG QPSGGSKSVS EAQSAGRSWA DSADQLSGGF LVGPLDQANG ESQPVSGELA
     A
//
ID   A3KMM1_MOUSE            Unreviewed;       342 AA.
AC   A3KMM1;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAR-2011, entry version 22.
DE   SubName: Full=6430704M03Rik protein;
DE   Flags: Fragment;
GN   Name=6430704M03Rik;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; 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; BC132345; AAI32346.1; -; mRNA.
DR   IPI; IPI00227260; -.
DR   RefSeq; NP_001136437.1; NM_001142965.1.
DR   UniGene; Mm.207654; -.
DR   Ensembl; ENSMUST00000053681; ENSMUSP00000052507; ENSMUSG00000045589.
DR   GeneID; 230235; -.
DR   KEGG; mmu:230235; -.
DR   MGI; MGI:2442704; 6430704M03Rik.
DR   eggNOG; roNOG04805; -.
DR   HOGENOM; HBG716023; -.
DR   HOVERGEN; HBG080407; -.
DR   InParanoid; A3KMM1; -.
DR   OrthoDB; EOG4640CQ; -.
DR   Bgee; A3KMM1; -.
DR   Genevestigator; A3KMM1; -.
DR   GO; GO:0004500; F:dopamine beta-monooxygenase activity; IEA:InterPro.
DR   GO; GO:0006548; P:histidine catabolic process; IEA:InterPro.
DR   InterPro; IPR005018; DOMON_domain.
DR   Pfam; PF03351; DOMON; 1.
DR   SMART; SM00664; DoH; 1.
DR   PROSITE; PS50836; DOMON; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   342 AA;  37376 MW;  86D7C0937566EC51 CRC64;
     EDAQSEAGRR RVRALRGCAA RAGGGSVPAR ARGVPAAAGA AWLRDPCAAM AGQPLRRPAW
     VPLLLRLLLA GIAACDASPA DDSAGPGGRG PRGRARGDAG ADEAVPRHDS SYGTFASEFY
     DLRYLSEEGY PFPTAPPVDP FAKIKVEDCG RTKGCFRYGK PGCNAETCDY FLSYRMIGAD
     VEFELSADTD GWVAVGFSSD KKMGGDDVMA CVHDDNGRVR IQHFYNVGQW AKEVQRNPAR
     DEEGVFENNR VTCRFKRPVN VPRDETIVDL HLSWYYLFAW GPAIQGAITR HDIDSPPASE
     RVVSIYKYED IFMPSAAYQT FSSPFCLLLI VALTFYLLMG TP
//
ID   A6BLZ0_MOUSE            Unreviewed;      1424 AA.
AC   A6BLZ0;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   08-MAR-2011, entry version 35.
DE   SubName: Full=Apoptosis-associated tyrosine kinase 3;
GN   Name=Lmtk3; Synonyms=aatyk3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; 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   Tomomura M., Morita N., Yoshikawa F., Furuichi T., Kamiguchi H.;
RT   "The members of apoptosis-associated tyrosine kinase (AATYK) family.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family.
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DR   EMBL; AB288873; BAF64834.1; -; mRNA.
DR   IPI; IPI00881155; -.
DR   UniGene; Mm.44928; -.
DR   ProteinModelPortal; A6BLZ0; -.
DR   SMR; A6BLZ0; 126-411.
DR   Ensembl; ENSMUST00000072580; ENSMUSP00000072388; ENSMUSG00000062044.
DR   Ensembl; ENSMUST00000118564; ENSMUSP00000113323; ENSMUSG00000062044.
DR   Ensembl; ENSMUST00000120005; ENSMUSP00000112592; ENSMUSG00000062044.
DR   MGI; MGI:3039582; Lmtk3.
DR   HOVERGEN; HBG081921; -.
DR   InParanoid; A6BLZ0; -.
DR   Bgee; A6BLZ0; -.
DR   Genevestigator; A6BLZ0; -.
DR   GO; GO:0005524; F:ATP binding; 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   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Transferase;
KW   Tyrosine-protein kinase.
SQ   SEQUENCE   1424 AA;  150861 MW;  8C282F43E0398094 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 GHPALGCPHP PEDDSSLRAE RGSLADLPLV
     PPTSAPLEFL DPLMGAAAPQ YPGRGPPPAP PPPPPPPRAS AEPAASPDPP SALASPGSGL
     SSPGPKPGDS GYETETPFSP EGAFPGGGAA EEEGVPRPRA PPEPPDPGAP RPPPDPGPLP
     LPGSQEKPTF VVQVSTEQLL MSLREDVTKN LLGDKGSTPG ETGPRKAGRS PANREKGPGP
     NRDLTSLVSR KKVPSRSLPV NGVTVLENGK PGVPDMKEKV EENGLESPER 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
     AAGSRGPGRT REAPVPVVVS SADGDTARPL RGLLKSPRAA DEPEDSELER KRKMVSFHGD
     VTVYLFDQET PTNELSVQGT PEGDTEPSTP PAPPTPPHPT TPGDGFPNND SGFGGSFEWA
     EDFPLLPPPG PPLCFSRFSV SPALETPGPP ARAPDARPAG PVEN
//
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).
CC   -----------------------------------------------------------------------
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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   A6MDD2_MOUSE            Unreviewed;       981 AA.
AC   A6MDD2;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   08-MAR-2011, entry version 36.
DE   SubName: Full=Protein tyrosine phosphatase receptor type N;
DE   Flags: Precursor;
GN   Name=Ptprn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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=17560335; DOI=10.1016/j.ccr.2007.04.017;
RA   Seaman S., Stevens J., Yang M.Y., Logsdon D., Graff-Cherry C.,
RA   St Croix B.;
RT   "Genes that distinguish physiological and pathological angiogenesis.";
RL   Cancer Cell 11:539-554(2007).
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
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DR   EMBL; DQ832283; ABI30217.1; -; mRNA.
DR   IPI; IPI00313306; -.
DR   RefSeq; NP_033011.2; NM_008985.2.
DR   UniGene; Mm.2902; -.
DR   ProteinModelPortal; A6MDD2; -.
DR   SMR; A6MDD2; 470-560, 689-978.
DR   STRING; A6MDD2; -.
DR   Ensembl; ENSMUST00000027404; ENSMUSP00000027404; ENSMUSG00000026204.
DR   GeneID; 19275; -.
DR   KEGG; mmu:19275; -.
DR   CTD; 19275; -.
DR   MGI; MGI:102765; Ptprn.
DR   HOVERGEN; HBG053762; -.
DR   InParanoid; A6MDD2; -.
DR   OMA; EVCIQDG; -.
DR   NextBio; 296176; -.
DR   Bgee; A6MDD2; -.
DR   Genevestigator; A6MDD2; -.
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: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   Hydrolase; Receptor; Signal.
FT   SIGNAL        1     37       Potential.
FT   CHAIN        38    981       Potential.
FT                                /FTId=PRO_5000254106.
SQ   SEQUENCE   981 AA;  106025 MW;  09C58C9DD0D6F4D2 CRC64;
     MRRPRRPGGS GGSGGSGGLR LLVCLLLLSG RPGGCSAISA HGCLFDRRLC SHLEVCIQDG
     LFGQCQAGVG QARPLLQVTS PVLQRLQGVL RQLMSQGLSW HDDLTQHVIS QEMERIPRLR
     PPEPHPRDRS GLVPRKPGPA GELLTQGNPT GSSPAAQGFP RPAGGGDGAG AGSPLSSLQA
     ELLPPLLEHL LMPPQPPHPA LTYEPALLQP YLFHQFGSRD GSRGSESSSG VVGVGHLSKA
     EGPALFSRSA SKAILGTHSG HSFGDLTGPS PAQLFQDSGL LYMAQELPVP GRARAPRLPE
     NGGNRAEDSS EGHEEEVLGG RGEKSPPQAA QPELSLQRLT AVLAGYGVEL RQLTPEQFST
     LLTLLQLLPK GTGRNLEGAV NVGGADVKKT IQQMQRGDPA EALPPTPSLP GYLTASPASS
     EVQQVLSPGF PEPPHTPSPL GSSSVLLEKK SPLGQSQPTV VGRPSARPSA EEYGYIVTDQ
     KPLSLVAGVR LLEILAEHVH MSSGSFINIS VVGPAVTFRI RHNEQNLSLA DVTQQAGLVK
     SELEAQTGLQ ILQTGVGQRE EAAEVLPRQA HGISPMRSVL LTLVALAGVA GLLVALAVAL
     CMRHHSRQRD KERLAALGPE GAHGDTTFEY QDLCRQHMAT KSLFNRAEGQ PEPSRVSSVS
     SQFSDAAQAS PSSHSSTPSW CEEPAQANMD ISTGHMILAY MEDHLRNRDR LAKEWQALCA
     YQAEPNTCAA AQDESNIKKN RHPDFLPYDH ARIKLKVESS PSRSDYINAS PIIEHDPRMP
     AYIATQGPLS HTIADFWQMV WESGCTVIVM LTPLVEDGVK QCDRYWPDEG SSLYHVYEVN
     LVSEHIWCED FLVRSFYLKN LQTQETRTLT QFHFLSWPAE GTPASTRPLL DFRRKVNKCY
     RGRSCPIIVH CSDGAGRTGT YILIDMVLNR MAKGVKEIDI AATLEHVRDQ RPGLVRSKDQ
     FEFALTAVAE EVNAILKALP Q
//
ID   A7MCX4_MOUSE            Unreviewed;       210 AA.
AC   A7MCX4;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   05-OCT-2010, entry version 15.
DE   SubName: Full=Epb4.1l3 protein;
DE   Flags: Fragment;
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).
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DR   EMBL; BC152368; AAI52369.1; -; mRNA.
DR   IPI; IPI00404739; -.
DR   UniGene; Mm.131135; -.
DR   STRING; A7MCX4; -.
DR   Ensembl; ENSMUST00000024843; ENSMUSP00000024843; ENSMUSG00000024044.
DR   Ensembl; ENSMUST00000077529; ENSMUSP00000076734; ENSMUSG00000024044.
DR   Ensembl; ENSMUST00000080208; ENSMUSP00000079098; ENSMUSG00000024044.
DR   Ensembl; ENSMUST00000112678; ENSMUSP00000108298; ENSMUSG00000024044.
DR   Ensembl; ENSMUST00000112679; ENSMUSP00000108299; ENSMUSG00000024044.
DR   Ensembl; ENSMUST00000112680; ENSMUSP00000108300; ENSMUSG00000024044.
DR   MGI; MGI:103008; Epb4.1l3.
DR   HOGENOM; HBG715532; -.
DR   HOVERGEN; HBG007777; -.
DR   InParanoid; A7MCX4; -.
DR   Bgee; A7MCX4; -.
DR   Genevestigator; A7MCX4; -.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR008379; Band_4.1_C.
DR   Pfam; PF05902; 4_1_CTD; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   210 AA;  22498 MW;  00CFFAFBA26CA68C CRC64;
     SRTPAPARSP RHTGKGKEGS SVTEAAKEQR GEEVDQSAPE QEQPATVSHE EEQASTIRTS
     EGLEQKSHFE SSTVRVESTS VGSISPGGAK LEISTKEVPV VHTETKTITY ESSQVDPGAD
     LEPGVLMSAQ TITSETTSTT TTTHITKTVK GGISETRIEK RIVITGDADI DHDQALAQAI
     KEAKEQHPDM SVTKVVVHKE TEITPEDGED
//
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   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.
CC   -----------------------------------------------------------------------
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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   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   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   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   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   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   B1AWT3_MOUSE            Unreviewed;       454 AA.
AC   B1AWT3;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   05-OCT-2010, entry version 18.
DE   SubName: Full=Ras-related GTP binding D;
GN   Name=Rragd; ORFNames=RP23-360H6.3-002;
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   Dunn M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL772288; CAM22252.1; -; Genomic_DNA.
DR   IPI; IPI00187271; -.
DR   UniGene; Mm.300814; -.
DR   UniGene; Mm.396693; -.
DR   ProteinModelPortal; B1AWT3; -.
DR   SMR; B1AWT3; 115-293.
DR   PRIDE; B1AWT3; -.
DR   Ensembl; ENSMUST00000029946; ENSMUSP00000029946; ENSMUSG00000028278.
DR   MGI; MGI:1098604; Rragd.
DR   HOGENOM; HBG329490; -.
DR   HOVERGEN; HBG059482; -.
DR   InParanoid; B1AWT3; -.
DR   OMA; CDMIDVT; -.
DR   PhylomeDB; B1AWT3; -.
DR   Bgee; B1AWT3; -.
DR   Genevestigator; B1AWT3; -.
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   454 AA;  51803 MW;  461B574F9655A2E7 CRC64;
     MSQVLGKPQP QGEDGGEDEE EDELVGLAGY EDGPESSDAE LDSGPEEGES RRNSWMPRSW
     CSEATRHECW EPGLWRSSHL LGIGGGWRMP FILVLRRQRQ ADFFLDFSDP FSTEVKPRIL
     LMGLRRSGKS SIQKVVFHKM SPSETLFLES TNRICREDVS NSSFVNFQIW DFPGQIDFFD
     PTFDYEMIFR GTGALIFVID SQDDYMEALA RLHLTVTRAY KVNTDINFEV FIHKVDGLSD
     DHKIETQRDI HQRANDDLAD AGLEKIHLSF YLTSIYDHSI FEAFSKVVQK LIPQLPTLEN
     LLNIFISNSG IEKAFLFDVV SKIYIATDST PVDMQTYELC CDMIDVVIDI SCIYGLKEDG
     AGAPYDKDST AIIKLNNTTV LYLKEVTKFL ALVCFVREES FERKGLIDYN FHCFRKAIHE
     VFEVRMKMVK SRKAQSRLPK KTGATPNGTP RVLL
//
ID   B1AXB2_MOUSE            Unreviewed;       921 AA.
AC   B1AXB2;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 29.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase;
DE            EC=3.1.2.15;
GN   Name=Usp11; ORFNames=RP23-394F6.4-001, mCG_126526;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; 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.
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   -!- 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; AL807240; CAM23095.1; -; Genomic_DNA.
DR   EMBL; CH466625; EDL00740.1; -; Genomic_DNA.
DR   IPI; IPI00889874; -.
DR   RefSeq; NP_663603.3; NM_145628.4.
DR   UniGene; Mm.34489; -.
DR   ProteinModelPortal; B1AXB2; -.
DR   SMR; B1AXB2; 27-134.
DR   STRING; B1AXB2; -.
DR   Ensembl; ENSMUST00000033383; ENSMUSP00000033383; ENSMUSG00000031066.
DR   GeneID; 236733; -.
DR   KEGG; mmu:236733; -.
DR   CTD; 236733; -.
DR   MGI; MGI:2384312; Usp11.
DR   HOVERGEN; HBG000864; -.
DR   InParanoid; B1AXB2; -.
DR   OMA; ENQIESK; -.
DR   PhylomeDB; B1AXB2; -.
DR   NextBio; 383051; -.
DR   Bgee; B1AXB2; -.
DR   Genevestigator; B1AXB2; -.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:EC.
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   Pfam; PF06337; DUF1055; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00695; DUSP; 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   3: Inferred from homology;
KW   Hydrolase; Protease; Thiol protease; Ubl conjugation pathway.
SQ   SEQUENCE   921 AA;  105384 MW;  269E4A3267B9EE1D CRC64;
     MAAVAADPAA AAVPASAEDR DTQPEAMPDL DEQWRQIGNG RERPLRAGES WFLVEKHWYK
     QWEVYVKGGD QDASTFPGCI NNAGLFEDQI SWHLRERLLE GDDYVLLPAP AWNYMVSWYG
     LMDGQPPIER KVIELPGIRK VEVYPLELLL VQHSDMETAL TIQFSYTDSV ELVLQTAREQ
     FLVEPQEDTR LWTKNSEGSL DRLCNTQITL LDACLETGQL VIMETRNKDG TWPSAQLCGM
     NNIPDEDEDF QGQPGICGLT NLGNTCFMNS ALQCLSNVPQ LTEYFLNNRY LEELNFRNPL
     GMKGELAEAY ADLVKQTWSG YHRSIVPNVF KNKVGHFASQ FLGYQQHDSQ ELLSFLLDGL
     HEDLNRVKKK EYVELCNGAG RPDLEVAQEA WQNHKRRNDS VIVDTFHGLF KSTLVCPDCG
     NVSVTFDPFC YLSVPLPVCS RRVLEVFFVP MDPRRKPEQH RVVVPKKGNI SDLCVALSTH
     TSVAPDKMIV ADVFSHRFYK LYQLEDPLSG ILDRDDIFVY EVTGRIEPVE GSRDDIVVPV
     YLRERTPSRD YNNSYYGLIL FGHPLLVSVP RDRFSWEGLY NILMYRLSRY VTKPTSDEDD
     GDEKVDEDED EDVEDDSSSE EEKEEMSAPT VNDGTREAEQ EQAGTSSGVT ERCPSLLDNS
     LRASQWPPRR RRKQLFTLQT VNSNGTSDRT TSPEEMQTQP YIAMDWEPDM KRRYYDEVEA
     EGYVKHDCVG YMLKKSPVQL KECIKLFTTV ETLEKENPWY CSSCKQHQLA TKKLDLWMLP
     EVLIIHLKRF SFSKISREKL DTLVQFPIRD LDFSEFVIKP KNESSPDLYK YDLIAVSNHY
     GGMRDGHYTT FACNKDSGQW HYFDDNSVSP VNENQIESKA AYVLFYQRQD VGRRQSQTSS
     SDTPASPVSS STPNSDIMDI N
//
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   B1AZ45_MOUSE            Unreviewed;       482 AA.
AC   B1AZ45;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   30-NOV-2010, entry version 26.
DE   SubName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2;
GN   Name=Baiap2; ORFNames=RP23-390H16.1-004;
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   Holt K.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Matthews L.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL953913; CAM22926.1; -; Genomic_DNA.
DR   EMBL; AL929234; CAM22926.1; JOINED; Genomic_DNA.
DR   EMBL; AL929234; CAM27714.1; -; Genomic_DNA.
DR   EMBL; AL953913; CAM27714.1; JOINED; Genomic_DNA.
DR   IPI; IPI00459465; -.
DR   RefSeq; NP_001032843.1; NM_001037754.3.
DR   UniGene; Mm.197534; -.
DR   ProteinModelPortal; B1AZ45; -.
DR   SMR; B1AZ45; 1-248, 339-401.
DR   STRING; B1AZ45; -.
DR   PRIDE; B1AZ45; -.
DR   Ensembl; ENSMUST00000103021; ENSMUSP00000099310; ENSMUSG00000025372.
DR   GeneID; 108100; -.
DR   KEGG; mmu:108100; -.
DR   CTD; 108100; -.
DR   MGI; MGI:2137336; Baiap2.
DR   HOVERGEN; HBG054462; -.
DR   NextBio; 360066; -.
DR   Bgee; B1AZ45; -.
DR   Genevestigator; B1AZ45; -.
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   4: Predicted;
SQ   SEQUENCE   482 AA;  53274 MW;  F3FA1DFDC1E0D579 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 PPELAPFVGS QSKLSDSYSN
     TLPVRKSVTP KNSYATTENK TLPRSSSMAA GLERNGRMRV KAIFSHAAGD NSTLLSFKEG
     DLITLLVPEA RDGWHYGESE KTKMRGWFPF SYTRVLDSDG SDRLHMSLQQ GKSSSTGNLL
     DKDDLALPPP DYGTSSRAFP TQTAGTFKQR PYSVAVPAFS QGLDDYGARS VSSGSGTLVS
     TV
//
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   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   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).
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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   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.
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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   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   B2RU85_MOUSE            Unreviewed;      1095 AA.
AC   B2RU85;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   11-JAN-2011, entry version 30.
DE   SubName: Full=Potassium voltage-gated channel, subfamily H (Eag-related), member 3;
DE   SubName: Full=Potassium voltage-gated channel, subfamily H (Eag-related), member 3, isoform CRA_a;
GN   Name=Kcnh3; ORFNames=mCG_18387;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; 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.
CC   -!- SIMILARITY: Contains 1 cyclic nucleotide-binding domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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DR   EMBL; BC141013; AAI41014.1; -; mRNA.
DR   EMBL; BC145145; AAI45146.1; -; mRNA.
DR   EMBL; CH466550; EDL04139.1; -; Genomic_DNA.
DR   IPI; IPI00420151; -.
DR   RefSeq; NP_034731.3; NM_010601.3.
DR   UniGene; Mm.374793; -.
DR   ProteinModelPortal; B2RU85; -.
DR   SMR; B2RU85; 28-135.
DR   STRING; B2RU85; -.
DR   PRIDE; B2RU85; -.
DR   Ensembl; ENSMUST00000041415; ENSMUSP00000040548; ENSMUSG00000037579.
DR   GeneID; 16512; -.
DR   KEGG; mmu:16512; -.
DR   CTD; 16512; -.
DR   MGI; MGI:1341723; Kcnh3.
DR   HOGENOM; HBG717083; -.
DR   HOVERGEN; HBG052232; -.
DR   InParanoid; B2RU85; -.
DR   OMA; ETPYYLV; -.
DR   PhylomeDB; B2RU85; -.
DR   NextBio; 289857; -.
DR   Bgee; B2RU85; -.
DR   Genevestigator; B2RU85; -.
DR   GO; GO:0016021; C:integral to membrane; 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; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR   InterPro; IPR003950; K_chnl_volt-dep_ELK.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR013656; PAS_4.
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; PF08448; PAS_4; 1.
DR   PRINTS; PR01463; EAGCHANLFMLY.
DR   PRINTS; PR01465; ELKCHANNEL.
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; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   2: Evidence at transcript level;
KW   Ion transport; Ionic channel; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
SQ   SEQUENCE   1095 AA;  118244 MW;  C2C3A26090E37A50 CRC64;
     MPAMRGLLAP QNTFLDTIAT RFDGTHSNFV LGNAQVAGLF PVVYCSDGFC DLTGFSRAEV
     MQRGCACSFL YGPDTSELVR QQIRKALDEH KEFKAELILY RKSGLPFWCL LDVIPIKNEK
     GEVALFLVSH KDISETKNRG GPDNWKERGG GRRRYGRAGS KGFNANRRRS RAVLYHLSGH
     LQKQPKGKHK LNKGVFGEKP NLPEYKVAAI RKSPFILLHC GALRATWDGF ILLATLYVAV
     TVPYSVCVST AREPSAARGP PSVCDLAVEV LFILDIVLNF RTTFVSKSGQ VVFAPKSICL
     HYVTTWFLLD VIAALPFDLL HAFKVNVYVG AHLLKTVRLL RLLRLLPRLD RYSQYSAVVL
     TLLMAVFALL AHWVACVWFY IGQQEIESSE SELPEIGWLQ ELARRLETPY YLVSRSPDGG
     NSSGQSENCS SSSSSSGSGG GRGSEANGTG LELLGGPSLR SAYITSLYFA LSSLTSVGFG
     NVSANTDTEK IFSICTMLIG ALMHAVVFGN VTAIIQRMYA RRFLYHSRTR DLRDYIRIHR
     IPKPLKQRML EYFQATWAVN NGIDTTELLQ SLPDELRADI AMHLHKEVLQ LPLFEAASRG
     CLRALSLALR PAFCTPGEYL IHQGDALQAL YFVCSGSMEV LKGGTVLAIL GKGDLIGCEL
     PQREQVVKAN ADVKGLTYCV LQCLQLAGLH ESLALYPEFA PRFSRGLRGE LSYNLGAGGV
     SAEVDTSSLS GDNTLMSTLE EKETDGEQGH TVSPAPADEP SSPLLSPGCT SSSSAAKLLS
     PRRTAPRPRL GGRGRPSRAG VLKPEAGPSA HPRSLDGLQL PPMPWNVPPD LSPRVVDGIE
     DGCSSDQPKF SFRVGQSGPE CSSSPSPGTE SGLLTVPLGP SEARNTDTLD KLRQAVMELS
     EQVLQMREGL QSLRQAVQLI LVPQGEGQCP RGSGEEPCPA TASGLLQPLR VDTGASSYCL
     QPPAGSVLSG TWPHPRPGQP PPLMAPWPWG PPASQSSPWP RATALWTSTS DSEPPGSGDL
     CSEPSTPASP PPSEEGARTG TPAPVSQAEA TSTGEPPPGP GGRALPWDPH SLEMVLIGCH
     GPGTVQWTQE EGTGV
//
ID   B2RXS8_MOUSE            Unreviewed;      1463 AA.
AC   B2RXS8;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 22.
DE   SubName: Full=Ptprz1 protein;
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC157965; AAI57966.1; -; mRNA.
DR   IPI; IPI00627008; -.
DR   UniGene; Mm.41639; -.
DR   ProteinModelPortal; B2RXS8; -.
DR   SMR; B2RXS8; 37-300, 846-1432.
DR   STRING; B2RXS8; -.
DR   HOVERGEN; HBG053760; -.
DR   Genevestigator; B2RXS8; -.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
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.
SQ   SEQUENCE   1463 AA;  164358 MW;  2AED8BD868EAC191 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 YNEASNSSHE SRIGLAEGLE
     SEKKAVIPLV IVSALTFICL VVLVGILIYW RKCFQTAHFY LEDNTSPRVI STPPTPIFPI
     SDDIGAIPIK HFPKHVADLH ASNGFTEEFE TLKEFYQEVQ SCTADLGITA DSSNHPDNKH
     KNRYVNIVAY DHSRVKLTQL AEKDGKLTDY INANYVDGYN RPKAYIAAQG PLKSTAEDFW
     RMIWEHNVEV IVMITNLVEK GRRKCDQYWP TDGSEEYGSF LVNQKSVQVL AYYTVRNFTL
     RNTKLKKGSQ KGRSSGRLVT QYHYTQWPDM GVPEYSLPVL AFVRKAAQAK RHAVGPVVVH
     CSAGVGRTGT YIVLDSMLQQ IQHEGTVNIF GFLKHIRSQR NYLVQTEEQY VFIHDTLVEA
     ILSKETEVPD SHIHSYVNTL LIPGPTGKTK LEKQFQLLSQ SNILQSDYST ALKQCNREKN
     RTSSIIPVER SRVGISSLSG EGTDYINASY IMGYYQSNEF IITQHPLLHT IKDFWRMIWD
     HNAQLVVMIP DGQNMAEDEF VYWPNKDEPI NCESFKVTLM SEEHKCLSNE EKLIVQDFIL
     EATQDDYVLE VRHFQCPKWP NPDSPISKTF ELISIIKEEA ANRDGPMIVH DEHGGVTAGT
     FCALTTLMHQ LEKENAMDVY QVAKMINLMR PGVFTDIEQY QFLYKVVLSL VSTRQEENPS
     TSLDSNGAAL PDGNIAESLE SLV
//
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   B6ZHC4_MOUSE            Unreviewed;        95 AA.
AC   B6ZHC4;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   05-OCT-2010, entry version 8.
DE   SubName: Full=Erythrocyte protein band 4.1-like 1;
DE   Flags: Fragment;
GN   Name=Epb4.1l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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=Crebellum;
RA   Okumura K., Mochizuki E., Yokohama M., Mburu P., Yonekawa H.,
RA   Brown S., Kikkawa Y.;
RT   "Protein 4.1 expression in the developing mouse hair cells of
RT   cochlea.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AB370257; BAG84706.1; -; mRNA.
DR   UniGene; Mm.20852; -.
DR   Genevestigator; B6ZHC4; -.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR008379; Band_4.1_C.
DR   Pfam; PF05902; 4_1_CTD; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   95 AA;  10523 MW;  84C3B4FF46D0A752 CRC64;
     VDGGTPMVKD FMTTPPCITT ETISTTMTVK GGFSETRIEK RIIITGDEDV DQDQALALAI
     KEAKLQHPDM LVTKAVVYRE TDPSPEERDK KPQES
//
ID   B6ZHC5_MOUSE            Unreviewed;       794 AA.
AC   B6ZHC5;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   05-OCT-2010, entry version 18.
DE   SubName: Full=Erythrocyte protein band 4.1-like 2;
GN   Name=Epb4.1l2;
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=C3H/HeN; TISSUE=Cochlea;
RA   Okumura K., Mochizuki E., Yokohama M., Mburu P., Yonekawa H.,
RA   Brown S., Kikkawa Y.;
RT   "Protein 4.1 expression in the developing mouse hair cells of
RT   cochlea.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 FERM domain.
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DR   EMBL; AB370258; BAG84707.1; -; mRNA.
DR   IPI; IPI00330290; -.
DR   UniGene; Mm.306026; -.
DR   STRING; B6ZHC5; -.
DR   Ensembl; ENSMUST00000092644; ENSMUSP00000090313; ENSMUSG00000019978.
DR   MGI; MGI:103009; Epb4.1l2.
DR   HOVERGEN; HBG007777; -.
DR   Bgee; B6ZHC5; -.
DR   Genevestigator; B6ZHC5; -.
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;  88490 MW;  FE57D9C0F2573069 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 YFGLLFQDRP EHKNWLDPAK 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   B6ZHD0_MOUSE            Unreviewed;       988 AA.
AC   B6ZHD0;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   05-OCT-2010, entry version 18.
DE   SubName: Full=Erythrocyte protein band 4.1-like 2;
GN   Name=Epb4.1l2;
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=C3H/HeN; TISSUE=Cochlea;
RA   Okumura K., Mochizuki E., Yokohama M., Mburu P., Yonekawa H.,
RA   Brown S., Kikkawa Y.;
RT   "Protein 4.1 expression in the developing mouse hair cells of
RT   cochlea.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 FERM domain.
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DR   EMBL; AB370263; BAG84712.1; -; mRNA.
DR   IPI; IPI00330289; -.
DR   UniGene; Mm.306026; -.
DR   STRING; B6ZHD0; -.
DR   Ensembl; ENSMUST00000053748; ENSMUSP00000055122; ENSMUSG00000019978.
DR   MGI; MGI:103009; Epb4.1l2.
DR   HOVERGEN; HBG007777; -.
DR   Bgee; B6ZHD0; -.
DR   Genevestigator; B6ZHD0; -.
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   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   988 AA;  109896 MW;  B4458E3AA4902477 CRC64;
     MTTEVGSASE VKKGSDQAGA DASKEKAKEV ENEQTPVSEP EEEKGSQPGP PVERQSTPRL
     RNRGKDPSEN 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 AEGKKNTLRV
     DGDNIYVRHS NLMLEDLDKA QEAILKHQAS ISELKRNFMA STPEPRPSEW EKRRVTPLPF
     QPQASSHETL NVVEEKKRAE VGKDESVITE EMNGKEMSPG HGPGETRKVE PVAHKDSTSL
     SSESSSSSSE SEEDVGEYQP HHRVTEGTIR EEQEECDEEL EEEPGQGAKV VEREAAVPDA
     VPDRQAGASV LPVETEAQEH VVAQKLPGEK GAHGGTAEQD PREEAEEDPH RVNGEVPHLD
     LDGLPEIICC SEPPVVKTEM VTISDASQRT EISTKEVPIV QTETKTITYE SPQIDGGAGG
     DSGVLLTAQT ITSESASTTT TTHITKTVKG GISVTRIEKR IVITGDAALD HDQALAQAIR
     EAREQHPDMS VTRVVVHKET ELAEEGEE
//
ID   B6ZHD1_MOUSE            Unreviewed;       929 AA.
AC   B6ZHD1;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   05-OCT-2010, entry version 18.
DE   SubName: Full=Erythrocyte protein band 4.1-like 3;
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=Brain;
RA   Okumura K., Mochizuki E., Yokohama M., Mburu P., Yonekawa H.,
RA   Brown S., Kikkawa Y.;
RT   "Protein 4.1 expression in the developing mouse hair cells of
RT   cochlea.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 FERM domain.
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DR   EMBL; AB370264; BAG84713.1; -; mRNA.
DR   IPI; IPI00125501; -.
DR   UniGene; Mm.131135; -.
DR   STRING; B6ZHD1; -.
DR   Ensembl; ENSMUST00000080208; ENSMUSP00000079098; ENSMUSG00000024044.
DR   MGI; MGI:103008; Epb4.1l3.
DR   HOVERGEN; HBG007777; -.
DR   Bgee; B6ZHD1; -.
DR   Genevestigator; B6ZHD1; -.
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   929 AA;  103368 MW;  56C29FC6CF187E33 CRC64;
     MTTESGSDSE SKPDQEAEPQ EAAGPQGQAG AQPGPEPAGG NGSLNGEKQQ PALEQFPEAA
     AHSTPVKREI GDKDRDFAAA AAKQLEYQQF EDDKLSQRSS SSKLSRSPLK IVKRPKSTQC
     KVTLLDGSEY GCDVDKRSRG QVLFDKVCEH QNLLEKDYFG LTYRDAENQE NWLDPAKEIK
     KQIRSGAWHF SFNVKFYPPD PAQLSEDITR YYLCLQRRDD IVSGRLPCSF VTLALLGSYT
     VQSELGDYDP DECGNDYISE FRFAPNHTKE LEDKVIELHK SHRGTTPAEA EMHFLENAKK
     LSMYGVDLHH AKDSEGVEIM LGVCASGLLI YRDRLRINRF AWPKVLKISY KRNNFYIKIR
     PGEFEQFEST IGFKLPNHRA AKRLWKVCVE HHTFFRLLLP EAPPKKFLTL GSKFRYSGRT
     QAQTRRASAL IDRPAPYFER SSSKRYTMSR SLDGASVSEN HEIYMKDSVS AAEVGTGQYA
     TTKGISQTNL ITTVAPEKKA EEERVEEEDR RKKAEEATPV TALRHEGKTD SERTDTAADG
     ETSATESDQE EDAEIKAQDL DKTQDELMKH QTNISELKRT FLETSTETAL TNEWEKRLST
     SPVRLAARQE DAPMIEPLVP EETKQSSGEK LMDGSEIFSL LESARKPTEF IGGVSSTTQS
     WVQKLETKTE PVEAEVESTP HPQPLSTEKV LQETILVEER HVMSVHASGD ASHTARDEVD
     AAESTPTDRR HTGKGREGSS VTEAAKEQRG EEVDQSAPEQ EQPATVSHEE EQASTIRTSE
     GLEQKSHFES STVRVESTSV GSISPGGAKL EISTKEVPVV HTETKTITYE SSQVDPGADL
     EPGVLMSAQT ITSETTSTTT TTHITKTVKG GISETRIEKR IVITGDADID HDQALAQAIK
     EAKEQHPDMS VTKVVVHKET EITPEDGED
//
ID   B7ZBW3_MOUSE            Unreviewed;       463 AA.
AC   B7ZBW3;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 18.
DE   RecName: Full=Elongation factor 1-alpha;
GN   Name=Eef1a2; ORFNames=RP23-401L17.3-001;
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   Wall M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC       aminoacyl-tRNA to the A-site of ribosomes during protein
CC       biosynthesis (By similarity).
CC   -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC       EF-Tu/EF-1A subfamily.
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DR   EMBL; AL450341; CAX15866.1; -; Genomic_DNA.
DR   IPI; IPI00119667; -.
DR   UniGene; Mm.2645; -.
DR   PhosphoSite; B7ZBW3; -.
DR   Ensembl; ENSMUST00000140437; ENSMUSP00000118595; ENSMUSG00000016349.
DR   MGI; MGI:1096317; Eef1a2.
DR   GeneTree; ENSGT00570000078778; -.
DR   HOVERGEN; HBG000179; -.
DR   OrthoDB; EOG40K7ZP; -.
DR   Bgee; B7ZBW3; -.
DR   Genevestigator; B7ZBW3; -.
DR   GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IDA:MGI.
DR   GO; GO:0006916; P:anti-apoptosis; IDA:MGI.
DR   HAMAP; MF_00118_A; EF_Tu_A; 1; -.
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   3: Inferred from homology;
KW   Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
SQ   SEQUENCE   463 AA;  50390 MW;  B5111C017A602A85 CRC64;
     MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEVG KGSFKYAWVL
     DKLKAERERG ITIDISLWKF ETTKYYITII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV
     GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP AYSEKRYDEI VKEVSAYIKK
     IGYNPATVPF VPISGWHGDN MLEPSPNVPW 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   B7ZCA7_MOUSE            Unreviewed;       261 AA.
AC   B7ZCA7;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-FEB-2011, entry version 12.
DE   SubName: Full=Novel protein (9030409G11Rik);
DE   Flags: Fragment;
GN   Name=9030409G11Rik; Synonyms=RP24-548L8.1; ORFNames=RP24-548L8.1-006;
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   Lad H.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL663037; CAX15670.1; -; Genomic_DNA.
DR   IPI; IPI00918224; -.
DR   Ensembl; ENSMUST00000129032; ENSMUSP00000115897; ENSMUSG00000040606.
DR   MGI; MGI:1918779; 9030409G11Rik.
DR   GeneTree; ENSGT00550000074230; -.
DR   HOVERGEN; HBG058719; -.
DR   Bgee; B7ZCA7; -.
DR   Genevestigator; B7ZCA7; -.
PE   4: Predicted;
FT   NON_TER       1      1
SQ   SEQUENCE   261 AA;  29629 MW;  F8B64F910303246B CRC64;
     GKCSEVLSAT ELRVQLVQKE QELARAKEAL QAMKADRKRL KGEKTDLVSQ MQQLYATLES
     REEQLRDFIR NYEQHRKESE DAVKALAKEK DLLEREKWEL RRQAKEATDH AAALRSQLDL
     KDNRMKELEA ELAMAKQSLA TLTKDVPKRH SLAMPGETVL NGNQEWVVQA DLPLTAAIRQ
     SQQTLYHSHP PHPADRQAVR VSPCHSRQPS VISDASAAEG DRSSTPSDIN SPRHRTHSLW
     RQSRPSSEEP TQPYCTVTRG S
//
ID   B7ZNF6_MOUSE            Unreviewed;      1221 AA.
AC   B7ZNF6;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 14.
DE   SubName: Full=Ctnnd2 protein;
GN   Name=Ctnnd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; 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; BC145217; AAI45218.1; -; mRNA.
DR   IPI; IPI00136135; -.
DR   UniGene; Mm.321648; -.
DR   ProteinModelPortal; B7ZNF6; -.
DR   Ensembl; ENSMUST00000110414; ENSMUSP00000106044; ENSMUSG00000022240.
DR   MGI; MGI:1195966; Ctnnd2.
DR   HOVERGEN; HBG004284; -.
DR   Bgee; B7ZNF6; -.
DR   Genevestigator; B7ZNF6; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0007612; P:learning; IMP:MGI.
DR   GO; GO:0001763; P:morphogenesis of a branching structure; IDA:MGI.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; IMP: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; 4.
DR   SMART; SM00185; ARM; 7.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 3.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1221 AA;  132358 MW;  200141729DF577C4 CRC64;
     MFARKQSGAA PFGAMPVPDQ PPSASEKNSS LSPGLNTSNG DGSETETTSA ILASVKEQEL
     QFERLTRELE AERQIVASQL ERCKLGSETG SMSSISSAEQ FHWQTQDGQK DIEDELTTGL
     ELVDSCIRSL QESGILDPQD YSTSERPSLL SQSALQLNSK PEGSFQYPAS YHSNQTLALG
     DTAPSQLPAR STQARAAGQS FSQGTTGRAG HLAGSEPAPP PPPPREPFAP SLGSAFHLPD
     APPAAAALYY SSSTLPAPPR GGSPLTTTQG GSPTKLQRGG SAPEGAAYAA PRGSSPKQSP
     SRLAKSYSTS SPINIVVSSA GLSPIRVTSP PTVQSTISSS PIHQLSSTIG TYATLSPTKR
     LVHASEQYSK HSQELYATAT LQRPGSLAAG SRASYSSQHG HLAPELRALQ SPEHHIDPIY
     EDRVYQKPPM RSLSQSQGDP LPPAHTGTFR TSTAPSSPGV DSVPLQRTGS QHGPQNAAAA
     TFQRASYAAG PASNYADPYR QLQYCASVDS PYSKSGPALP PEGTLARSPS IDSIQKDPRE
     FGWRDPELPE VIQMLQHQFP SVQSNAAAYL QHLCFGDNKI KAEIRRQGGI QLLVDLLDHR
     MTEVHRSACG ALRNLVYGKA NDDNKIALKN CGGIPALVRL LRKTTDLEIR ELVTGVLWNL
     SSCDALKMPI IQDALAVLTN AVIIPHSGWE NSPLQDDRKI QLHSSQVLRN ATGCLRNVSS
     AGEEARRRMR ECDGLTDALL YVIQSALGSS EIDSKTVENC VCILRNLSYR LAAETSQGQH
     MGTDELDGLL CGETNGKDTE SSGCWGKKKK KKKSQDQWDG VGPLPDCAEP PKGIQMLWHP
     SIVKPYLTLL SECSNPDTLE GAAGALQNLA AGSWKWSVYI RAAVRKEKGL PILVELLRID
     NDRVVCAVAT ALRNMALDVR NKELIGKYAM RDLVHRLPGG NNSNNSGSKA MSDDTVTAVC
     CTLHEVITKN MENAKALRDA GGIEKLVGIS KSKGDKHSPK VVKAASQVLN SMWQYRDLRS
     LYKKDGWSQY HFVASSSTIE RDRQRPYSSS RTPSISPVRV SPNNRSASAP ASPREMISLK
     ERKTDYESAG NNATYHGTKG EHTSRKDTMT AQNTGVSTLY RNSYGAPAED IKQNQVSTQP
     VPQEPSRKDY ETYQPFPNST RNYDESFFED QVHHRPPASE YTMHLGLKST GNYVDFYSAA
     RPYSELNYET SHYPASPDSW V
//
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   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   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).
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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   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).
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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   C9K0Z8_MOUSE            Unreviewed;       863 AA.
AC   C9K0Z8;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   30-NOV-2010, entry version 11.
DE   SubName: Full=Hyperpolarization-activated cation channel 2;
GN   Name=Hcn2; Synonyms=hcn2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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.
CC   -!- SIMILARITY: Contains 1 cyclic nucleotide-binding domain.
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DR   EMBL; AB154248; BAI44633.1; -; mRNA.
DR   IPI; IPI00133980; -.
DR   UniGene; Mm.12956; -.
DR   ProteinModelPortal; C9K0Z8; -.
DR   Ensembl; ENSMUST00000020581; ENSMUSP00000020581; ENSMUSG00000020331.
DR   Ensembl; ENSMUST00000099513; ENSMUSP00000097113; ENSMUSG00000020331.
DR   MGI; MGI:1298210; Hcn2.
DR   Bgee; C9K0Z8; -.
DR   GO; GO:0016021; C:integral to membrane; 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; PS50042; CNMP_BINDING_3; 1.
PE   2: Evidence at transcript level;
KW   Ion transport; Ionic channel; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
SQ   SEQUENCE   863 AA;  94712 MW;  006DEDDC8C3B6C87 CRC64;
     MDARGGGGRP GDSPGTTPAP GPPPPPPPPA PPQPQPPPAP PPNPTTPSHP ESADESGPRA
     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   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   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.
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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   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
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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   D3YZB1_MOUSE            Unreviewed;        78 AA.
AC   D3YZB1;
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=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   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; AC114919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC132368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC140983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00874805; -.
DR   Ensembl; ENSMUST00000115793; ENSMUSP00000111459; ENSMUSG00000038128.
DR   MGI; MGI:88258; Camk4.
DR   GeneTree; ENSGT00550000074354; -.
DR   Bgee; D3YZB1; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; TAS:MGI.
DR   GO; GO:0005515; F:protein binding; IPI: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.
PE   4: Predicted;
SQ   SEQUENCE   78 AA;  8002 MW;  6BF847AAB653A3D4 CRC64;
     MSCANNDQAA AGGSSSGSGG VFRSPAAKML KVTVPSCPSS PCSSVTASTE NLVPDYWIDG
     SNRDPLGDFF EVESELGR
//
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   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   D3Z000_MOUSE            Unreviewed;      3490 AA.
AC   D3Z000;
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=Csmd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; 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; AL611934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL611969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL627093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL807807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL928698; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL954639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00761714; -.
DR   Ensembl; ENSMUST00000097884; ENSMUSP00000095494; ENSMUSG00000028804.
DR   MGI; MGI:2386401; Csmd2.
DR   GeneTree; ENSGT00600000084158; -.
DR   OrthoDB; EOG451DPS; -.
DR   Bgee; D3Z000; -.
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; 26.
DR   Gene3D; G3DSA:2.60.120.290; CUB; 14.
DR   Pfam; PF00431; CUB; 14.
DR   Pfam; PF00084; Sushi; 25.
DR   SMART; SM00032; CCP; 26.
DR   SMART; SM00042; CUB; 14.
DR   SUPFAM; SSF57535; Complement_control_module; 26.
DR   SUPFAM; SSF49854; CUB; 14.
DR   PROSITE; PS01180; CUB; 14.
DR   PROSITE; PS50923; SUSHI; 26.
PE   4: Predicted;
SQ   SEQUENCE   3490 AA;  379420 MW;  A9CA5A5A8C932919 CRC64;
     MPRSRGPEQG CCGCPAVRAR GEIGIWALVP GTGSRWGRPP PPPPPPPPPP PLLLLLGWGL
     LSASAAAGQN CTFHLQGPNG TVESPGFPYG YPNYANCTWT ITAEDQHRIQ LVFQSFALEE
     DFDVLSVFDG PPQAENLRTR LTGFQLPATI VSAASTLSLS LISDYAVSAQ GFRASYEVLP
     SHTCGNPGRL PNGIQQGSTF NLGDKVRYSC NPGFFLEGHA VLTCHASSEN SATWDFPLPS
     CRADDACGGT LRGQSGIISS PHFPAEYHNN ADCTWTILAE LGDTIALVFI DFQLEDGYDF
     LEVTGTEGSS LWFTGASLPA PVISSKNWLR LHFTSDGNHR QRGFSAQYQV KKQIELKSRG
     VKLMPSKDNN QKTSVLTQVG VSQGHNMCPD PGIPEKGKRL GSDFRLGSSV QFTCNEGYDL
     QGSKRITCMK VSDMFAAWSD HRPVCRARMC DAHLRGPSGI ITSPNFPIQY DNNAHCVWII
     TALNPAKVIK LAFEEFDLER GYDTLTVGDG GQDGDQKTVL YILTGTSVPD LIVSTHHQMW
     LLFQSDSSGS SLGFKASYEE IEQGSCGDPG IPAYGQREGS RFRHGDTLEF ECQPAFELVG
     QKSITCQKNN QWSAKKPGCV FSCFFNFTSP SGIVLSPNYP EDYGNHLHCV WLILARPESR
     IHLAFNDIDV EPQFDFLVIK DGATAEAPVL GTFSGNQLPS SITSSGHVAR LEFQTDHSTG
     KRGFNITFTT FRHNECPDPG VPVNGKRFGD SLQLGSSISF LCDEGFLGTQ GSETITCVLK
     EGSVVWNSAV LRCEAPCGGH LTSPSGTILS PGWPGFYKDA LSCAWVIEAQ PGYPIKITFD
     RFKTEVNYDT LEVRDGRTYS APLIGVYHGT QVPQFLISTS NYLYLLFSTD KSHSDIGFQL
     RYETITLQSD HCLDPGIPVN GQRHGNDFYV GALVTFSCDS GYTLSDGEPL ECEPNFQWSH
     ALPSCEALCG GFIQGSSGTI LSPGFPDFYP NNLNCTWVIE TSHGKGVFFT FHTFHLESGH
     DYLLITENGS FSQPLRQLTG SRLPAPISAG LYGNFTAQVR FISDFSMSYE GFNITFSEYD
     LEPCEEPEVP AYSIRKGLQF GVGDTLTFSC FPGYRLEGTA RITCLGGRRR LWSSPLPRCV
     AECGNSVTGT QGTLLSPNFP VNYNNNHECI YSIQTQPGKG IQLKAKAFEL AEGDLLKVYD
     GTNNSARLLG VFSRSEMLGV TLNSTSSSLW LDFITDAENT SKGFELQFSS FELIRCEDPG
     TPQFGYKVHD GGHFAGSSVT FSCDPGYSLR GSEELMCLSG ERRTWDRPLP TCVAECGGTV
     RGEVSGQVLS PGYPAPYEHN LNCIWTIEAD AGCTIGLHFL VFDTEEVHDV LRIWDGPVES
     GVLLKELSGP MLPKDLHSTF NSVVLQFSTD FFTSKQGFAI QFSVSTATSC NDPGVPQNGS
     RSGDSWEAGD STVFQCDPGY ALQGSAEISC VKIQNRFFWQ PSPPTCIAPC GGDLTGPSGV
     ILSPNYPEPY PPGKECDWKV TVSPDYVIAL VFNTFNLEPG YDFLHIYDGR DSLSPLIGSF
     YGSQLPSRIE SSSNSLFLAF RSDASVSNAG FVIDYTENPR ESCFDPGSIK NGTRVGSDLK
     LGSSVTYYCH GGYEVEGAST LSCILGPDGK PMWNNPRPVC TAPCGGQYVG SDGVVLSPNY
     PQNYTSGQTC LYFVTVPKDY VVFGQFAFFH TALNDIVEVH DGYSQHSRLL SSLSGSHTGE
     SLPLATSNQV LIKFSAKGQV SARGFHFVYQ AVPRTSATQC SSVPEPRYGK RLGSDFSVGA
     IIRFECNSGY ALQGSPEIEC LPVPGALAQW NVSAPTCVVP CGGNLTERRG TILSPGFPEP
     YLNSLNCVWK IMVPEGAGIQ IQVISFVTEQ NWDSLEVFDG ADNTVTMLGS FSGTTVPALL
     NSTSNQLYLH FYSDISVSAA GFHLEYKTVG LSSCPEPAVP SNGVKTGERY LVNDVVSFQC
     EPGYALQGHA HISCMPGTVR RWNYPPPLCI AQCGGAVEEM EGVILSPGFP GNYPSNMDCS
     WKISLPVGFG AHIQFLNFST EPNHDFLEIR SGPSETSRMM GRFSGSELPG SLLSTSHDSI
     VYFHSDHSQN RPGFKLEYQA YELQECPDPE PFANGIVRGA GYNVGQSVTF ECLPGYQLTG
     QPVLTCQHGT NRNWDHPLPR CEVPCGGNIT SFNGTVYSPG YPSPYSSSQD CVWQITVPIG
     HGVHLNLSLL QIEPFGDYIT VWDGPQQTSL QLGVFTRSLS KKIAHSSSNQ VLLKFHRDTA
     TGGIFAIAFS AYPLTKCPPP TILPNAEVVT ENEEFNIGDI VRYRCLPGFT LVGSEILTCK
     LGTYLQFEGP PPICEVHCPT NELLTDSTGV ILSQSYPGSY PQFQTCSWLV RVEPEYNISI
     TVEYFLSEKQ YDEFEIFDGP SGQSPLLKAL SGNYSAPLIV TSSSNSVYLR WSSDHAYNRK
     GFKIRYSAPY CSLPKAPLHG FILGQTTTQP GGSIHFGCNT GYRLVGHSMA ICTRHPQGYH
     LWSEAIPLCQ ALSCGLPDAP KNGIVFGKEY TVGTKAVYSC NEGYHLQAGA EATAECLDTG
     LWSNSNVPPQ CVPVTCPDIS SISVEHGRWR LIFETQYQFQ AQLMLICDPG YYYTGQRVIR
     CQANGRWSLG ESMPTCQIIS CGELPTPPSG HRIGTMSVYG ATAIFSCNSG YTLVGSRVRE
     CMANGLWSGS EVRCLAGHCG TPEPIVNGHI NGENFNYRGS VVYQCRAGFR LIGMSVRICQ
     QDHHWSGKTP FCVLVSCGHP GSPPHAQMSG DSYIVGAVVR YSCTGKRTLV GNSTRMCGLD
     GHWTGSLPHC SGTSTGVCGD PGIPAHGIRL GDSFAPGSVM RFSCDAGHVL RGSSERMCQA
     NGSWSGSQPE CGVISCGNPG TPSNARVVFS DGLVFSSSVV YECREGYYAT GLLSRHCSVN
     GTWTGSDPEC TVINCGDPGI PANGIRLGND FRYNKTVTYQ CVPGYVMESH RVSVLSCTKD
     RTWNGTKPVC KAIMCKPPQL IPNGKVVGSD FTWGSSVSYA CLEGYQLSLP AVLTCEGNGS
     WTGELPQCFP VFCGDPGVPP RGRREDRGFS YRSSVSFSCH APLVLVGSPR RFCQSDGTWS
     GTQPSCIDPT LTTCADPGMP QFGIQNSSQG YQVGSTVLFR CQKGYLLQGS TTRTCLPNLT
     WSGTPPDCVP HHCKQPETPT HANVGALDLP SMGYTLIYSC QEGFSLRGGS EHRTCKADGS
     WTGKPPVCLE VRPSGRPINT AREPMLTQAS VPGDVFAKNS LWKGAYEYQG KKQPAMLRVT
     GFQVANSKVN ATMIDHSGVE LHLAGNYKKE DFRLLLQVYQ VTGPVESFVN KFKDDHWALD
     GHVSSESSGG TFVYQGSVKG QGFGQFGFQR LDLRLLESDP ESIGRHFASN SSSVAAAILV
     PFIALIIAGF VLYLYKHRRR PKVPFNGYAG HENTNVRATF ENPMYDRNIQ PTDIMSNEAE
     FTVSTVCTAV
//
ID   D3Z0V7_MOUSE            Unreviewed;       995 AA.
AC   D3Z0V7;
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=Tsc22d1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; 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; AC134842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC142266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00464104; -.
DR   Ensembl; ENSMUST00000088906; ENSMUSP00000086296; ENSMUSG00000022010.
DR   Ensembl; ENSMUST00000110888; ENSMUSP00000106513; ENSMUSG00000022010.
DR   MGI; MGI:109127; Tsc22d1.
DR   GeneTree; ENSGT00530000063062; -.
DR   Bgee; D3Z0V7; -.
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; 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   995 AA;  102086 MW;  0F0D851AB9B3D158 CRC64;
     MHQPPESTAA AAAAADISAR KMAHPAMFPR RGSGGGSASA LNAAGTGVSG AAPSSEDFPP
     PSLLQPPPPA ASSTQGPQPP PPQSLNLLSQ AQLQGQPLAP GGTQMKKKSG FQITSVTPAQ
     ISASISSNNS IAEDTESYDD LDESHTEDLS SSEILDVSLS RATDLGEPER SSSEETLNNF
     QEAETPGAVS PNQPHLPQPH LPHLPQQNVV INGNAHPHHL HHHHHPHHGH HLHHGHHHSS
     HAAVAGPSIP GGPPSSPVSR KLSTTGSSDG GVPVAPPPAV PSSGLPASVM TNIRTPSTTG
     SLAAGITVGV VSSQQQQQQQ QQPTVNTSRF RVVKLDSTSE PFKKGRWTCT EFYEKENAVP
     ATEGVAVNKV VETVKQTPTE ASSSERESTS GSSVSSSVST LSHYTESVGS GEMMGAPAVV
     APQQPPLPPA PPGLQGVALQ QLEFSSPAPQ SIAAVSMPQS ISQSQMSQVQ LQPQELSFQQ
     KQTLQPVPLQ ATMSAATGIQ PSPVSVVGIT AAVGQQPSVS SLAQPQLPYS QTAPPVQTPL
     PGAPPQQLQY GQQQPMVPAQ IAPGHGQPVT QNPTSEYVQQ QQQPIFQAAL SSGQSSSTGT
     GAGISVIPVA QAQGIQLPGQ PTAVQTQPAG AAGQPIGQAQ TAVSTVPTGG QIASIGQQAN
     IPTAVQQPST QVTPSVIQQG APPSSQVVLP APTGIIHQGV QTRASSLPQQ LVIAPQSTLV
     TVPPQPQGVE TVAQGVVSQQ LPTGSPLPSA STISVTNQVS SAAPSGMPSV PTNLVPPQNI
     AQPPATQNGS LVQSVSQSPL IATNINLPLA QQIPLSSTQF STQSLAQAIG SQMEDARRPA
     EPSLGGLPQT MSGDSGGMSA VSDGSSSSLA APASLFPLKV LPLTTPLVDG EDESSGASVV
     AIDNKIEQAM DLVKSHLMYA VREEVEVLKE QIKELIEKNS QLEQENNLLK TLASPEQLAQ
     FQAQLQTGSP PATTQPQGTT QPPAQPASQG SGSTA
//
ID   D3Z2J5_MOUSE            Unreviewed;      1025 AA.
AC   D3Z2J5;
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=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   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; AC132118; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC139377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00775787; -.
DR   Ensembl; ENSMUST00000134404; ENSMUSP00000121588; ENSMUSG00000029478.
DR   MGI; MGI:1337080; Ncor2.
DR   GeneTree; ENSGT00550000074554; -.
DR   Bgee; D3Z2J5; -.
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: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: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; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   PROSITE; PS51293; SANT; 1.
PE   4: Predicted;
KW   Nucleus.
SQ   SEQUENCE   1025 AA;  108869 MW;  BE07BD201157B515 CRC64;
     MFPENLAEGE TQMRGCLLEH GRNWSAIARM VGSKTVSQCK NFYFNYKKRQ NLDEILQQHK
     LKMPGPGLRH RASPAVTATV LSQEKERNAR RKKKKTPAAA SEETAFPPAA EDEEMEASGA
     SANEEELAEE AEASQASGNE VPRVGECSGP AAVNNSSDTE SVPSPRSEAT KDTGPKPTGT
     EALPAATQPP VPPPEEPAVA PAEPSPVPDA SGPPSPEPSP SPAAPPATVD KDEQEAPAAP
     APQTEDAKEQ KSEAEEIDVG KPEEPEASEE PPESVKSDHK EETEEEPEDK AKGTEAIETV
     SEAPLKVEEA GSKAAVTKGS SSGATQDSDS SATCSADEVD EPEGGDKGRL LSPRPSLLTP
     AGDPRASTSP QKPLDLKQLK QRAAAIPPIV TKVHEPPRED TVPPKPVPPV PPPTQHLQPE
     GDVSQQSGGS PRGKSRSPVP PAEKEAEKPA FFPAFPTEGP KLPTEPPRWS SGLPFPIPPR
     EVIKTSPHAA DPSAFSYTPP GHPLPLGLHD SARPVLPRPP ISNPPPLISS AKHPGVLERQ
     LGAISQGMSV QLRVPHSEHA KAPMGPLTMG LPLAVDPKKL APFSGVKQEQ LSPRGQAGPP
     ESLGVPTAQE TSVLRGTALG SATSGSITKG LPSTRAADGP SYRGSITHGT PADVLYKGTI
     SRIVGEDSPS RLDRAREDTL PKGHVIYEGK KGHVLSYEGG MSVSQCSKED GRSSSGPPHE
     TAAPKRTYDM MEGRVGRTVT SASIEGLMGR AIPEQHSPHL KEQHHIRGSI TQGIPRSYVE
     AQEDYLRREA KLLKREGTPP PPPPPRDLTE TYKPRPLDPL GPLKLKPTHE GVVATVKEAG
     RSIHEIPREE LRRTPELPLA PRPLKEGSIT QGTPLKYDSG APSTGTKKHD VRSIIGSPGR
     PFPALHPLDI MADARALERA CYEESLKSRS GTSSGAGGSI TRGAPVVVPE LGKPRQSPLT
     YEDHGAPFTS HLPRGSPVTT REPTPRLQEG SLLSSKASQD RKLTSTPREI AKSPHSTVPE
     HHPHP
//
ID   D3Z425_MOUSE            Unreviewed;       219 AA.
AC   D3Z425;
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=Spock1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; 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; AC142258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CT010428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00953746; -.
DR   Ensembl; ENSMUST00000080367; ENSMUSP00000079237; ENSMUSG00000056222.
DR   MGI; MGI:105371; Spock1.
DR   GeneTree; ENSGT00510000046429; -.
DR   OrthoDB; EOG4MSCZ5; -.
DR   Bgee; D3Z425; -.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR002350; Prot_inh_Kazal.
DR   InterPro; IPR011497; Prot_Inh_Kazal_2.
DR   InterPro; IPR019577; SPARC/Testican_Ca-bd-dom.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF07648; Kazal_2; 1.
DR   Pfam; PF10591; SPARC_Ca_bdg; 1.
DR   SMART; SM00280; KAZAL; 1.
PE   4: Predicted;
SQ   SEQUENCE   219 AA;  24675 MW;  9213D919CF7CC837 CRC64;
     MVCGSDGHTY TSKCKLEFHA CSTGKSLNSL CDGPCPCLPE PEPLKPKAEK SACTDKELRN
     LASRLKDWFG ALHEDANRVI KPTSSDPAQG RFDTSILPIC KDSLGWMFNK LDMNYDLLLD
     HSEINAIYLD KYEPCIKPLF NSCDSFKDGK LSNNEWCYCF QKPAGLPCQN EMNRIQKLSK
     GKSLLGTTLE NGTVPTRLSV HQFLLSLWRS SWVLPIHRQ
//
ID   D3Z4Y4_MOUSE            Unreviewed;       563 AA.
AC   D3Z4Y4;
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=Krt5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; 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 intermediate filament 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; AC104862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC120787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00470126; -.
DR   Ensembl; ENSMUST00000080158; ENSMUSP00000079053; ENSMUSG00000061527.
DR   MGI; MGI:96702; Krt5.
DR   GeneTree; ENSGT00560000076943; -.
DR   Bgee; D3Z4Y4; -.
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   3: Inferred from homology;
KW   Coiled coil; Intermediate filament.
SQ   SEQUENCE   563 AA;  60362 MW;  E5E5404D3D9B4D21 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 SSQGGMSFGS
     GGGSGSSVKF VSTTSSSRRS FKS
//
ID   D3Z7K1_MOUSE            Unreviewed;      4833 AA.
AC   D3Z7K1;
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=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 (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 C2 domain.
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   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AC125043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC125533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC144625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00225140; -.
DR   Ensembl; ENSMUST00000115309; ENSMUSP00000110964; ENSMUSG00000061601.
DR   MGI; MGI:1349390; Pclo.
DR   GeneTree; ENSGT00600000084489; -.
DR   OrthoDB; EOG495ZSJ; -.
DR   Bgee; D3Z7K1; -.
DR   GO; GO:0045202; C:synapse; IEA:InterPro.
DR   GO; GO:0005522; F:profilin binding; IDA:MGI.
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   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; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF05715; zf-piccolo; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 2.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   4: Predicted;
SQ   SEQUENCE   4833 AA;  525011 MW;  510E14572D1CA6B7 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
     PAKPQPQQPT 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 TGPHPSAPAK
     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 SVSGEILGQE 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 VQQLRIQPSK RRK
//
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.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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   -----------------------------------------------------------------------
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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   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.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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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   AIP_MOUSE               Reviewed;         330 AA.
AC   O08915; Q3UJM2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=AH receptor-interacting protein;
DE            Short=AIP;
DE   AltName: Full=Aryl-hydrocarbon receptor-interacting protein;
GN   Name=Aip;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=97238809; PubMed=9083006; DOI=10.1074/jbc.272.14.8912;
RA   Ma Q., Whitlock J.P. Jr.;
RT   "A novel cytoplasmic protein that interacts with the Ah receptor,
RT   contains tetratricopeptide repeat motifs, and augments the
RT   transcriptional response to 2,3,7,8-tetrachlorodibenzo-p-dioxin.";
RL   J. Biol. Chem. 272:8878-8884(1997).
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/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and 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 291-304, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
CC   -!- FUNCTION: May play a positive role in AHR-mediated (aromatic
CC       hydrocarbon receptor) signaling, possibly by influencing its
CC       receptivity for ligand and/or its nuclear targeting.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Contains 1 PPIase FKBP-type domain.
CC   -!- SIMILARITY: Contains 2 TPR repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U85489; AAB59009.1; -; mRNA.
DR   EMBL; AK146390; BAE27133.1; -; mRNA.
DR   EMBL; BC075614; AAH75614.1; -; mRNA.
DR   IPI; IPI00117178; -.
DR   RefSeq; NP_057875.1; NM_016666.2.
DR   UniGene; Mm.10433; -.
DR   ProteinModelPortal; O08915; -.
DR   SMR; O08915; 2-317.
DR   MINT; MINT-3374208; -.
DR   STRING; O08915; -.
DR   PhosphoSite; O08915; -.
DR   REPRODUCTION-2DPAGE; O08915; -.
DR   PRIDE; O08915; -.
DR   Ensembl; ENSMUST00000025767; ENSMUSP00000025767; ENSMUSG00000024847.
DR   Ensembl; ENSMUST00000117831; ENSMUSP00000113807; ENSMUSG00000024847.
DR   GeneID; 11632; -.
DR   KEGG; mmu:11632; -.
DR   UCSC; uc008fyp.1; mouse.
DR   CTD; 11632; -.
DR   MGI; MGI:109622; Aip.
DR   eggNOG; roNOG05585; -.
DR   GeneTree; ENSGT00390000001289; -.
DR   HOGENOM; HBG444299; -.
DR   HOVERGEN; HBG004198; -.
DR   InParanoid; O08915; -.
DR   OMA; ATFHYRT; -.
DR   PhylomeDB; O08915; -.
DR   NextBio; 279197; -.
DR   ArrayExpress; O08915; -.
DR   Bgee; O08915; -.
DR   CleanEx; MM_AIP; -.
DR   Genevestigator; O08915; -.
DR   GermOnline; ENSMUSG00000024847; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0003712; F:transcription cofactor activity; IPI:MGI.
DR   GO; GO:0051082; F:unfolded protein binding; ISS:HGNC.
DR   GO; GO:0022417; P:protein maturation by protein folding; ISS:HGNC.
DR   GO; GO:0006626; P:protein targeting to mitochondrion; ISS:HGNC.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IPI:MGI.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
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; PF00254; FKBP_C; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; FALSE_NEG.
DR   PROSITE; PS50005; TPR; 1.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW   Repeat; TPR repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    330       AH receptor-interacting protein.
FT                                /FTId=PRO_0000075340.
FT   DOMAIN       31    121       PPIase FKBP-type.
FT   REPEAT      179    212       TPR 1.
FT   REPEAT      265    298       TPR 2.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     248    248       Phosphotyrosine (By similarity).
SQ   SEQUENCE   330 AA;  37605 MW;  25C61AB65F9064F2 CRC64;
     MADLIARLRE DGIQKRVIQE GRGELPDFQD GTKATFHFRT LHSDNEGSVI DDSRTRGKPM
     ELIVGKKFKL PVWETIVCTM REGEIAQFLC DIKHVVLYPL VAKSLRNIAE GKDPLEGQRH
     CCGIAQMHEH SSLGHADLDA LQQNPQPLIF HIEMLKVESP GTYQQDPWAM TDEEKAKAVP
     VIHQEGNRLY REGQVKEAAA KYYDAIACLK NLQMKEQPGS PDWIQLDLQI TPLLLNYCQC
     KLVAQEYYEV LDHCSSILNK YDDNVKAYFK RGKAHAAVWN AQEAQADFAK VLELDPALAP
     VVSRELRALE TRIRQKDEED KARFRGIFSH
//
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   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   -----------------------------------------------------------------------
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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   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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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   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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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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   Distributed under the Creative Commons Attribution-NoDerivs License
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   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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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   ACK1_MOUSE              Reviewed;        1055 AA.
AC   O54967; Q0Z844; Q8C2U0; Q8K0K4;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=Activated CDC42 kinase 1;
DE            Short=ACK-1;
DE            EC=2.7.10.2;
DE   AltName: Full=Non-receptor protein tyrosine kinase Ack;
DE   AltName: Full=Tyrosine kinase non-receptor protein 2;
GN   Name=Tnk2; Synonyms=Ack1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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, AND MUTAGENESIS OF LYS-158; TRP-424 AND HIS-464.
RX   PubMed=16777958; DOI=10.1073/pnas.0603714103;
RA   Galisteo M.L., Yang Y., Urena J., Schlessinger J.;
RT   "Activation of the nonreceptor protein tyrosine kinase Ack by multiple
RT   extracellular stimuli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9796-9801(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RA   Her J.-H., Bolen J.B.;
RT   "The protein tyrosine kinase Ack is associated with and activated in
RT   vivo by CDC42Hs.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 121-1055 (ISOFORM 3).
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   INTERACTION WITH CDC42, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=16052498; DOI=10.1002/cne.20656;
RA   Urena J.M., La Torre A., Martinez A., Lowenstein E., Franco N.,
RA   Winsky-Sommerer R., Fontana X., Casaroli-Marano R., Ibanez-Sabio M.A.,
RA   Pascual M., Del Rio J.A., de Lecea L., Soriano E.;
RT   "Expression, synaptic localization, and developmental regulation of
RT   Ack1/Pyk1, a cytoplasmic tyrosine kinase highly expressed in the
RT   developing and adult brain.";
RL   J. Comp. Neurol. 490:119-132(2005).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18477472; DOI=10.1016/j.bbrc.2008.05.016;
RA   Eley L., Moochhala S.H., Simms R., Hildebrandt F., Sayer J.A.;
RT   "Nephrocystin-1 interacts directly with Ack1 and is expressed in human
RT   collecting duct.";
RL   Biochem. Biophys. Res. Commun. 371:877-882(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-533 AND TYR-874, 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   FUNCTION, AND INTERACTION WITH UBA.
RX   PubMed=17182860; DOI=10.1091/mbc.E06-02-0142;
RA   Shen F., Lin Q., Gu Y., Childress C., Yang W.;
RT   "Activated Cdc42-associated kinase 1 is a component of EGF receptor
RT   signaling complex and regulates EGF receptor degradation.";
RL   Mol. Biol. Cell 18:732-742(2007).
CC   -!- FUNCTION: Downstream effector of CDC42 which mediates CDC42-
CC       dependent cell migration via phosphorylation of BCAR1. Binds to
CC       both poly- and mono-ubiquitin and regulates ligand-induced
CC       degradation of EGFR. Participates in clathrin-mediated
CC       endocytosis. May be involved both in adult synaptic function and
CC       plasticity and in brain development.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: The SH3 domain appears to play an
CC       autoinhibitory role.
CC   -!- SUBUNIT: Interacts with CDC42. Interacts with activated CSPG4 (By
CC       similarity). Interacts with AR (By similarity). Interacts with
CC       WWOX (By similarity). Interacts with MERTK (activated); stimulates
CC       autophosphorylation (By similarity). May interact (phosphorylated)
CC       with HSP90AB1; maintains kinase activity. Interacts with NPHP1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane. Cell junction, adherens
CC       junction.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O54967-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O54967-2; Sequence=VSP_008657, VSP_008658;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=O54967-3; Sequence=VSP_008657;
CC   -!- TISSUE SPECIFICITY: Ubiquitously present in all tisssues tested.
CC       Highly expressed in the hippocampus, neocortex, and cerebellum,
CC       both at dendritic spines and presynaptic axon terminals. Levels
CC       are strongly up-regulated by increased neural activity.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed at E14-E16 in the forebrain,
CC       in the proliferative ventricular zone of the neocortex and
CC       hippocampus, and in the cortical and hippocampal plates. Also
CC       observed in the septal area, the ganglionic eminence, and in the
CC       dorsal thalamus and hypothalamus. In the hindbrain, expressed in
CC       many nuclei in the brain stem and in the cerebellar anlage,
CC       external granule cell layer, in Purkinje cells and the deep
CC       cerebellar nuclei.
CC   -!- PTM: Autophosphorylation regulates kinase activity (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family.
CC   -!- SIMILARITY: Contains 1 CRIB domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH31168.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part;
CC   -----------------------------------------------------------------------
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DR   EMBL; DQ666696; ABG46266.1; -; mRNA.
DR   EMBL; AF037260; AAC04786.1; -; mRNA.
DR   EMBL; BC031168; AAH31168.1; ALT_SEQ; mRNA.
DR   EMBL; BC052421; AAH52421.1; -; mRNA.
DR   EMBL; AK087965; BAC40063.1; -; mRNA.
DR   IPI; IPI00119965; -.
DR   IPI; IPI00377737; -.
DR   IPI; IPI00874745; -.
DR   RefSeq; NP_001103617.1; NM_001110147.1.
DR   RefSeq; NP_058068.2; NM_016788.3.
DR   UniGene; Mm.251115; -.
DR   ProteinModelPortal; O54967; -.
DR   SMR; O54967; 117-390, 400-445, 447-489, 1011-1049.
DR   STRING; O54967; -.
DR   PhosphoSite; O54967; -.
DR   PRIDE; O54967; -.
DR   Ensembl; ENSMUST00000023480; ENSMUSP00000023480; ENSMUSG00000022791.
DR   Ensembl; ENSMUST00000115121; ENSMUSP00000110774; ENSMUSG00000022791.
DR   Ensembl; ENSMUST00000115122; ENSMUSP00000110775; ENSMUSG00000022791.
DR   Ensembl; ENSMUST00000115124; ENSMUSP00000110777; ENSMUSG00000022791.
DR   GeneID; 51789; -.
DR   KEGG; mmu:51789; -.
DR   UCSC; uc007yzc.1; mouse.
DR   UCSC; uc007yzd.1; mouse.
DR   UCSC; uc007yze.1; mouse.
DR   CTD; 51789; -.
DR   MGI; MGI:1858308; Tnk2.
DR   eggNOG; roNOG11609; -.
DR   GeneTree; ENSGT00600000084141; -.
DR   HOGENOM; HBG445655; -.
DR   HOVERGEN; HBG100429; -.
DR   InParanoid; O54967; -.
DR   OrthoDB; EOG4Q58NQ; -.
DR   BRENDA; 2.7.10.2; 244.
DR   NextBio; 308016; -.
DR   ArrayExpress; O54967; -.
DR   Bgee; O54967; -.
DR   CleanEx; MM_TNK2; -.
DR   Genevestigator; O54967; -.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0030426; C:growth cone; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; 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:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR015116; GTPase_binding.
DR   InterPro; IPR021619; Inhibitor_Mig-6.
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; IPR001452; SH3_domain.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   InterPro; IPR000449; UBA/transl_elong_EF1B_N.
DR   Pfam; PF09027; GTPase_binding; 1.
DR   Pfam; PF11555; Inhibitor_Mig-6; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF00627; UBA; 1.
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; PS50108; CRIB; FALSE_NEG.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell junction; Cell membrane;
KW   Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; SH3 domain; Transferase; Tyrosine-protein kinase.
FT   CHAIN         1   1055       Activated CDC42 kinase 1.
FT                                /FTId=PRO_0000088059.
FT   DOMAIN      126    385       Protein kinase.
FT   DOMAIN      386    448       SH3.
FT   DOMAIN      454    466       CRIB.
FT   NP_BIND     132    140       ATP (By similarity).
FT   COMPBIAS    517    950       Pro-rich.
FT   ACT_SITE    252    252       Proton acceptor (By similarity).
FT   BINDING     158    158       ATP.
FT   MOD_RES     284    284       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     532    532       Phosphothreonine (By similarity).
FT   MOD_RES     533    533       Phosphotyrosine.
FT   MOD_RES     743    743       Phosphoserine (By similarity).
FT   MOD_RES     800    800       Phosphoserine (By similarity).
FT   MOD_RES     842    842       Phosphotyrosine (By similarity).
FT   MOD_RES     874    874       Phosphotyrosine.
FT   MOD_RES     875    875       Phosphotyrosine (By similarity).
FT   MOD_RES     896    896       Phosphoserine (By similarity).
FT   MOD_RES     940    940       Phosphothreonine (By similarity).
FT   VAR_SEQ     515    531       REPPPRPPQPAIFTQKT -> KP (in isoform 2 and
FT                                isoform 3).
FT                                /FTId=VSP_008657.
FT   VAR_SEQ     980   1011       Missing (in isoform 2).
FT                                /FTId=VSP_008658.
FT   MUTAGEN     158    158       K->A: Loss of kinase activity.
FT   MUTAGEN     424    424       W->K: Increase in autophosphorylation
FT                                activity.
FT   MUTAGEN     464    464       H->D: Loss of CDC42-binding and
FT                                impairment of autophosphorylation.
FT   CONFLICT     57     58       RR -> SG (in Ref. 2; AAC04786).
FT   CONFLICT    531    531       T -> P (in Ref. 1; ABG46266).
FT   CONFLICT    574    574       K -> E (in Ref. 1; ABG46266).
FT   CONFLICT    649    649       A -> V (in Ref. 2; AAC04786).
FT   CONFLICT    818    818       L -> V (in Ref. 3; BAC40063).
FT   CONFLICT    955    955       A -> T (in Ref. 2; AAH52421 and 3;
FT                                BAC40063).
SQ   SEQUENCE   1055 AA;  116975 MW;  4A029C67C350B89A CRC64;
     MQPEEGTGWL LELLSEVQLQ QYFLRLRDDL NITRLSHFEY VKNEDLEKIG MGRPGQRRLW
     EAVKRRKAMC KRKSWMSKVF SGKRLEAEFP SQHSQSTFRK PSPTPGSLPG EGTLQSLTCL
     IGEKDLRLLE KLGDGSFGVV RRGEWDAPAG KTVSVAVKCL KPDVLSQPEA MDDFIREVNA
     MHSLDHRNLI RLYGVVLTLP MKMVTELAPL GSLLDRLRKH QGHFLLGTLS RYAVQVAEGM
     AYLESKRFIH RDLAARNLLL ATRDLVKIGD FGLMRALPQN DDHYVMQEHR KVPFAWCAPE
     SLKTRTFSHA SDTWMFGVTL WEMFTYGQEP WIGLNGSQIL HKIDKEGERL PRPEDCPQDI
     YNVMVQCWAH KPEDRPTFVA LRDFLLEAQP TDMRALQDFE EPDKLHIQMN DVITVIEGRA
     ENYWWRGQNT RTLCVGPFPR NVVTSVAGLS AQDISQPLQN SFIHTGHGDS DPRHCWGFPD
     RIDELYLGNP MDPPDLLSVE LSTSRPTQHL GRVKREPPPR PPQPAIFTQK TTYDPVSEDP
     DPLSSDFKRL GLRKPALPRG LWLAKPSARV PGTKADRSSG GEVTLIDFGE EPVVPTPRPC
     APSLAQLAMD ACSLLDKTPP QSPTRALPRP LHPTPVVDWD ARPLPPPPAY DDVAQDEDDF
     EVCSINSTLV GAGLPAGPSQ GETNYAFVPE QAQMPPALED NLFLPPQGGG KPPSSVQTAE
     IFQALQQECM RQLQVPTGQL TPSPTPGGDD KPQVPPRVPI PPRPTRPRVE LSPAPSGEEE
     TSRWPGPASP PRVPPREPLS PQGSRTPSPL VPPGSSPLPH RLSSSPGKTM PTTQSFASDP
     KYATPQVIQA PGPRAGPCIL PIVRDGRKVS STHYYLLPER PPYLERYQRF LREAQSPEEP
     AALPVPPLLP PPSTPAPAAP TATVRPMPQA APDPKANFST NNSNPGARPP SLRAAARLPQ
     RGCPGDGQEA ARPADKVQML QAMVHGVTTE ECQAALQSHS WSVQRAAQYL KVEQLFGLGL
     RPRVECHKVL EMFDWNLEQA GCHLLGSCGP AHHKR
//
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   FKBP7_MOUSE             Reviewed;         218 AA.
AC   O54998;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP7;
DE            Short=PPIase FKBP7;
DE            EC=5.2.1.8;
DE   AltName: Full=23 kDa FK506-binding protein;
DE            Short=23 kDa FKBP;
DE            Short=FKBP-23;
DE   AltName: Full=FK506-binding protein 7;
DE            Short=FKBP-7;
DE   AltName: Full=Rotamase;
DE   Flags: Precursor;
GN   Name=Fkbp7; Synonyms=Fkbp23;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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   DEVELOPMENTAL STAGE, GLYCOSYLATION, AND CALCIUM-BINDING.
RC   STRAIN=NIH Swiss; TISSUE=Embryonic heart;
RX   MEDLINE=99026129; PubMed=9806833; DOI=10.1006/geno.1998.5571;
RA   Nakamura T., Yabe D., Kanazawa N., Tashiro K., Sasayama S., Honjo T.;
RT   "Molecular cloning, characterization, and chromosomal localization of
RT   FKBP23, a novel FK506-binding protein with Ca2+-binding ability.";
RL   Genomics 54:89-98(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).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins during
CC       protein synthesis.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC   -!- TISSUE SPECIFICITY: Expressed at highest levels in heart, lung and
CC       testis. Weakly expressed in kidney and lymph node. Little or no
CC       expression detected in brain, thymus, spleen and liver.
CC   -!- DEVELOPMENTAL STAGE: Expression begins at embryonic day 8.5.
CC   -!- PTM: Glycosylated.
CC   -!- MISCELLANEOUS: Binds calcium.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
CC   -!- SIMILARITY: Contains 1 PPIase FKBP-type domain.
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DR   EMBL; AF040252; AAC79959.1; -; mRNA.
DR   EMBL; BC032961; AAH32961.1; -; mRNA.
DR   IPI; IPI00120073; -.
DR   RefSeq; NP_034352.1; NM_010222.2.
DR   UniGene; Mm.24720; -.
DR   ProteinModelPortal; O54998; -.
DR   SMR; O54998; 41-143, 147-211.
DR   STRING; O54998; -.
DR   PRIDE; O54998; -.
DR   Ensembl; ENSMUST00000002809; ENSMUSP00000002809; ENSMUSG00000002732.
DR   GeneID; 14231; -.
DR   KEGG; mmu:14231; -.
DR   UCSC; uc008kfh.1; mouse.
DR   CTD; 14231; -.
DR   MGI; MGI:1336879; Fkbp7.
DR   eggNOG; roNOG15052; -.
DR   HOGENOM; HBG731200; -.
DR   HOVERGEN; HBG051623; -.
DR   InParanoid; O54998; -.
DR   OMA; AVTKGPR; -.
DR   OrthoDB; EOG4G7BZZ; -.
DR   PhylomeDB; O54998; -.
DR   BRENDA; 5.2.1.8; 244.
DR   NextBio; 285503; -.
DR   ArrayExpress; O54998; -.
DR   Bgee; O54998; -.
DR   CleanEx; MM_FKBP7; -.
DR   Genevestigator; O54998; -.
DR   GermOnline; ENSMUSG00000002732; Mus musculus.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion 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:0006457; P:protein folding; 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; IPR001179; PPIase_FKBP_dom.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   SMART; SM00054; EFh; 2.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   1: Evidence at protein level;
KW   Calcium; Endoplasmic reticulum; Glycoprotein; Isomerase; Repeat;
KW   Rotamase; Signal.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20    218       Peptidyl-prolyl cis-trans isomerase
FT                                FKBP7.
FT                                /FTId=PRO_0000025514.
FT   DOMAIN       49    141       PPIase FKBP-type.
FT   DOMAIN      141    176       EF-hand 1.
FT   DOMAIN      185    218       EF-hand 2.
FT   CA_BIND     154    165       1 (Potential).
FT   CA_BIND     198    209       2 (Potential).
FT   MOTIF       215    218       Prevents secretion from ER (Potential).
FT   CARBOHYD     41     41       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    128    128       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   218 AA;  24913 MW;  DB0AE509E60EEEBA CRC64;
     MNLLFRLAVF LSLWCCSDAQ GQTKEESTEE VKIEVLHRPE NCSKTSRKGD LLNAHYDGYL
     AKDGSKFYCS RTQDEGHPKW FVLGVGHVIK GLDIAMMDMC PGEKRKVIIP PSFAYGKEGY
     AEGKIPPNAT LMFEIELYAV TKGPRSIETF KQIDTDNDRQ LSKAEIELYL QKDFEKDANP
     RDKSYQKAVL EDIFKKNDHN GDGFISPKEY NVHQHDEL
//
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;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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.
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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   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.
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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   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   PGAM2_MOUSE             Reviewed;         253 AA.
AC   O70250;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 100.
DE   RecName: Full=Phosphoglycerate mutase 2;
DE            EC=3.1.3.13;
DE            EC=5.4.2.1;
DE            EC=5.4.2.4;
DE   AltName: Full=BPG-dependent PGAM 2;
DE   AltName: Full=Muscle-specific phosphoglycerate mutase;
DE   AltName: Full=Phosphoglycerate mutase isozyme M;
DE            Short=PGAM-M;
GN   Name=Pgam2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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 G., Yu L., Tu Q., Jiang Y., Fan Y., Zhao S.;
RT   "Cloning and expression analysis of a mouse gene coding
RT   phosphoglycerate mutase muscle-specific subunit.";
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=21147938; PubMed=11250083; DOI=10.1016/S0378-1119(00)00597-7;
RA   Zhang J., Yu L., Fu Q., Gao J., Xie Y., Chen J., Zhang P., Liu Q.,
RA   Zhao S.;
RT   "Mouse phosphoglycerate mutase M and B isozymes: cDNA cloning, enzyme
RT   activity assay and mapping.";
RL   Gene 264:273-279(2001).
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 TYR-92, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., 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; AF029843; AAC13263.1; -; mRNA.
DR   EMBL; AF317587; AAK06662.1; -; Genomic_DNA.
DR   EMBL; BC010750; AAH10750.1; -; mRNA.
DR   IPI; IPI00230706; -.
DR   RefSeq; NP_061358.1; NM_018870.3.
DR   UniGene; Mm.219627; -.
DR   ProteinModelPortal; O70250; -.
DR   SMR; O70250; 4-245.
DR   STRING; O70250; -.
DR   PhosphoSite; O70250; -.
DR   SWISS-2DPAGE; O70250; -.
DR   PRIDE; O70250; -.
DR   Ensembl; ENSMUST00000020768; ENSMUSP00000020768; ENSMUSG00000020475.
DR   GeneID; 56012; -.
DR   KEGG; mmu:56012; -.
DR   UCSC; uc007hxe.1; mouse.
DR   CTD; 56012; -.
DR   MGI; MGI:1933118; Pgam2.
DR   eggNOG; roNOG12297; -.
DR   HOGENOM; HBG658938; -.
DR   HOVERGEN; HBG027528; -.
DR   InParanoid; O70250; -.
DR   OMA; SDAAIME; -.
DR   OrthoDB; EOG4MCX10; -.
DR   PhylomeDB; O70250; -.
DR   BRENDA; 3.1.3.13; 244.
DR   BRENDA; 5.4.2.1; 244.
DR   BRENDA; 5.4.2.4; 244.
DR   NextBio; 311738; -.
DR   ArrayExpress; O70250; -.
DR   Bgee; O70250; -.
DR   CleanEx; MM_PGAM2; -.
DR   Genevestigator; O70250; -.
DR   GermOnline; ENSMUSG00000020475; 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: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   Glycolysis; Hydrolase; Isomerase; Isopeptide bond; Phosphoprotein;
KW   Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    253       Phosphoglycerate mutase 2.
FT                                /FTId=PRO_0000179830.
FT   COMPBIAS    122    125       Poly-Pro.
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      92     92       Phosphotyrosine.
FT   CROSSLNK    195    195       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
SQ   SEQUENCE   253 AA;  28827 MW;  477AF9EC59A15B86 CRC64;
     MTTHRLVMVR HGESLWNQEN RFCGWFDAEL SEKGAEEAKR GATAIKDAKI EFDICYTSVL
     KRAIRTLWTI LDVTDQMWVP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD
     TPPPPMDEKH NYYTSISKDR RYAGLKPEEL PTCESLKDTI ARALPFWNEE IAPKIKAGQR
     VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL DQNLKPTKPM RFLGDEETVR
     KAMEAVAAQG KAK
//
ID   SGCE_MOUSE              Reviewed;         437 AA.
AC   O70258; Q921G2;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Epsilon-sarcoglycan;
DE            Short=Epsilon-SG;
GN   Name=Sgce;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; 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=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 [MRNA] OF 11-437 (ISOFORM 1).
RC   TISSUE=Lung;
RX   MEDLINE=98070432; PubMed=9405466; DOI=10.1074/jbc.272.51.32534;
RA   Ettinger A.J., Feng G., Sanes J.R.;
RT   "Epsilon-sarcoglycan, a broadly expressed homologue of the gene
RT   mutated in limb-girdle muscular dystrophy 2D.";
RL   J. Biol. Chem. 272:32534-32538(1997).
RN   [3]
RP   ERRATUM.
RA   Ettinger A.J., Feng G., Sanes J.R.;
RL   J. Biol. Chem. 273:19922-19922(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-437 (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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 27-437 (ISOFORM 2).
RC   TISSUE=Lung;
RX   MEDLINE=99419091; PubMed=10488149; DOI=10.1074/jbc.274.39.27989;
RA   Straub V., Ettinger A.J., Durbeej M., Venzke D.P., Cutshall S.,
RA   Sanes J.R., Campbell K.P.;
RT   "Epsilon-sarcoglycan replaces alpha-sarcoglycan in smooth muscle to
RT   form a unique dystrophin-glycoprotein complex.";
RL   J. Biol. Chem. 274:27989-27996(1999).
CC   -!- FUNCTION: Component of the sarcoglycan complex, a subcomplex of
CC       the dystrophin-glycoprotein complex which forms a link between the
CC       F-actin cytoskeleton and the extracellular matrix.
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Single-pass
CC       membrane protein (Potential). Cytoplasm, cytoskeleton (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O70258-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O70258-2; Sequence=VSP_006019;
CC   -!- TISSUE SPECIFICITY: Identified in all tissues tested. Expression
CC       highest in lung and placenta, moderate in brain, heart and
CC       skeletal muscle, low in kidney and liver. Also detected in embryo.
CC   -!- SIMILARITY: Belongs to the sarcoglycan alpha/epsilon family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC14020.1; Type=Erroneous initiation;
CC       Sequence=AAH12665.1; Type=Erroneous initiation;
CC       Sequence=BAC36184.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; BC012665; AAH12665.1; ALT_INIT; mRNA.
DR   EMBL; AF031919; AAC14020.1; ALT_INIT; mRNA.
DR   EMBL; AK076102; BAC36184.1; ALT_INIT; mRNA.
DR   EMBL; AF103877; AAF21895.1; -; mRNA.
DR   IPI; IPI00750388; -.
DR   IPI; IPI00858145; -.
DR   RefSeq; NP_001123660.1; NM_001130188.1.
DR   RefSeq; NP_001123661.1; NM_001130189.1.
DR   RefSeq; NP_001123662.1; NM_001130190.1.
DR   RefSeq; NP_035490.3; NM_011360.3.
DR   UniGene; Mm.8739; -.
DR   STRING; O70258; -.
DR   PhosphoSite; O70258; -.
DR   Ensembl; ENSMUST00000115577; ENSMUSP00000111240; ENSMUSG00000004631.
DR   Ensembl; ENSMUST00000115579; ENSMUSP00000111242; ENSMUSG00000004631.
DR   GeneID; 20392; -.
DR   KEGG; mmu:20392; -.
DR   UCSC; uc009avp.1; mouse.
DR   UCSC; uc009avq.1; mouse.
DR   CTD; 20392; -.
DR   MGI; MGI:1329042; Sgce.
DR   eggNOG; roNOG07796; -.
DR   GeneTree; ENSGT00390000005672; -.
DR   HOVERGEN; HBG006891; -.
DR   OrthoDB; EOG46WZ8J; -.
DR   ArrayExpress; O70258; -.
DR   Bgee; O70258; -.
DR   CleanEx; MM_SGCE; -.
DR   Genevestigator; O70258; -.
DR   GermOnline; ENSMUSG00000004631; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:MGI.
DR   GO; GO:0016012; C:sarcoglycan complex; IEA:InterPro.
DR   GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   InterPro; IPR006644; Cadg.
DR   InterPro; IPR008908; Sarcoglycan_2.
DR   PANTHER; PTHR10132; Sarcoglycan_2; 1.
DR   Pfam; PF05510; Sarcoglycan_2; 1.
DR   SMART; SM00736; CADG; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Cytoplasm; Cytoskeleton;
KW   Glycoprotein; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    437       Epsilon-sarcoglycan.
FT                                /FTId=PRO_0000031678.
FT   TOPO_DOM      1    317       Extracellular (Potential).
FT   TRANSMEM    318    338       Helical; (Potential).
FT   TOPO_DOM    339    437       Cytoplasmic (Potential).
FT   COMPBIAS    235    341       Cys-rich.
FT   CARBOHYD    200    200       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ      36     36       T -> TAFLLSCADGINGTVNWKTKQASSFSISRKLAAGKK
FT                                D (in isoform 2).
FT                                /FTId=VSP_006019.
FT   CONFLICT    401    401       T -> M (in Ref. 1; AAH12665).
SQ   SEQUENCE   437 AA;  49736 MW;  A294007261593637 CRC64;
     MLLFWWWELG DPCAWTGKGR GTLKMSPATT GTFLLTVYTL FSKVHSDRNV YPSAGVLFVH
     VLEREYFKGE FPPYPKPGEV SNDPITFNTN LMGYPDRPGW LRYIQRTPYS DGVLYGSPTA
     ENVGKPTIIE ITAYNRRTFE TARHNLIINI MSAEEFPLPY QAEFFIKNMN VEEMLASEVL
     GDFLGAVKNV WQPERLNAIN ITSALDRGGR VPLPINDMKE GVYVMVGADV AFSSCLREVE
     NPQNQLRCSQ EMEPVITCDK KFRTHFHIDW CKISLVDKTK QVSTYQEVVR GEGILPDGGE
     YKPPSDSLKS RDYYTDFLVT LAVPSAVALV LFLILAYIMC CRREGVEKRD MQTPDIQLVH
     HSSIQKSTKE LRDMSKNREI AWPLSTLPVF HPVTGEVIPP THTDNYDSTN MPLMQAQQNL
     PHQTQIPQPQ TTGKWYP
//
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.
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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   TM131_MOUSE             Reviewed;        1829 AA.
AC   O70472; Q8CHH3;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Transmembrane protein 131;
DE   AltName: Full=Protein RW1;
GN   Name=Tmem131; Synonyms=D1Bwg0491e, Kiaa0257, Rw1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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=10996388; DOI=10.1016/S0165-2478(00)00239-X;
RA   Tscharke D.C., Wilkinson R., Simmons A.;
RT   "Use of mRNA differential display to study the action of lymphocyte
RT   subsets in vivo and application to a murine model of herpes simplex
RT   virus infection.";
RL   Immunol. Lett. 74:127-132(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 81-1829.
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1570, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.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 immune response to viral
CC       infection.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the TMEM131 family.
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DR   EMBL; AF060565; AAC15232.1; -; mRNA.
DR   EMBL; AB093221; BAC41405.1; -; mRNA.
DR   IPI; IPI00118333; -.
DR   PIR; T14280; T14280.
DR   RefSeq; NP_061360.2; NM_018872.2.
DR   UniGene; Mm.186943; -.
DR   ProteinModelPortal; O70472; -.
DR   STRING; O70472; -.
DR   PhosphoSite; O70472; -.
DR   PRIDE; O70472; -.
DR   Ensembl; ENSMUST00000027290; ENSMUSP00000027290; ENSMUSG00000026116.
DR   GeneID; 56030; -.
DR   KEGG; mmu:56030; -.
DR   CTD; 56030; -.
DR   MGI; MGI:1927110; Tmem131.
DR   HOGENOM; HBG446614; -.
DR   HOVERGEN; HBG017768; -.
DR   InParanoid; O70472; -.
DR   OrthoDB; EOG4TMR16; -.
DR   NextBio; 311784; -.
DR   ArrayExpress; O70472; -.
DR   Bgee; O70472; -.
DR   CleanEx; MM_TMEM131; -.
DR   Genevestigator; O70472; -.
DR   GermOnline; ENSMUSG00000026116; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR022113; DUF3651_TMEM131.
DR   InterPro; IPR008962; PapD-like.
DR   Gene3D; G3DSA:2.60.40.360; MSP; 2.
DR   Pfam; PF12371; DUF3651; 3.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1   1829       Transmembrane protein 131.
FT                                /FTId=PRO_0000097539.
FT   TRANSMEM   1041   1061       Helical; (Potential).
FT   TRANSMEM   1068   1088       Helical; (Potential).
FT   COMPBIAS   1254   1280       Pro-rich.
FT   COMPBIAS   1565   1776       Ser-rich.
FT   MOD_RES    1284   1284       Phosphoserine (By similarity).
FT   MOD_RES    1293   1293       Phosphoserine (By similarity).
FT   MOD_RES    1570   1570       Phosphoserine.
FT   MOD_RES    1809   1809       Phosphoserine (By similarity).
FT   CONFLICT    440    440       A -> V (in Ref. 2; BAC41405).
FT   CONFLICT    702    702       R -> C (in Ref. 2; BAC41405).
FT   CONFLICT    728    728       N -> D (in Ref. 2; BAC41405).
FT   CONFLICT    887    887       S -> F (in Ref. 2; BAC41405).
FT   CONFLICT   1742   1742       S -> R (in Ref. 2; BAC41405).
SQ   SEQUENCE   1829 AA;  200511 MW;  D0B3E209257AFAE9 CRC64;
     MNASFAARAE KEAFIQSESI IEVLRFDDGG LLQTETTLGL GSYQQKSISL YRGNCRPIRF
     EPPMLDFHEQ PVGMPKMEKV YLHNPSSEET ITLVSISATT SHFHASFFQN RKILPGGNTS
     FDVVFLARVV GNVENTLFIN TSNHGVFTYQ VFGVGVPNPY RLRPFLGARV PVNSSFSPII
     NIHNPHSEPL QVVEMYSSGG DLHLELPTGQ QGGTRKLWEI PPYETKGVMR ASFSSREADN
     HTAFIRIKTN ASDSTEFIIL PVEVEVTTAP GIYSSTEMLD FGTLRTQDLP KVLNLHLLNS
     GTKDVPITSV RPTPQNDAIT VHFKPVTLKA SESKYTKVAS ISFDASRAKK PSQFSGKITV
     KAKEKSYSKL EIPYQAEVLD GYLGFDHAAT LFHIQDSPAD PVERPIYLTN TFSFAILIHD
     VLLPEEARIM FQVHNFSQPA LILPNESGYI FTLFFMPSTS SMHIDNNILL VTNASKFHLP
     VRVYTGFLDY FVLPPKIEER FIDFGVLSAT EASSILFAII NSNPIELAIK SWHIIGDGLS
     IELVATERGN RSTVIASLPE LERSSLPDQS PVTLASGHFA VFRVKLTAKK LEGVHDGAIQ
     ITTDYEILTI PVKAVIAVGS LTCFPKHMVL PPSFPGKIVH QSLNIMNSFS QKVKIQQIRS
     LSEDVRFYYK RLRGNREDLE PGKKSKIANI YFDPGLQCGD HRYIGLPFLS KSEPKVQPGV
     AMQEDLWNAD WDAHQSLFKA WMGIKENAGH RLNAMFEVNT DLQKNIVSKV SAELSWPSVL
     SSPRLLKFPL TNTNCSSEEE ISLENPADVP VYVQFIPLAL YSNPSVFADK LVSRFNLSKV
     AKLDLRTLEF QVYRNSAHPL QSPTGFTEGL SRHFILNLIL KPGEKKSVKV KFTPLHNRTV
     SSLIIVRNNL TVMDAVMVQG QGTTENLRVA GKLPGPGSSL RFKITEALLK DCIDRLKLRE
     PNFTLKRTFK VENTGQLEIR VXTIEISGYA CEGYGFKVVN CQEFALSANA SRDIVILFTP
     DFTASRVIRE LKFVTSSGSE FVFVLNASLP YHMLAACAEA LPRPNWELAL YIIISGVMSA
     LFLLVIGTAY LEAQGIWEPF RRRLSFEASN PPFDVGRPFD LRRIVGISSE GNLNTLGCEH
     SHGRGFYSNA SSRPGTGSHR QCGTSVHPHS SHGSKNSADV DNVRTRNSSS MSSRTSPQAA
     ASQSTSKTSP LVSETAAATQ GHTASRKSRG AKQGQHSSQH HSHSHSPLEQ HSQPPPPVPQ
     HQEPPPERLS PAPLTHPSHP ERASTTRHSS EDSDITSLIE AMDKDFDHHD SSPLDVFTEQ
     PPSPMSKSKG KGKSLQQRKA KPPKKQEEKE KRGKGKPQED ELKDALADDD SSSTTTETSN
     PDTEPLLRED TEKHKGRPAV PEKQESELSQ GKPKSKKLLN AKKEIPTDVK GSSFELPYTP
     SLENKQRRNL PTKIPLPTTL ASGSKSRNPP KTKGTNKLVE NRPVALSKFL PSSQELGNTS
     SSEGEKDSPP PEWDAVPVHK PSSSTDSLYK LSLQTLNADI FLKQRQTSPT PASPSLPTAP
     CPFTSRGSYS SVVNSSGSDT KAKQTSSSKS KLTKAASLPG KNGNPTFAAV AAGYDKSPGG
     NGFAKISSNK SDFSSSLGIS HIPVDSDGSD SSGLWSPVSN PNSPDFTPLN SFSAFGNSFN
     LTGAVFSKLS RSCSQSSQRS WNEFNSGPSY LWDSPATDPS PSWPASSSSP THTATSILGN
     SSGLWSTTPF SSSIWSSNIN SNLPFSTPTN ALSSISLMGT ENSAAAHTPS ASGPADDLGQ
     TYNPWRIWSP TVGRRSSDPW SNSHFPHEN
//
ID   KDM6A_MOUSE             Reviewed;        1401 AA.
AC   O70546; A2AID2; Q6DI80; Q7TSG4;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Lysine-specific demethylase 6A;
DE            EC=1.14.11.-;
DE   AltName: Full=Histone demethylase UTX;
DE   AltName: Full=Ubiquitously transcribed TPR protein on the X chromosome;
DE   AltName: Full=Ubiquitously transcribed X chromosome tetratricopeptide repeat protein;
GN   Name=Kdm6a; Synonyms=Utx;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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 255-1401 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic germ cell, 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   NUCLEOTIDE SEQUENCE [MRNA] OF 69-1401 (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Embryo;
RX   MEDLINE=98167860; PubMed=9499428; DOI=10.1093/hmg/7.4.737;
RA   Greenfield A., Carrel L., Pennisi D., Phillippe C., Quaderi N.,
RA   Siggers P., Steiner K., Tam P.P.L., Monaco A.P., Willard H.F.,
RA   Koopman P.;
RT   "The UTX gene escapes X inactivation in mice and humans.";
RL   Hum. Mol. Genet. 7:737-742(1998).
RN   [4]
RP   INTERACTION WITH TLE1.
RX   MEDLINE=99072804; PubMed=9854018; DOI=10.1042/0264-6021:3370013;
RA   Grbavec D., Lo R., Liu Y., Greenfield A., Stifani S.;
RT   "Groucho/transducin-like enhancer of split (TLE) family members
RT   interact with the yeast transcriptional co-repressor SSN6 and
RT   mammalian SSN6-related proteins: implications for evolutionary
RT   conservation of transcription repression mechanisms.";
RL   Biochem. J. 337:13-17(1999).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-829, 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-1061, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., 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 demethylase that specifically demethylates 'Lys-
CC       27' of histone H3, thereby playing a central role in histone code.
CC       Demethylates trimethylated and dimethylated but not monomethylated
CC       H3 'Lys-27'. Plays a central role in regulation of posterior
CC       development, by regulating HOX gene expression. Demethylation of
CC       'Lys-27' of histone H3 is concomitent with methylation of 'Lys-4'
CC       of histone H3, and regulates the recruitment of the PRC1 complex
CC       and monoubiquitination of histone H2A (By similarity).
CC   -!- COFACTOR: Ascorbate (By similarity).
CC   -!- COFACTOR: Fe(2+) (By similarity).
CC   -!- SUBUNIT: Component of the MLL3/MLL4 complex, at least composed of
CC       MLL3, MLL4, ASH2L, RBBP5, DPY30, WDR5, NCOA6, KDM6A, PAXIP1/PTIP
CC       and C16orf53/PA1. Some fraction of the complex contains MLL2
CC       instead of MLL4 and is named MLL2/MLL3 complex. Interacts with
CC       TLE1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O70546-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O70546-2; Sequence=VSP_022196;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, heart and spleen.
CC   -!- DEVELOPMENTAL STAGE: Widely expressed at E13.5.
CC   -!- MISCELLANEOUS: Escapes X chromosome inactivation.
CC   -!- SIMILARITY: Belongs to the UTX family.
CC   -!- SIMILARITY: Contains 1 JmjC domain.
CC   -!- SIMILARITY: Contains 8 TPR repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH75703.1; Type=Erroneous initiation;
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CC   -----------------------------------------------------------------------
DR   EMBL; AL732451; CAM27157.1; -; Genomic_DNA.
DR   EMBL; AL773547; CAM27157.1; JOINED; Genomic_DNA.
DR   EMBL; AL773547; CAM18408.1; -; Genomic_DNA.
DR   EMBL; AL732451; CAM18408.1; JOINED; Genomic_DNA.
DR   EMBL; BC053433; AAH53433.1; -; mRNA.
DR   EMBL; BC075703; AAH75703.1; ALT_INIT; mRNA.
DR   EMBL; AJ002730; CAA05692.1; -; mRNA.
DR   IPI; IPI00323510; -.
DR   IPI; IPI00338053; -.
DR   RefSeq; NP_033509.1; NM_009483.1.
DR   UniGene; Mm.257498; -.
DR   UniGene; Mm.417709; -.
DR   ProteinModelPortal; O70546; -.
DR   SMR; O70546; 92-384, 933-1252.
DR   STRING; O70546; -.
DR   PhosphoSite; O70546; -.
DR   PRIDE; O70546; -.
DR   Ensembl; ENSMUST00000044484; ENSMUSP00000045862; ENSMUSG00000037369.
DR   Ensembl; ENSMUST00000052368; ENSMUSP00000061539; ENSMUSG00000037369.
DR   GeneID; 22289; -.
DR   KEGG; mmu:22289; -.
DR   UCSC; uc009ssm.1; mouse.
DR   UCSC; uc009ssn.1; mouse.
DR   CTD; 22289; -.
DR   MGI; MGI:1095419; Kdm6a.
DR   eggNOG; roNOG13048; -.
DR   OMA; QSPMKTD; -.
DR   OrthoDB; EOG4M91QN; -.
DR   NextBio; 302431; -.
DR   ArrayExpress; O70546; -.
DR   Bgee; O70546; -.
DR   Genevestigator; O70546; -.
DR   GermOnline; ENSMUSG00000037369; Mus musculus.
DR   GO; GO:0035097; C:histone methyltransferase complex; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR013129; TF_JmjC.
DR   InterPro; IPR003347; TF_JmjC_AAH.
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; PF02373; JmjC; 1.
DR   Pfam; PF00515; TPR_1; 2.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00028; TPR; 6.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS50005; TPR; 7.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromatin regulator; Dioxygenase; Iron;
KW   Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; Repeat;
KW   TPR repeat.
FT   CHAIN         1   1401       Lysine-specific demethylase 6A.
FT                                /FTId=PRO_0000106410.
FT   REPEAT       95    128       TPR 1.
FT   REPEAT      132    165       TPR 2.
FT   REPEAT      169    203       TPR 3.
FT   REPEAT      207    240       TPR 4.
FT   REPEAT      245    285       TPR 5.
FT   REPEAT      286    319       TPR 6.
FT   REPEAT      321    353       TPR 7.
FT   REPEAT      355    387       TPR 8.
FT   DOMAIN     1095   1258       JmjC.
FT   COMPBIAS      9     19       Poly-Ala.
FT   COMPBIAS    919    941       Pro-rich.
FT   MOD_RES     769    769       Phosphoserine (By similarity).
FT   MOD_RES     818    818       Phosphoserine (By similarity).
FT   MOD_RES     829    829       Phosphoserine.
FT   MOD_RES    1061   1061       Phosphoserine.
FT   VAR_SEQ    1393   1401       APPLPSASS -> VSEINMLLHYHPPHLDIVPWTLNMRPFL
FT                                LFRK (in isoform 2).
FT                                /FTId=VSP_022196.
FT   CONFLICT    321    321       D -> G (in Ref. 2; AAH75703).
FT   CONFLICT   1198   1198       E -> G (in Ref. 2; AAH75703).
SQ   SEQUENCE   1401 AA;  154355 MW;  293DA417F49EECFF CRC64;
     MKSCGVSLAT AAAAAAAAAF GDEEKKMAAG KASGESEEAS PSLTAEEREA LGGLDSRLFG
     FVRFHEDGAR MKALLGKAVR CYESLILKAE GKVESDFFCQ LGHFNLLLED YPKALSAYQR
     YYSLQSDYWK NAAFLYGLGL VYFHYNAFQW AIKAFQEVLY VDPSFCRAKE IHLRLGLMFK
     VNTDYESSLK HFQLALVDCN PCTLSNAEIQ FHIAHLYETQ RKYHSAKEAY EQLLQTENLS
     AQVKATILQQ LGWMHHTVDL LGDKATKESY AIQYLQKSLE ADPNSGQSWY FLGRCYSSIG
     KVQDAFISYR QSIDKSEASA DTWCSIGVLY QQQNQPMDAL QAYICAVQLD HGHAAAWMDL
     GTLYESCNQP QDAIKCYLNA TRSKNCSNTS GLAARIKYLQ AQLCNLPQGS LQNKTKLLPS
     IEEAWSLPIP AELTSRQGAM NTAQQNTSDN WSGGNAPPPV EQQTHSWCLT PQKLQHLEQL
     RANRNNLNPA QKLMLEQLES QFVLMQQHQM RQTGVAQVRP TGILNGPTVD SSLPTNSVSG
     QQPQLPLTRM PSVSQPGVHT ACPRQTLANG PFSAGHVPCS TSRTLGSTDT VLIGNNHVTG
     SGSNGNVPYL QRNAPTLPHN RTNLTSSTEE PWKNQLSNST QGLHKGPSSH LAGPNGERPL
     SSTGPSQHLQ AAGSGIQNQN GHPTLPSNSV TQGAALNHLS SHTATSGGQQ GITLTKESKP
     SGNTLTVPET SRQTGETPNS TASVEGLPNH VHQVMADAVC SPSHGDSKSP GLLSSDNPQL
     SALLMGKANN NVGPGTCDKV NNIHPTVHTK TDNSVASSPS SAISTATPSP KSTEQTTTNS
     VTSLNSPHSG LHTINGEGME ESQSPIKTDL LLVSHRPSPQ IIPSMSVSIY PSSAEVLKAC
     RNLGKNGLSN SSILLDKCPP PRPPSSPYPP LPKDKLNPPT PSIYLENKRD AFFPPLHQFC
     TNPNNPVTVI RGLAGALKLD LGLFSTKTLV EANNEHMVEV RTQLLQPADE NWDPTGTKKI
     WHCESNRSHT TIAKYAQYQA SSFQESLREE NEKRSHHKDH SDSESTSSDN SGKRRKGPFK
     TIKFGTNIDL SDDKKWKLQL HELTKLPAFV RVVSAGNLLS HVGHTILGMN TVQLYMKVPG
     SRTPGHQENN NFCSVNINIG PGDCEWFVVP EGYWGVLNDF CEKNNLNFLM GSWWPNLEDL
     YEANVPVYRF IQRPGDLVWI NAGTVHWVQA IGWCNNIAWN VGPLTACQYK LAVERYEWNK
     LQNVKSIVPM VHLSWNMARN IKVSDPKLFE MIKYCLLRTL KQCQTLREAL IAAGKEIIWH
     GRTKEEPAHY CSICEVEVFD LLFVTNESNS RKTYIVHCQD CARKTSGNLE NFVVLEQYKM
     EDLMQVYDQF TLAPPLPSAS S
//
ID   PLIN4_MOUSE             Reviewed;        1403 AA.
AC   O88492; Q69Z80; Q8BNV5;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Perilipin-4;
DE   AltName: Full=Adipocyte protein S3-12;
GN   Name=Plin4; Synonyms=Kiaa1881;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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   SUBCELLULAR LOCATION.
RC   TISSUE=Adipocyte;
RX   MEDLINE=98287788; PubMed=9624692; DOI=10.1038/nbt0698-581;
RA   Scherer P.E., Bickel P.E., Kotler M., Lodish H.F.;
RT   "Cloning of cell-specific secreted and surface proteins by subtractive
RT   antibody screening.";
RL   Nat. Biotechnol. 16:581-586(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1263-1403 (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   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12840023; DOI=10.1074/jbc.M304025200;
RA   Wolins N.E., Skinner J.R., Schoenfish M.J., Tzekov A., Bensch K.G.,
RA   Bickel P.E.;
RT   "Adipocyte protein S3-12 coats nascent lipid droplets.";
RL   J. Biol. Chem. 278:37713-37721(2003).
RN   [5]
RP   INDUCTION, AND TISSUE SPECIFICITY.
RX   PubMed=15111493;
RA   Dalen K.T., Schoonjans K., Ulven S.M., Weedon-Fekjaer M.S.,
RA   Bentzen T.G., Koutnikova H., Auwerx J., Nebb H.I.;
RT   "Adipose tissue expression of the lipid droplet-associating proteins
RT   S3-12 and perilipin is controlled by peroxisome proliferator-activated
RT   receptor-gamma.";
RL   Diabetes 53:1243-1252(2004).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15731108; DOI=10.1074/jbc.M500978200;
RA   Wolins N.E., Quaynor B.K., Skinner J.R., Schoenfish M.J., Tzekov A.,
RA   Bickel P.E.;
RT   "S3-12, Adipophilin, and TIP47 package lipid in adipocytes.";
RL   J. Biol. Chem. 280:19146-19155(2005).
CC   -!- FUNCTION: May play a role in triacylglycerol packaging into
CC       adipocytes. May function as a coat protein involved in the
CC       biogenesis of lipid droplets.
CC   -!- SUBCELLULAR LOCATION: Cell membrane. Cytoplasm. Lipid droplet.
CC       Note=Nascent lipid droplet surface-associated; association with
CC       lipid droplets is triacylglycerol synthesis-dependent.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O88492-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O88492-2; Sequence=VSP_027279, VSP_027280;
CC   -!- TISSUE SPECIFICITY: Specifically expressed in white adipose tissue
CC       and also weakly detected in heart and skeletal muscle (at protein
CC       level).
CC   -!- INDUCTION: Up-regulated by PPARG and during adipocyte
CC       differentiation.
CC   -!- SIMILARITY: Belongs to the perilipin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC37834.1; Type=Erroneous initiation;
CC       Sequence=BAD32564.1; Type=Erroneous initiation;
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DR   EMBL; AF064748; AAC23666.1; -; mRNA.
DR   EMBL; AK173286; BAD32564.1; ALT_INIT; Transcribed_RNA.
DR   EMBL; AK080156; BAC37834.1; ALT_INIT; mRNA.
DR   IPI; IPI00131113; -.
DR   IPI; IPI00856568; -.
DR   PIR; T17372; T17372.
DR   RefSeq; NP_065593.2; NM_020568.3.
DR   UniGene; Mm.12966; -.
DR   UniGene; Mm.480728; -.
DR   HSSP; Q9DBG5; 1SZI.
DR   ProteinModelPortal; O88492; -.
DR   SMR; O88492; 1195-1397.
DR   PRIDE; O88492; -.
DR   Ensembl; ENSMUST00000002908; ENSMUSP00000002908; ENSMUSG00000002831.
DR   GeneID; 57435; -.
DR   KEGG; mmu:57435; -.
DR   UCSC; uc008day.2; mouse.
DR   CTD; 57435; -.
DR   MGI; MGI:1929709; Plin4.
DR   eggNOG; roNOG14304; -.
DR   GeneTree; ENSGT00570000079269; -.
DR   HOGENOM; HBG506061; -.
DR   HOVERGEN; HBG099259; -.
DR   InParanoid; O88492; -.
DR   OrthoDB; EOG44MXT5; -.
DR   NextBio; 313810; -.
DR   ArrayExpress; O88492; -.
DR   Bgee; O88492; -.
DR   CleanEx; MM_S3-12; -.
DR   Genevestigator; O88492; -.
DR   GO; GO:0005811; C:lipid particle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   InterPro; IPR004279; Perilipin.
DR   PANTHER; PTHR14024; Perilipin; 1.
DR   Pfam; PF03036; Perilipin; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasm; Lipid droplet;
KW   Membrane; Repeat.
FT   CHAIN         1   1403       Perilipin-4.
FT                                /FTId=PRO_0000297560.
FT   REPEAT      104    136       1.
FT   REPEAT      137    169       2.
FT   REPEAT      170    202       3.
FT   REPEAT      203    235       4.
FT   REPEAT      236    268       5.
FT   REPEAT      269    301       6.
FT   REPEAT      302    334       7.
FT   REPEAT      335    367       8.
FT   REPEAT      368    400       9.
FT   REPEAT      401    433       10.
FT   REPEAT      434    466       11.
FT   REPEAT      467    499       12.
FT   REPEAT      500    532       13.
FT   REPEAT      533    565       14.
FT   REPEAT      566    598       15.
FT   REPEAT      599    631       16.
FT   REPEAT      632    664       17.
FT   REPEAT      665    697       18.
FT   REPEAT      698    730       19.
FT   REPEAT      731    763       20.
FT   REPEAT      764    796       21.
FT   REPEAT      797    829       22.
FT   REPEAT      830    862       23.
FT   REPEAT      863    895       24.
FT   REPEAT      896    928       25.
FT   REPEAT      929    961       26.
FT   REPEAT      962    994       27.
FT   REPEAT      995   1027       28.
FT   REPEAT     1028   1060       29.
FT   REGION      104   1060       29 X 33 AA approximate tandem repeat.
FT   VAR_SEQ     206    601       Missing (in isoform 2).
FT                                /FTId=VSP_027279.
FT   VAR_SEQ    1267   1271       Missing (in isoform 2).
FT                                /FTId=VSP_027280.
FT   CONFLICT   1121   1121       H -> Q (in Ref. 2; BAD32564).
FT   CONFLICT   1258   1258       V -> L (in Ref. 2; BAD32564).
SQ   SEQUENCE   1403 AA;  139382 MW;  5ECFCCA9ACCB62BD CRC64;
     MSASGDGTRV PPKSKGKTLS SFFGSLPGFS SARNLVSHTH SSTSTKDLQT ATDPSGTPAP
     SSKVSTNSQM AGDAAGLLQP SEQTAGDKDM GSFSVTSSED AFSGVFGIMD AAKGMVQGGL
     GATQSALVGT KEAVSGGVMG AVGVAKGLVK GGLDTSKNVL TNTKDTVTTG VMGAANMAKG
     TVQTGLDTTK SVVMGTKDTV ATGLAGAVNV AKGTIQGGLD TTKSVVMGTK DTVTTGLTGA
     ANVAKGVVQG GLDTTKSVVM GTKDTVTTGL TGAMNVAKGT AQMGIDTSKT VLTGTKDTVC
     AGATGAINVA KGAAQGGLDT TKSVLIGTKD TVTTGLTGAV NVAKGAVQGG LDTTKSVVMG
     TKDTVTTGLT GAMNVAKGTA QMGLGTSKTV LTGTKDTVCA GLTGAINVAK GAAQGGLDTT
     KSVLMGTKDT VTTGLTGAVN VAKGTIQGGL DTTKSVVMGT KDTVTTGLTG AVNVAKGTIQ
     GGLDTTKSVV MGTKDTVTTG LTGAVNVAKG AAQGGLDTTK SVVMGTKDTV TTGLTGAMNV
     AKGTAQMGLG TSKTVLTGTK DTVCAGLTGA INVAKGAAQG GLDTTKSVLM GTKDTVTTGL
     TGAVNVAKGT IQGGLDTTKS VVMGTKDTVT TGLTGAVNVA KGAVQGGLDT TKSVVMGTKD
     TVTTGLTGAL NVAKGTAQMG IDTSKTVLIG TKDTVCAGAT GAINMAKGAA QGGLDTTKSV
     LMGTKDTVTT GLTGAINVAK GSAQGGLDTT KSVLIGTKDT VTTGLTGALN VAKGTVQTGL
     DTSQRVLTGT KDNVYAGVTG AVNVAKGTIQ GGLDTTKSVV MGTKDTVTTG LTGAVNVAKG
     AVQGGLDTTK SVVMGTKDTV TTGLTGAMNV AKGTAQMGID TSKTVLTGTK DTVCAGLTGA
     INVAKGATQG GLDTTKSVLM GTKDTVTTGL TGAINVAKGA AQGGLDTTKS VLLGTKDTVT
     TGLTGAANVA KETVQMGLDT SKNILMDTKD SICAGATGAI TVVKGAAQGG LDTSNAALTG
     TMDTAKGTVQ TSLDTSKHML IGMKDTVCAG VTSAMNMAKG IHKNTDTTRD TQSSVLAHSG
     NVATNAIHTG VHTVPSSLSG SHSIICHEPS IYRATNHGVG HAILTSTESL CCETSSFSDK
     YGLGHVTEPR ADTKTLVSGM ASSACAATRS VEECGQLAAT GFAALPDELK GLGDIFQPMT
     TEEQAQLAVS ESGPRVLSAD RGSYYIRLGD LAPSFRQRAF EHALSHIQHN QFQARAAVAQ
     LQEAFQMTDM TMEAACGKLC SDQSLNTMVE AVGSHEMRAS VAQDRLCTLA HQLHAAYSSL
     VTSLQGLPEV QQQAGQARHS LCKLYGLVSS EAGSELQTEQ LAQSSAGVVE AWQGLEVLLE
     KLQQNPPLSW LVGPFTSMPC GQL
//
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;
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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   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   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   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   HIPK1_MOUSE             Reviewed;        1210 AA.
AC   O88904; A6H5Z7; Q80TV5; Q9QUQ8; Q9QZR3; Q9WVN7;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   08-MAR-2011, entry version 101.
DE   RecName: Full=Homeodomain-interacting protein kinase 1;
DE            EC=2.7.11.1;
DE   AltName: Full=Nuclear body-associated kinase 2;
DE   AltName: Full=Protein kinase Myak;
GN   Name=Hipk1; Synonyms=Kiaa0630, Myak, Nbak2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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 NKX1-2
RP   AND NKX2-5.
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] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=CD-1; TISSUE=Testis;
RX   MEDLINE=20160527; PubMed=10694743;
RX   DOI=10.1002/(SICI)1098-2795(200004)55:4<372::AID-MRD3>3.0.CO;2-A;
RA   Shang E., Wang X., Huang J., Yoshida W., Kuroiwa A., Wolgemuth D.J.;
RT   "Murine Myak, a member of a family of yeast YAK1-related genes, is
RT   highly expressed in hormonally modulated epithelia in the reproductive
RT   system and in the embryonic central nervous system.";
RL   Mol. Reprod. Dev. 55:372-378(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
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   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 608-1209 (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   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH DAXX,
RP   AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-219.
RX   MEDLINE=22417486; PubMed=12529400; DOI=10.1128/MCB.23.3.950-960.2003;
RA   Ecsedy J.A., Michaelson J.S., Leder P.;
RT   "Homeodomain-interacting protein kinase 1 modulates Daxx localization,
RT   phosphorylation, and transcriptional activity.";
RL   Mol. Cell. Biol. 23:950-960(2003).
RN   [7]
RP   INTERACTION WITH TP53, AUTOPHOSPHORYLATION, AND FUNCTION.
RX   MEDLINE=22608637; PubMed=12702766; DOI=10.1073/pnas.0530308100;
RA   Kondo S., Lu Y., Debbas M., Lin A.W., Sarosi I., Itie A., Wakeham A.,
RA   Tuan J., Saris C., Elliott G., Ma W., Benchimol S., Lowe S.W.,
RA   Mak T.W., Thukral S.K.;
RT   "Characterization of cells and gene-targeted mice deficient for the
RT   p53-binding kinase homeodomain-interacting protein kinase 1 (HIPK1).";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5431-5436(2003).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-352, 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-352, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
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 as a corepressor for homeodomain
CC       transcription factors. Phosphorylates DAXX in response to stress,
CC       and mediates its translocation from the nucleus to the cytoplasm.
CC       May be involved in malignant squamous cell tumor formation.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts with Nkx1-2, Nkx2-5, DAXX, and TP53.
CC   -!- INTERACTION:
CC       Q9UER7:DAXX (xeno); NbExp=1; IntAct=EBI-692945, EBI-77321;
CC       O35613:Daxx; NbExp=2; IntAct=EBI-692945, EBI-77304;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly
CC       nuclear.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=2b, Myak-L;
CC         IsoId=O88904-1; Sequence=Displayed;
CC       Name=2; Synonyms=2a;
CC         IsoId=O88904-2; Sequence=VSP_013133;
CC       Name=3; Synonyms=Myak-S;
CC         IsoId=O88904-3; Sequence=VSP_013132, VSP_013134;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, with high levels in
CC       reproductive tissues. Expressed in the epithelial layer of mammary
CC       gland, uterus and epididymis, in the corpus luteum, and in post-
CC       meiotic round spermatids.
CC   -!- DEVELOPMENTAL STAGE: Highest at E12, where it is expressed
CC       primarily in the central nervous system.
CC   -!- PTM: Phosphorylated and activated by JNK1 (By similarity).
CC       Autophosphorylated.
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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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF077658; AAC63010.1; -; mRNA.
DR   EMBL; AF071070; AAD41592.1; -; mRNA.
DR   EMBL; AF071071; AAD41593.1; -; mRNA.
DR   EMBL; AF170303; AAD52568.1; -; mRNA.
DR   EMBL; AF170304; AAD52569.1; -; mRNA.
DR   EMBL; BC145697; AAI45698.1; -; mRNA.
DR   EMBL; BC145699; AAI45700.1; -; mRNA.
DR   EMBL; AK122333; BAC65615.1; -; mRNA.
DR   IPI; IPI00133158; -.
DR   IPI; IPI00136238; -.
DR   IPI; IPI00553580; -.
DR   PIR; T14357; T14357.
DR   RefSeq; NP_034562.2; NM_010432.2.
DR   UniGene; Mm.20827; -.
DR   UniGene; Mm.477324; -.
DR   ProteinModelPortal; O88904; -.
DR   SMR; O88904; 174-520.
DR   IntAct; O88904; 7.
DR   STRING; O88904; -.
DR   PhosphoSite; O88904; -.
DR   PRIDE; O88904; -.
DR   Ensembl; ENSMUST00000029438; ENSMUSP00000029438; ENSMUSG00000008730.
DR   Ensembl; ENSMUST00000106838; ENSMUSP00000102451; ENSMUSG00000008730.
DR   Ensembl; ENSMUST00000106845; ENSMUSP00000102458; ENSMUSG00000008730.
DR   Ensembl; ENSMUST00000118317; ENSMUSP00000113998; ENSMUSG00000008730.
DR   GeneID; 15257; -.
DR   KEGG; mmu:15257; -.
DR   UCSC; uc008qth.1; mouse.
DR   CTD; 15257; -.
DR   MGI; MGI:1314873; Hipk1.
DR   GeneTree; ENSGT00550000074148; -.
DR   HOGENOM; HBG443763; -.
DR   HOVERGEN; HBG051908; -.
DR   InParanoid; O88904; -.
DR   OMA; KADRREY; -.
DR   OrthoDB; EOG4K9BBD; -.
DR   PhylomeDB; O88904; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 287873; -.
DR   ArrayExpress; O88904; -.
DR   Bgee; O88904; -.
DR   CleanEx; MM_HIPK1; -.
DR   Genevestigator; O88904; -.
DR   GermOnline; ENSMUSG00000008730; Mus musculus.
DR   GO; GO:0016607; C:nuclear speck; IDA:MGI.
DR   GO; GO:0016605; C:PML body; 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:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR   GO; GO:0009952; P:anterior/posterior pattern formation; IGI:MGI.
DR   GO; GO:0042771; P:DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis; IGI:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IGI:MGI.
DR   GO; GO:0043388; P:positive regulation of DNA binding; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0007224; P:smoothened signaling pathway; IGI: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; Cytoplasm; Kinase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1   1210       Homeodomain-interacting protein kinase 1.
FT                                /FTId=PRO_0000085994.
FT   DOMAIN      190    518       Protein kinase.
FT   NP_BIND     196    204       ATP (Probable).
FT   REGION      885   1093       Interaction with TP53.
FT   ACT_SITE    315    315       Proton acceptor (Probable).
FT   BINDING     219    219       ATP (Probable).
FT   MOD_RES     352    352       Phosphotyrosine.
FT   MOD_RES     872    872       Phosphoserine (By similarity).
FT   VAR_SEQ     661    719       TGLQATTKHSGFPVRMDNAVPIVPQAPAAQPLQIQSGVLTQ
FT                                GSCTPLMVATLHPQVATI -> KSEQAEGNEGLGETESSPG
FT                                GQESGSGVSQGETTGGAQEQIHNPWTTSNNKAFWIPCEDG
FT                                (in isoform 3).
FT                                /FTId=VSP_013132.
FT   VAR_SEQ     702    746       Missing (in isoform 2).
FT                                /FTId=VSP_013133.
FT   VAR_SEQ     720   1209       Missing (in isoform 3).
FT                                /FTId=VSP_013134.
FT   MUTAGEN     219    219       K->A: Abolishes enzymatic activity.
FT   CONFLICT    732    732       Missing (in Ref. 1; AAC63010).
FT   CONFLICT    921    921       K -> E (in Ref. 1; AAC63010).
FT   CONFLICT    953    953       H -> Y (in Ref. 5).
FT   CONFLICT    954    954       P -> S (in Ref. 1 and 5).
FT   CONFLICT   1134   1134       S -> F (in Ref. 1; AAC63010).
SQ   SEQUENCE   1210 AA;  130723 MW;  26D264B883220640 CRC64;
     MASQLQVFSP PSVSSSAFCS AKKLKIEPSG WDVSGQSSND KYYTHSKTLP ATQGQASSSH
     QVANFNLPAY DQGLLLPAPA VEHIVVTAAD SSGSAATATF QSSQTLTHRS NVSLLEPYQK
     CGLKRKSEEV ESNGSVQIIE EHPPLMLQNR TVVGAAATTT TVTTKSSSSS GEGDYQLVQH
     EILCSMTNSY EVLEFLGRGT FGQVAKCWKR STKEIVAIKI LKNHPSYARQ GQIEVSILSR
     LSSENADEYN FVRSYECFQH KNHTCLVFEM LEQNLYDFLK QNKFSPLPLK YIRPILQQVA
     TALMKLKSLG LIHADLKPEN IMLVDPVRQP YRVKVIDFGS ASHVSKAVCS TYLQSRYYRA
     PEIILGLPFC EAIDMWSLGC VIAELFLGWP LYPGASEYDQ IRYISQTQGL PAEYLLSAGT
     KTTRFFNRDP NLGYPLWRLK TPEEHELETG IKSKEARKYI FNCLDDMAQV NMSTDLEGTD
     MLAEKADRRE YIDLLKKMLT IDADKRITPL KTLNHQFVTM SHLLDFPHSS HVKSCFQNME
     ICKRRVHMYD TVSQIKSPFT THVAPNTSTN LTMSFSNQLN TVHNQASVLA SSSTAAAATL
     SLANSDVSLL NYQSALYPSS AAPVPGVAQQ GVSLQPGTTQ ICTQTDPFQQ TFIVCPPAFQ
     TGLQATTKHS GFPVRMDNAV PIVPQAPAAQ PLQIQSGVLT QGSCTPLMVA TLHPQVATIT
     PQYAVPFTLS CAAGRPALVE QTAAVLQAWP GGTQQILLPS AWQQLPGVAL HNSVQPAAVI
     PEAMGSSQQL ADWRNAHSHG NQYSTIMQQP SLLTNHVTLA TAQPLNVGVA HVVRQQQSSS
     LPSKKNKQSA PVSSKSSLEV LPSQVYSLVG SSPLRTTSSY NSLVPVQDQH QPIIIPDTPS
     PPVSVITIRS DTDEEEDNKY KPNSSSLKAR SNVISYVTVN DSPDSDSSLS SPHPTDTLSA
     LRGNSGTLLE GPGRPAADGI GTRTIIVPPL KTQLGDCTVA TQASGLLSSK TKPVASVSGQ
     SSGCCITPTG YRAQRGGASA VQPLNLSQNQ QSSSASTSQE RSSNPAPRRQ QAFVAPLSQA
     PYAFQHGSPL HSTGHPHLAP APAHLPSQPH LYTYAAPTSA AALGSTSSIA HLFSPQGSSR
     HAAAYTTHPS TLVHQVPVSV GPSLLTSASV APAQYQHQFA TQSYIGSSRG STIYTGYPLS
     PTKISQYSYL
//
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.
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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   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.
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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   DNJB5_MOUSE             Reviewed;         348 AA.
AC   O89114;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=DnaJ homolog subfamily B member 5;
DE   AltName: Full=Heat shock protein Hsp40-3;
DE   AltName: Full=Heat shock protein cognate 40;
DE            Short=Hsc40;
GN   Name=Dnajb5; Synonyms=Hsc40;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; 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=20035738; PubMed=10570961; DOI=10.1016/S0378-1119(99)00333-9;
RA   Chen M.-S., Roti J.R., Laszlo A.;
RT   "Hsc40, a new member of the hsp40 family, exhibits similar expression
RT   profile to that of hsc70 in mammalian cells.";
RL   Gene 238:333-341(1999).
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).
CC   -!- INDUCTION: Expressed under normal conditions, its expression can
CC       further be increased after various stress treatments.
CC   -!- SIMILARITY: Contains 1 J domain.
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DR   EMBL; AF092536; AAC64141.1; -; Genomic_DNA.
DR   EMBL; AF088983; AAC35861.1; -; mRNA.
DR   EMBL; AF321322; AAG53972.1; -; mRNA.
DR   EMBL; BC048902; AAH48902.1; -; mRNA.
DR   EMBL; BC057087; AAH57087.1; -; mRNA.
DR   IPI; IPI00131539; -.
DR   RefSeq; NP_063927.1; NM_019874.3.
DR   UniGene; Mm.20437; -.
DR   ProteinModelPortal; O89114; -.
DR   SMR; O89114; 1-76, 126-342.
DR   PRIDE; O89114; -.
DR   Ensembl; ENSMUST00000037872; ENSMUSP00000040451; ENSMUSG00000036052.
DR   Ensembl; ENSMUST00000084662; ENSMUSP00000081712; ENSMUSG00000036052.
DR   Ensembl; ENSMUST00000098112; ENSMUSP00000095716; ENSMUSG00000036052.
DR   Ensembl; ENSMUST00000107973; ENSMUSP00000103607; ENSMUSG00000036052.
DR   GeneID; 56323; -.
DR   KEGG; mmu:56323; -.
DR   UCSC; uc008som.1; mouse.
DR   CTD; 56323; -.
DR   MGI; MGI:1930018; Dnajb5.
DR   HOVERGEN; HBG066727; -.
DR   InParanoid; O89114; -.
DR   OrthoDB; EOG4PRSQW; -.
DR   PhylomeDB; O89114; -.
DR   NextBio; 312294; -.
DR   ArrayExpress; O89114; -.
DR   Bgee; O89114; -.
DR   CleanEx; MM_DNAJB5; -.
DR   Genevestigator; O89114; -.
DR   GermOnline; ENSMUSG00000036052; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
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; IEA:InterPro.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IGI: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   2: Evidence at transcript level;
KW   Chaperone.
FT   CHAIN         1    348       DnaJ homolog subfamily B member 5.
FT                                /FTId=PRO_0000071024.
FT   DOMAIN        4     68       J.
SQ   SEQUENCE   348 AA;  39119 MW;  833D2F3547321687 CRC64;
     MGKDYYKILG IPSGANEDEI KKAYRKMALK YHPDKNKEPN AEEKFKEIAE AYDVLSDPKK
     RSLYDQYGEE GLKTGGGSSG GSGGSFHYTF HGDPHATFAS FFGGSNPFDI FFASSRSTRP
     FSGFDPDDMD VDEDEDPFGA FGRFGFNGLS RGPRRAPEPL YPRRKVQDPP VVHELRVSLE
     EIYHGSTKRM KITRRRLNPD GRTVRTEDKI LHIVIKRGWK EGTKITFPKE GDATPDNIPA
     DIVFVLKDKP HAHFRRDGTN VLYSALISLK EALCGCTVNI PTIDGRVIPL PCNDVIKPGT
     VKRLRGEGLP FPKVPTQRGD LIVEFKVRFP DRLTPQTRQI LKQHLPCS
//
ID   HBA_MOUSE               Reviewed;         142 AA.
AC   P01942;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 104.
DE   RecName: Full=Hemoglobin subunit alpha;
DE   AltName: Full=Alpha-globin;
DE   AltName: Full=Hemoglobin alpha chain;
GN   Name=Hba; Synonyms=Hba-a1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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=80090039; PubMed=519760; DOI=10.1016/0092-8674(79)90139-9;
RA   Nishioka Y., Leder P.;
RT   "The complete sequence of a chromosomal mouse alpha-globin gene
RT   reveals elements conserved throughout vertebrate evolution.";
RL   Cell 18:875-882(1979).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-142.
RC   STRAIN=BALB/c, C57BL/6, and NB;
RX   MEDLINE=67208815; PubMed=5340470; DOI=10.1016/0022-2836(67)90347-6;
RA   Popp R.A.;
RT   "Hemoglobins of mice: sequence and possible ambiguity at one position
RT   of the alpha chain.";
RL   J. Mol. Biol. 27:9-16(1967).
RN   [3]
RP   PROTEIN SEQUENCE OF 18-57; 94-100 AND 129-140, 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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-99.
RX   MEDLINE=79096141; PubMed=282635; DOI=10.1073/pnas.75.12.6187;
RA   Leder A., Miller H.I., Hamer D.H., Seidman J.G., Norman B.,
RA   Sullivan M., Leder P.;
RT   "Comparison of cloned mouse alpha- and beta-globin genes: conservation
RT   of intervening sequence locations and extragenic homology.";
RL   Proc. Natl. Acad. Sci. U.S.A. 75:6187-6191(1978).
RN   [5]
RP   NUCLEOTIDE SEQUENCE OF 84-109.
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   [6]
RP   VARIANTS VAL-26; ILE-63; ASN-69; THR-69 AND ALA-79.
RX   MEDLINE=70009408; PubMed=5345070;
RA   Popp R.A.;
RT   "Studies on the mouse hemoglobin loci. 8. A fourth alpha-chain
RT   phenotype.";
RL   J. Hered. 60:126-133(1969).
RN   [7]
RP   VARIANTS VAL-26; ILE-63; ASN-69; THR-69 AND ALA-79.
RA   Popp R.A.;
RL   (In) Altman P.A., Katz D.D. (eds.);
RL   Inbred and genetically defined strains of laboratory animals,
RL   pp.105-105, Federation of American Societies for Experimental Biology,
RL   Bethesda (1979).
RN   [8]
RP   VARIANTS VAL-26; ILE-63; ASN-69; THR-69 AND ALA-79.
RX   MEDLINE=82231171; PubMed=7092800; DOI=10.1007/BF00484946;
RA   Popp R.A., Bailiff E.G., Skow L.C., Whitney J.B. III;
RT   "The primary structure of genetic variants of mouse hemoglobin.";
RL   Biochem. Genet. 20:199-208(1982).
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: In inbred mouse strains there are at least 6 alleles
CC       that can occur at the HBA locus: A, B, C, D, F, or G. Strains
CC       carrying the A and F alleles produce a single kind of alpha chain,
CC       whereas those carrying B, C, D, or G each produce 2 kinds of
CC       chains. The sequence shown is that of the B(1) and D(1) allele
CC       chains.
CC   -!- SIMILARITY: Belongs to the globin family.
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DR   EMBL; V00714; CAA24095.1; -; Genomic_DNA.
DR   EMBL; M10703; AAA37782.2; -; Genomic_DNA.
DR   EMBL; M10840; AAA37784.1; -; mRNA.
DR   IPI; IPI00469114; -.
DR   PIR; A90791; HAMS.
DR   UniGene; Mm.196110; -.
DR   PDB; 3HRW; X-ray; 2.80 A; A/C=2-142.
DR   PDBsum; 3HRW; -.
DR   ProteinModelPortal; P01942; -.
DR   SMR; P01942; 2-142.
DR   STRING; P01942; -.
DR   PhosphoSite; P01942; -.
DR   SWISS-2DPAGE; P01942; -.
DR   REPRODUCTION-2DPAGE; IPI00469114; -.
DR   REPRODUCTION-2DPAGE; P01942; -.
DR   PRIDE; P01942; -.
DR   Ensembl; ENSMUST00000093207; ENSMUSP00000090895; ENSMUSG00000069917.
DR   Ensembl; ENSMUST00000093209; ENSMUSP00000090897; ENSMUSG00000069919.
DR   MGI; MGI:96015; Hba-a1.
DR   eggNOG; roNOG16000; -.
DR   HOGENOM; HBG715197; -.
DR   HOVERGEN; HBG009709; -.
DR   InParanoid; P01942; -.
DR   OrthoDB; EOG47M209; -.
DR   Bgee; P01942; -.
DR   CleanEx; MM_HBA-A1; -.
DR   Genevestigator; P01942; -.
DR   GermOnline; ENSMUSG00000069917; Mus musculus.
DR   GermOnline; ENSMUSG00000069919; 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   GO; GO:0035634; P:response to stilbenoid; IEP:UniProtKB.
DR   InterPro; IPR012292; Globin.
DR   InterPro; IPR009050; Globin-like.
DR   InterPro; IPR000971; Globin_subset.
DR   InterPro; IPR002338; Haemoglobin_a.
DR   InterPro; IPR018331; Haemoglobin_alpha_chain.
DR   InterPro; IPR002339; Haemoglobin_pi.
DR   Gene3D; G3DSA:1.10.490.10; Globin_related; 1.
DR   PANTHER; PTHR11442:SF14; Pi_haem; 1.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00612; ALPHAHAEM.
DR   PRINTS; PR00815; PIHAEM.
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; Polymorphism; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    142       Hemoglobin subunit alpha.
FT                                /FTId=PRO_0000052694.
FT   METAL        59     59       Iron (heme distal ligand).
FT   METAL        88     88       Iron (heme proximal ligand).
FT   VARIANT      26     26       G -> V (in allele chain C(1) and in
FT                                strain NB).
FT   VARIANT      63     63       V -> I (in allele chain C(1) and in
FT                                strain NB).
FT   VARIANT      69     69       S -> N (in allele chains A, C(2), D(2),
FT                                F, G(1) and G(2) and in strain C57BL).
FT   VARIANT      69     69       S -> T (in allele chain B(2) and in 1
FT                                BALB/C strain sequence).
FT   VARIANT      79     79       G -> A (in allele chains F and G(2)).
FT   HELIX         7     13
FT   HELIX        28     36
FT   HELIX        39     43
FT   STRAND       45     47
FT   TURN         54     56
FT   HELIX        62     70
FT   HELIX        84     89
FT   HELIX        97    113
FT   TURN        115    117
FT   HELIX       120    137
FT   HELIX       138    141
SQ   SEQUENCE   142 AA;  15085 MW;  2F70043BFF66E24A CRC64;
     MVLSGEDKSN IKAAWGKIGG HGAEYGAEAL ERMFASFPTT KTYFPHFDVS HGSAQVKGHG
     KKVADALASA AGHLDDLPGA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL ASHHPADFTP
     AVHASLDKFL ASVSTVLTSK YR
//
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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   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.
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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   ITAM_MOUSE              Reviewed;        1153 AA.
AC   P05555; Q8CA73;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 2.
DT   08-FEB-2011, entry version 108.
DE   RecName: Full=Integrin alpha-M;
DE   AltName: Full=CD11 antigen-like family member B;
DE   AltName: Full=CR-3 alpha chain;
DE   AltName: Full=Cell surface glycoprotein MAC-1 subunit alpha;
DE   AltName: Full=Leukocyte adhesion receptor MO1;
DE   AltName: CD_antigen=CD11b;
DE   Flags: Precursor;
GN   Name=Itgam;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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=88312584; PubMed=3044779;
RA   Pytela R.;
RT   "Amino acid sequence of the murine Mac-1 alpha chain reveals homology
RT   with the integrin family and an additional domain related to von
RT   Willebrand factor.";
RL   EMBO J. 7:1371-1378(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-45.
RC   STRAIN=BALB/c; TISSUE=Spleen;
RX   MEDLINE=86287312; PubMed=2942940; DOI=10.1073/pnas.83.15.5644;
RA   Sastre L., Roman J.M., Teplow D.B., Dreyer W.J., Gee C.E.,
RA   Larson R.S., Roberts T.M., Springer T.A.;
RT   "A partial genomic DNA clone for the alpha subunit of the mouse
RT   complement receptor type 3 and cellular adhesion molecule Mac-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:5644-5648(1986).
RN   [4]
RP   PROTEIN SEQUENCE OF 17-28.
RX   MEDLINE=85188276; PubMed=3887182; DOI=10.1038/314540a0;
RA   Springer T.A., Teplow D.B., Dreyer W.J.;
RT   "Sequence homology of the LFA-1 and Mac-1 leukocyte adhesion
RT   glycoproteins and unexpected relation to leukocyte interferon.";
RL   Nature 314:540-542(1985).
CC   -!- FUNCTION: Integrin alpha-M/beta-2 is implicated in various
CC       adhesive interactions of monocytes, macrophages and granulocytes
CC       as well as in mediating the uptake of complement-coated particles.
CC       It is identical with CR-3, the receptor for the iC3b fragment of
CC       the third complement component. It probably recognizes the R-G-D
CC       peptide in C3b. Integrin alpha-M/beta-2 is also a receptor for
CC       fibrinogen, factor X and ICAM1. It recognizes P1 and P2 peptides
CC       of fibrinogen gamma chain. Alpha-M/beta-2 play a critical role in
CC       mast cell development and in immune complex-mediated
CC       glomerulonephritis. Mice expressing a null mutation of the alpha-M
CC       subunit gene demonstrate increase in neutrophil accumulation, in
CC       response to a impaired degranulation and phagocytosis, events that
CC       apparently accelerate apoptosis in neutrophils. These mice develop
CC       obesity.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain. Alpha-M
CC       associates with beta-2.
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=P05555-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P05555-2; Sequence=VSP_010473;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in monocytes and
CC       granulocytes.
CC   -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins
CC       with I-domains do not undergo protease cleavage.
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC   -!- SIMILARITY: Contains 7 FG-GAP repeats.
CC   -!- SIMILARITY: Contains 1 VWFA domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; X07640; CAA30479.1; -; mRNA.
DR   EMBL; AK039444; BAC30350.1; -; mRNA.
DR   EMBL; M14293; AAA39484.1; -; Genomic_DNA.
DR   IPI; IPI00415773; -.
DR   IPI; IPI00876475; -.
DR   PIR; S00551; S00551.
DR   UniGene; Mm.262106; -.
DR   ProteinModelPortal; P05555; -.
DR   SMR; P05555; 149-337, 351-616, 1101-1139.
DR   STRING; P05555; -.
DR   PhosphoSite; P05555; -.
DR   PRIDE; P05555; -.
DR   Ensembl; ENSMUST00000064821; ENSMUSP00000068468; ENSMUSG00000030786.
DR   Ensembl; ENSMUST00000106240; ENSMUSP00000101847; ENSMUSG00000030786.
DR   MGI; MGI:96607; Itgam.
DR   GeneTree; ENSGT00600000084082; -.
DR   HOVERGEN; HBG100530; -.
DR   ArrayExpress; P05555; -.
DR   Bgee; P05555; -.
DR   CleanEx; MM_ITGAM; -.
DR   Genevestigator; P05555; -.
DR   GermOnline; ENSMUSG00000030786; 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:0005634; C:nucleus; 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:0001846; F:opsonin binding; IDA:MGI.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0050798; P:activated T cell proliferation; IMP:MGI.
DR   GO; GO:0045123; P:cellular extravasation; 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   GO; GO:0030593; P:neutrophil chemotaxis; 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   InterPro; IPR002035; VWF_A.
DR   Pfam; PF01839; FG-GAP; 1.
DR   Pfam; PF00357; Integrin_alpha; 1.
DR   Pfam; PF08441; Integrin_alpha2; 1.
DR   Pfam; PF00092; VWA; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   SMART; SM00191; Int_alpha; 5.
DR   SMART; SM00327; VWA; 1.
DR   PROSITE; PS51470; FG_GAP; 7.
DR   PROSITE; PS00242; INTEGRIN_ALPHA; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell adhesion;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Integrin;
KW   Membrane; Receptor; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     16
FT   CHAIN        17   1153       Integrin alpha-M.
FT                                /FTId=PRO_0000016290.
FT   TOPO_DOM     17   1105       Extracellular (Potential).
FT   TRANSMEM   1106   1129       Helical; (Potential).
FT   TOPO_DOM   1130   1153       Cytoplasmic (Potential).
FT   REPEAT       18     75       FG-GAP 1.
FT   REPEAT       76    135       FG-GAP 2.
FT   DOMAIN      164    338       VWFA.
FT   REPEAT      339    390       FG-GAP 3.
FT   REPEAT      391    444       FG-GAP 4.
FT   REPEAT      445    503       FG-GAP 5.
FT   REPEAT      506    564       FG-GAP 6.
FT   REPEAT      569    629       FG-GAP 7.
FT   CA_BIND     465    473       Potential.
FT   CA_BIND     529    537       Potential.
FT   CA_BIND     592    600       Potential.
FT   MOTIF      1132   1136       GFFKR motif.
FT   CARBOHYD     58     58       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     86     86       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    391    391       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    696    696       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    734    734       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    772    772       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    801    801       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    881    881       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    907    907       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    941    941       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    980    980       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    994    994       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1022   1022       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1045   1045       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1051   1051       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1076   1076       N-linked (GlcNAc...) (Potential).
FT   DISULFID     66     73       By similarity.
FT   DISULFID    105    123       By similarity.
FT   DISULFID    654    711       By similarity.
FT   DISULFID    770    776       By similarity.
FT   DISULFID    999   1023       By similarity.
FT   DISULFID   1028   1033       By similarity.
FT   VAR_SEQ     453    569       Missing (in isoform 2).
FT                                /FTId=VSP_010473.
FT   CONFLICT     37     37       N -> S (in Ref. 2; BAC30350).
FT   CONFLICT    683    683       V -> G (in Ref. 2; BAC30350).
SQ   SEQUENCE   1153 AA;  127481 MW;  178DB988AECB0343 CRC64;
     MTLKALLVTA LALCHGFNLD TEHPMTFQEN AKGFGQNVVQ LGGTSVVVAA PQEAKAVNQT
     GALYQCDYST SRCHPIPLQV PPEAVNMSLG LSLAVSTVPQ QLLACGPTVH QNCKENTYVN
     GLCYLFGSNL LRPPQQFPEA LRECPQQESD IVFLIDGSGS INNIDFQKMK EFVSTVMEQF
     KKSKTLFSLM QYSDEFRIHF TFNDFKRNPS PRSHVSPIKQ LNGRTKTASG IRKVVRELFH
     KTNGARENAA KILVVITDGE KFGDPLDYKD VIPEADRAGV IRYVIGVGNA FNKPQSRREL
     DTIASKPAGE HVFQVDNFEA LNTIQNQLQE KIFAIEGTQT GSTSSFEHEM SQEGFSASIT
     SNGPLLGSVG SFDWAGGAFL YTSKDKVTFI NTTRVDSDMN DAYLGYASAV ILRNRVQSLV
     LGAPRYQHIG LVVMFRENFG TWEPHTSIKG SQIGSYFGAS LCSVDMDADG NTNLILIGAP
     HYYEKTRGGQ VSVCPLPRGR ARWQCEALLH GDQGHPWGRF GAALTVLGDV NGDKLTDVAI
     GAPGEQENQG AVYIFYGASI ASLSASHSHR IIGAHFSPGL QYFGQSLSGG KDLTMDGLMD
     LAVGAQGHLL LLRAQPVLRL EATMEFSPKK VARSVFACQE QVLKNKDAGE VRVCLRVRKN
     TKDRLREGDI QSTVTYDLAL DPVRSRIRAF FDETKNNTRR RTQVFGLMQK CETLKLILPD
     CVDDSVSPII LRLNYTLVGE PLRSFGNLRP VLAMDAQRFF TAMFPFEKNC GNDSICQDDL
     SITMSAMGLD TLVVGGPQDF NMSVTLRNDG EDSYGTQVTV YYPSGLSYRK DSASQNPLTK
     KPWFVKPAES SSSSEGHGAL KSTTWNINHP IFPANSEVTF NVTFDVDSHA SFGNKLLLKA
     IVASENNMSR THKTKFQLEL PVKYAIYMIV TSDESSIRYL NFTASEMTSK VIQHQYQFNN
     LGQRSLPVSV VFWIPVQINN VTVWDHPQVI FSQNLSSACH TEQKSPPHSN FRDQLERTPV
     LNCSVAVCKR IQCDLPSFNT QEIFNVTLKG NLSFDWYIKT SHGHLLLVSS TEILFNDSAF
     ALLPGQESYV RSKTETKVEP YEVHNPVPLI VGSSIGGLVL LALITAGLYK LGFFKRQYKD
     MMNEAAPQDA PPQ
//
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.
CC   -----------------------------------------------------------------------
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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   SOMA_MOUSE              Reviewed;         216 AA.
AC   P06880; Q544X1;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   08-MAR-2011, entry version 103.
DE   RecName: Full=Somatotropin;
DE   AltName: Full=Growth hormone;
DE   Flags: Precursor;
GN   Name=Gh1; Synonyms=Gh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=85261358; PubMed=2991252;
RA   Linzer D.I.H., Talamantes F.;
RT   "Nucleotide sequence of mouse prolactin and growth hormone mRNAs and
RT   expression of these mRNAs during pregnancy.";
RL   J. Biol. Chem. 260:9574-9579(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FZTDU; TISSUE=Liver;
RX   MEDLINE=96194803; PubMed=8647448; DOI=10.1016/0378-1119(95)00815-2;
RA   Das P., Meyer L., Seyfert H.-M., Brockmann G., Schwerin M.;
RT   "Structure of the growth hormone-encoding gene and its promoter in
RT   mice.";
RL   Gene 169:209-213(1996).
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=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: Plays an important role in growth control. Its major
CC       role in stimulating body growth is to stimulate the liver and
CC       other tissues to secrete IGF-1. It stimulates both the
CC       differentiation and proliferation of myoblasts. It also stimulates
CC       amino acid uptake and protein synthesis in muscle and other
CC       tissues.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the somatotropin/prolactin family.
CC   -----------------------------------------------------------------------
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DR   EMBL; X02891; CAA26650.1; -; mRNA.
DR   EMBL; Z46663; CAA86658.1; -; Genomic_DNA.
DR   EMBL; AK019952; BAB31931.1; -; mRNA.
DR   EMBL; AK019954; BAB31932.1; -; mRNA.
DR   EMBL; AK019956; BAB31933.1; -; mRNA.
DR   EMBL; AK019959; BAB31935.1; -; mRNA.
DR   EMBL; AK019961; BAB31937.1; -; mRNA.
DR   EMBL; AK030715; BAC27096.1; -; mRNA.
DR   EMBL; BC061157; AAH61157.1; -; mRNA.
DR   IPI; IPI00129161; -.
DR   PIR; B23911; STMS.
DR   RefSeq; NP_032143.1; NM_008117.2.
DR   UniGene; Mm.343934; -.
DR   ProteinModelPortal; P06880; -.
DR   SMR; P06880; 27-215.
DR   STRING; P06880; -.
DR   PhosphoSite; P06880; -.
DR   PRIDE; P06880; -.
DR   Ensembl; ENSMUST00000103071; ENSMUSP00000099360; ENSMUSG00000020713.
DR   GeneID; 14599; -.
DR   KEGG; mmu:14599; -.
DR   UCSC; uc007lys.1; mouse.
DR   CTD; 14599; -.
DR   MGI; MGI:95707; Gh.
DR   eggNOG; roNOG15682; -.
DR   HOGENOM; HBG282184; -.
DR   HOVERGEN; HBG011318; -.
DR   InParanoid; P06880; -.
DR   OMA; FVESSCA; -.
DR   OrthoDB; EOG42FSJN; -.
DR   PhylomeDB; P06880; -.
DR   NextBio; 286364; -.
DR   ArrayExpress; P06880; -.
DR   Bgee; P06880; -.
DR   CleanEx; MM_GH; -.
DR   Genevestigator; P06880; -.
DR   GermOnline; ENSMUSG00000020713; Mus musculus.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; 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:0005131; F:growth hormone receptor binding; IPI:MGI.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IDA:MGI.
DR   GO; GO:0040018; P:positive regulation of multicellular organism growth; IGI:MGI.
DR   GO; GO:0032094; P:response to food; IDA:MGI.
DR   InterPro; IPR009079; 4_helix_cytokine-like_core.
DR   InterPro; IPR012351; 4_helix_cytokine_core.
DR   InterPro; IPR001400; Somatotropin.
DR   InterPro; IPR018116; Somatotropin_CS.
DR   Gene3D; G3DSA:1.20.1250.10; 4_helix_cytokine_core; 1.
DR   PANTHER; PTHR11417; Somatotropin; 1.
DR   Pfam; PF00103; Hormone_1; 1.
DR   PRINTS; PR00836; SOMATOTROPIN.
DR   SUPFAM; SSF47266; 4_helix_cytokine; 1.
DR   PROSITE; PS00266; SOMATOTROPIN_1; 1.
DR   PROSITE; PS00338; SOMATOTROPIN_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hormone; Metal-binding; Secreted; Signal; Zinc.
FT   SIGNAL        1     26       By similarity.
FT   CHAIN        27    216       Somatotropin.
FT                                /FTId=PRO_0000032992.
FT   METAL        45     45       Zinc (By similarity).
FT   METAL       198    198       Zinc (By similarity).
FT   DISULFID     78    189       By similarity.
FT   DISULFID    206    214       By similarity.
SQ   SEQUENCE   216 AA;  24716 MW;  98666A3AE25D65FC CRC64;
     MATDSRTSWL LTVSLLCLLW PQEASAFPAM PLSSLFSNAV LRAQHLHQLA ADTYKEFERA
     YIPEGQRYSI QNAQAAFCFS ETIPAPTGKE EAQQRTDMEL LRFSLLLIQS WLGPVQFLSR
     IFTNSLMFGT SDRVYEKLKD LEEGIQALMQ ELEDGSPRVG QILKQTYDKF DANMRSDDAL
     LKNYGLLSCF KKDLHKAETY LRVMKCRRFV ESSCAF
//
ID   EGR1_MOUSE              Reviewed;         533 AA.
AC   P08046; Q61777;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   08-MAR-2011, entry version 118.
DE   RecName: Full=Early growth response protein 1;
DE            Short=EGR-1;
DE   AltName: Full=Nerve growth factor-induced protein A;
DE            Short=NGFI-A;
DE   AltName: Full=Transcription factor Zif268;
DE   AltName: Full=Zinc finger protein Krox-24;
GN   Name=Egr1; Synonyms=Egr-1, Krox-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].
RX   MEDLINE=88165055; PubMed=3127059; DOI=10.1016/0092-8674(88)90485-0;
RA   Sukhatme V.P., Cao X., Chang L.C., Tsai-Morris C.-H., Stamenkovich D.,
RA   Ferreira P.C.P., Cohen D.R., Edwards S.A., Shows T.B., Curran T.,
RA   le Beau M.M., Adamson E.D.;
RT   "A zinc finger-encoding gene coregulated with c-fos during growth and
RT   differentiation, and after cellular depolarization.";
RL   Cell 53:37-43(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=89042085; PubMed=3141919; DOI=10.1073/pnas.85.21.7857;
RA   Christy B.A., Lau L.F., Nathans D.;
RT   "A gene activated in mouse 3T3 cells by serum growth factors encodes a
RT   protein with 'zinc finger' sequences.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:7857-7861(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=90060781; PubMed=2511075; DOI=10.1016/0378-1119(89)90296-5;
RA   Janssen-Timmen U., Lemaire P., Mattei M.-G., Revelant O., Charnay P.;
RT   "Structure, chromosome mapping and regulation of the mouse zinc-finger
RT   gene Krox-24; evidence for a common regulatory pathway for immediate-
RT   early serum-response genes.";
RL   Gene 80:325-336(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 50-533.
RX   MEDLINE=88263014; PubMed=3133658; DOI=10.1073/pnas.85.13.4691;
RA   Lemaire P., Revelant O., Bravo R., Charnay P.;
RT   "Two mouse genes encoding potential transcription factors with
RT   identical DNA-binding domains are activated by growth factors in
RT   cultured cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:4691-4695(1988).
RN   [5]
RP   MUTAGENESIS OF ZINC FINGERS.
RX   MEDLINE=92156104; PubMed=1740423;
RA   Wilson T.E., Day M.L., Pexton T., Padgett K.A., Johnston M.,
RA   Milbrandt J.;
RT   "In vivo mutational analysis of the NGFI-A zinc fingers.";
RL   J. Biol. Chem. 267:3718-3724(1992).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 333-421.
RX   MEDLINE=91227904; PubMed=2028256; DOI=10.1126/science.2028256;
RA   Pavletich N.P., Pabo C.O.;
RT   "Zinc finger-DNA recognition: crystal structure of a Zif268-DNA
RT   complex at 2.1 A.";
RL   Science 252:809-817(1991).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 333-421 WITH VARIATIONS.
RX   MEDLINE=98230744; PubMed=9562555; DOI=10.1016/S0969-2126(98)00047-1;
RA   Elrod-Erickson M., Benson T.E., Pabo C.O.;
RT   "High-resolution structures of variant Zif268-DNA complexes:
RT   implications for understanding zinc finger-DNA recognition.";
RL   Structure 6:451-464(1998).
CC   -!- FUNCTION: Transcriptional regulator. Recognizes and binds to the
CC       DNA sequence 5'-CGCCCCCGC-3'(EGR-site). Activates the
CC       transcription of target genes whose products are required for
CC       mitogenesis and differentiation.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- INDUCTION: By growth factors.
CC   -!- SIMILARITY: Belongs to the EGR 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
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DR   EMBL; M20157; AAA37544.1; -; mRNA.
DR   EMBL; M22326; AAA40416.1; -; mRNA.
DR   EMBL; M28845; AAB00468.1; -; Genomic_DNA.
DR   EMBL; M28844; AAB00468.1; JOINED; Genomic_DNA.
DR   EMBL; M19643; AAA39382.1; -; mRNA.
DR   IPI; IPI00128530; -.
DR   PIR; JS0304; JS0304.
DR   RefSeq; NP_031939.1; NM_007913.5.
DR   UniGene; Mm.181959; -.
DR   PDB; 1A1F; X-ray; 2.10 A; A=333-421.
DR   PDB; 1A1G; X-ray; 1.90 A; A=333-421.
DR   PDB; 1A1H; X-ray; 1.60 A; A=333-421.
DR   PDB; 1A1I; X-ray; 1.60 A; A=333-421.
DR   PDB; 1A1J; X-ray; 2.00 A; A=333-421.
DR   PDB; 1A1K; X-ray; 1.90 A; A=333-421.
DR   PDB; 1A1L; X-ray; 2.30 A; A=333-421.
DR   PDB; 1AAY; X-ray; 1.60 A; A=333-421.
DR   PDB; 1F2I; X-ray; 2.35 A; G/H/I/J/K/L=334-389.
DR   PDB; 1G2D; X-ray; 2.20 A; C/F=333-421.
DR   PDB; 1G2F; X-ray; 2.00 A; C/F=333-421.
DR   PDB; 1JK1; X-ray; 1.90 A; A=333-421.
DR   PDB; 1JK2; X-ray; 1.65 A; A=333-421.
DR   PDB; 1LLM; X-ray; 1.50 A; C/D=364-412.
DR   PDB; 1P47; X-ray; 2.20 A; A/B=333-419.
DR   PDB; 1ZAA; X-ray; 2.10 A; C=332-418.
DR   PDBsum; 1A1F; -.
DR   PDBsum; 1A1G; -.
DR   PDBsum; 1A1H; -.
DR   PDBsum; 1A1I; -.
DR   PDBsum; 1A1J; -.
DR   PDBsum; 1A1K; -.
DR   PDBsum; 1A1L; -.
DR   PDBsum; 1AAY; -.
DR   PDBsum; 1F2I; -.
DR   PDBsum; 1G2D; -.
DR   PDBsum; 1G2F; -.
DR   PDBsum; 1JK1; -.
DR   PDBsum; 1JK2; -.
DR   PDBsum; 1LLM; -.
DR   PDBsum; 1P47; -.
DR   PDBsum; 1ZAA; -.
DR   ProteinModelPortal; P08046; -.
DR   SMR; P08046; 334-533.
DR   STRING; P08046; -.
DR   PhosphoSite; P08046; -.
DR   PRIDE; P08046; -.
DR   Ensembl; ENSMUST00000064795; ENSMUSP00000069616; ENSMUSG00000038418.
DR   GeneID; 13653; -.
DR   KEGG; mmu:13653; -.
DR   UCSC; uc008elt.1; mouse.
DR   CTD; 13653; -.
DR   MGI; MGI:95295; Egr1.
DR   eggNOG; maNOG15075; -.
DR   HOGENOM; HBG717852; -.
DR   HOVERGEN; HBG003909; -.
DR   InParanoid; P08046; -.
DR   OMA; AVPSNDS; -.
DR   OrthoDB; EOG4BP1BT; -.
DR   PhylomeDB; P08046; -.
DR   NextBio; 284384; -.
DR   ArrayExpress; P08046; -.
DR   Bgee; P08046; -.
DR   CleanEx; MM_EGR1; -.
DR   Genevestigator; P08046; -.
DR   GermOnline; ENSMUSG00000038418; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0010843; F:promoter binding; IDA:BHF-UCL.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0016563; F:transcription activator activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
DR   GO; GO:0071504; P:cellular response to heparin; ISS:UniProtKB.
DR   GO; GO:0071506; P:cellular response to mycophenolic acid; ISS:UniProtKB.
DR   GO; GO:0071445; P:cellular response to protein stimulus; IDA:MGI.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt receptor signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0072303; P:positive regulation of glomerular metanephric mesangial cell proliferation; ISS:UniProtKB.
DR   GO; GO:0009749; P:response to glucose stimulus; IDA:UniProtKB.
DR   GO; GO:0032868; P:response to insulin stimulus; IDA:UniProtKB.
DR   GO; GO:0030217; P:T cell differentiation; IMP:MGI.
DR   InterPro; IPR021839; DUF3432.
DR   InterPro; IPR021849; DUF3446.
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; PF11914; DUF3432; 1.
DR   Pfam; PF11928; DUF3446; 1.
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; Activator; DNA-binding; Metal-binding; Nucleus; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    533       Early growth response protein 1.
FT                                /FTId=PRO_0000047110.
FT   ZN_FING     336    360       C2H2-type 1.
FT   ZN_FING     366    388       C2H2-type 2.
FT   ZN_FING     394    416       C2H2-type 3.
FT   COMPBIAS     57     81       Gly/Ser-rich.
FT   CONFLICT     76     76       S -> T (in Ref. 3 and 4).
FT   CONFLICT     80     80       S -> T (in Ref. 3 and 4).
FT   STRAND      346    349
FT   HELIX       350    361
FT   TURN        369    371
FT   STRAND      374    376
FT   HELIX       378    389
FT   TURN        397    399
FT   STRAND      402    405
FT   HELIX       406    413
FT   HELIX       414    416
SQ   SEQUENCE   533 AA;  56590 MW;  36E3935767CEAA0F CRC64;
     MAAAKAEMQL MSPLQISDPF GSFPHSPTMD NYPKLEEMML LSNGAPQFLG AAGTPEGSGG
     NSSSSTSSGG GGGGGSNSGS SAFNPQGEPS EQPYEHLTTE SFSDIALNNE KAMVETSYPS
     QTTRLPPITY TGRFSLEPAP NSGNTLWPEP LFSLVSGLVS MTNPPTSSSS APSPAASSSS
     SASQSPPLSC AVPSNDSSPI YSAAPTFPTP NTDIFPEPQS QAFPGSAGTA LQYPPPAYPA
     TKGGFQVPMI PDYLFPQQQG DLSLGTPDQK PFQGLENRTQ QPSLTPLSTI KAFATQSGSQ
     DLKALNTTYQ SQLIKPSRMR KYPNRPSKTP PHERPYACPV ESCDRRFSRS DELTRHIRIH
     TGQKPFQCRI CMRNFSRSDH LTTHIRTHTG EKPFACDICG RKFARSDERK RHTKIHLRQK
     DKKADKSVVA SPAASSLSSY PSPVATSYPS PATTSFPSPV PTSYSSPGSS TYPSPAHSGF
     PSPSVATTFA SVPPAFPTQV SSFPSAGVSS SFSTSTGLSD MTATFSPRTI EIC
//
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   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
CC   -----------------------------------------------------------------------
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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   ATX1L_MOUSE             Reviewed;         687 AA.
AC   P0C7T6;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 23.
DE   RecName: Full=Ataxin-1-like;
DE   AltName: Full=Brother of ataxin-1;
GN   Name=Atxn1l; Synonyms=Boat;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16121196; DOI=10.1038/sj.emboj.7600785;
RA   Mizutani A., Wang L., Rajan H., Vig P.J.S., Alaynick W.A.,
RA   Thaler J.P., Tsai C.-C.;
RT   "Boat, an AXH domain protein, suppresses the cytotoxicity of mutant
RT   ataxin-1.";
RL   EMBO J. 24:3339-3351(2005).
RN   [3]
RP   INTERACTION WITH ATXN1 AND CIC.
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: Can suppress the cytotoxicity of ATXN1 in
CC       spinocerebellar ataxia type 1 (SCA1).
CC   -!- SUBUNIT: Homodimer. Interacts (via AXH domain) with NCOR2 (By
CC       similarity). Interacts with ATXN1 and CIC.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cell projection, dendrite.
CC       Note=Forms nuclear foci. Colocalizes with NCOR2 and HDAC3.
CC       Distributed beyond the nucleus into the cell body and dendrites in
CC       Purkinje cells and in inferior olive cells.
CC   -!- TISSUE SPECIFICITY: Expressed in neuronal cells. Highly expressed
CC       in Purkinje cells of cerebellum.
CC   -!- MISCELLANEOUS: Its overexpression suppresses the ataxia caused by
CC       polyglutamine-expanded Atxn1. Competes with mutant Atxn1 and wild-
CC       type Atxn1 for association with CIC. Decreased association of
CC       mutant Atxn1 into its CIC-containing complexes decreases the
CC       levels of mutant Atxn1-containing CIC complexes, suppressing
CC       pathology, while promoting aggregation and thus increasing nuclear
CC       inclusions.
CC   -!- SIMILARITY: Belongs to the ATXN1 family.
CC   -!- SIMILARITY: Contains 1 AXH domain.
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DR   EMBL; AC132138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00605902; -.
DR   RefSeq; NP_001074399.1; NM_001080930.1.
DR   UniGene; Mm.276770; -.
DR   ProteinModelPortal; P0C7T6; -.
DR   SMR; P0C7T6; 466-580.
DR   PhosphoSite; P0C7T6; -.
DR   PRIDE; P0C7T6; -.
DR   Ensembl; ENSMUST00000093162; ENSMUSP00000090850; ENSMUSG00000069895.
DR   GeneID; 52335; -.
DR   KEGG; mmu:52335; -.
DR   CTD; 52335; -.
DR   MGI; MGI:3694797; Atxn1l.
DR   eggNOG; maNOG08335; -.
DR   GeneTree; ENSGT00390000005939; -.
DR   HOGENOM; HBG505759; -.
DR   HOVERGEN; HBG100955; -.
DR   InParanoid; P0C7T6; -.
DR   OMA; DVCISIS; -.
DR   OrthoDB; EOG43TZTZ; -.
DR   ArrayExpress; P0C7T6; -.
DR   Bgee; P0C7T6; -.
DR   Genevestigator; P0C7T6; -.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR013723; Ataxin-1_HBP1.
DR   Pfam; PF08517; AXH; 1.
DR   SUPFAM; SSF102031; Ataxin-1_HBP1; 1.
DR   PROSITE; PS51148; AXH; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Nucleus.
FT   CHAIN         1    687       Ataxin-1-like.
FT                                /FTId=PRO_0000343710.
FT   DOMAIN      455    586       AXH.
FT   REGION       20    197       Interaction with NCOR2 and ATXN1 (By
FT                                similarity).
FT   REGION       20    197       Self-association (By similarity).
SQ   SEQUENCE   687 AA;  73374 MW;  952C394FFB6B8300 CRC64;
     MKPVHERSQE CLPPKKRDLP VTSEDMGRTT SCSTNHTPSS DASEWSRGVV VAGQSQTGAR
     VSLGGDGTEA ITGLTVDQYG MLYKVAVPPA TFSPTGLPSV VNMSPLPPTF NVASSLIQHP
     GIHYPPVHYA QLPSTSLQFI GSPYSLPYAV PPNFLPSPLL SPSANLATTH LPHFVPYASL
     LAEEATPPPQ AASPAQSFNK SSSATSPPGQ LPHHSNTQPL DLAPGRMPIY YQMSRLPAGY
     TLHETSTAGA SPILTPQEGQ SALEAAAANG QRQRERNVRR ESEALDSASS KGESQGLVPV
     VECMADGQLF SGSQTPRVEV AAPAHRGTPD TDLEVQRVVG ALASQDYRVV AAQRKDEPSP
     LNLSHHNLDH QGEGRGSARN PTELVEKSQA RVFYPQSHQE PVKHRPLPKA MVVANGNLVP
     TGTDPSLLPV GSEILVASSL DLQARATFPD KEPTPPPVTS SHLPSHFMKG AIIQLATGEL
     KRVEDLQTQD FVRSAEVSGG LKIDSSTVVD IQESQWPGFV MLHFVVGEQQ SKVSIEVPPE
     HPFFVYGQGW SSCSPGRTAQ LFSLPCHRLQ VGDVCISISL QSLNSNSVSQ ASCAPPGQLG
     TPRERPERTV LGPRDLCDSE GKNQPSGEGS RVGEPSQPEP GAQACWPAPS FQRFSMQGEE
     ARAAMLRPSF IPQEVKLSIE GRSNAGK
//
ID   CTF8A_MOUSE             Reviewed;         533 AA.
AC   P0CG14; P0C6T0; Q8BHM2; Q8R5A5;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   RecName: Full=Chromosome transmission fidelity protein 8 homolog isoform 2;
GN   Name=Chtf8; Synonyms=Derpc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; 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=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., 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: Potential tumor suppressor (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2; Synonyms=DERPC;
CC         IsoId=P0CG14-1; Sequence=Displayed;
CC       Name=1;
CC         IsoId=P0CG15-1; Sequence=External;
CC   -!- SIMILARITY: Belongs to the DERPC family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK165993; BAE38506.1; -; mRNA.
DR   IPI; IPI00330037; -.
DR   RefSeq; NP_663387.3; NM_145412.3.
DR   UniGene; Mm.392086; -.
DR   ProteinModelPortal; P0CG14; -.
DR   Ensembl; ENSMUST00000057107; ENSMUSP00000058741; ENSMUSG00000046691.
DR   GeneID; 214987; -.
DR   KEGG; mmu:214987; -.
DR   NMPDR; fig|10090.3.peg.19191; -.
DR   CTD; 214987; -.
DR   MGI; MGI:2443370; Chtf8.
DR   eggNOG; maNOG16381; -.
DR   GeneTree; ENSGT00390000013870; -.
DR   HOGENOM; HBG126988; -.
DR   HOVERGEN; HBG107809; -.
DR   OrthoDB; EOG45DWPD; -.
DR   NextBio; 374562; -.
DR   Bgee; P0CG14; -.
DR   CleanEx; MM_5830457O10RIK; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Nucleus.
FT   CHAIN         1    533       Chromosome transmission fidelity protein
FT                                8 homolog isoform 2.
FT                                /FTId=PRO_0000326397.
FT   COMPBIAS      4    533       Pro-rich.
FT   COMPBIAS     95    374       Gly-rich.
SQ   SEQUENCE   533 AA;  52244 MW;  0399DF3ABE73C5F6 CRC64;
     MKEPRIFPRE RPTPWTRAPL PPRGRLDGGP VMNAGHPMGV NSDPFLMAAG SLGGNLAPFP
     RNAAPFQNPS GSLASNPAHF AAGARDPGMT SFPRGMNPTG TGAVSFPRPG GLLGPGPGPG
     LNPRTGALPG PGPMSNPRLG GLPGPGPMAN PRAGGLLGAS PDPRSGGPMV PGCGPNMRAG
     VLSSGTGPPN PRPVGLGPGP SPNLRSSFLG TNPAPRSGMF PGPGLGPNPR ACGLGPGLGP
     NPRAGGLGPG PNLDNRAGGL LGTGSGLNLR MAGPQGLDLA PILRAAGLLG TNSVSFSQAS
     GNMGTNPPTM TRVPGPIGPN TGPSSRGLGL PGPNPSPMSR APGPMGPNSA HFSRPGGPMG
     VNAGVFPRGT GSGGLNPNAF SQSSGTLASN PGTFQRSAGL QGSNQAVFPR ASGPLGPNPA
     NFPRATGLQG PSPAAFPRSA GPLGPGQVAF PRSAAGHLGS SPAGPVGINP APFARPTGTL
     GLNPASFPRM NGPVGKTLVP FPRVGSLPGS NPAAFPRPGG PMAAMYPNGM LPP
//
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.
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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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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   COX5A_MOUSE             Reviewed;         146 AA.
AC   P12787; Q9D2W1;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Cytochrome c oxidase subunit 5A, mitochondrial;
DE   AltName: Full=Cytochrome c oxidase polypeptide Va;
DE   Flags: Precursor;
GN   Name=Cox5a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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=Bone marrow;
RX   MEDLINE=89385997; PubMed=2550898; DOI=10.1093/nar/17.16.6723;
RA   Ayane M., Nielson P.J., Koehler G.;
RT   "Nucleotide sequence of cDNA encoding mouse cytochrome c oxidase
RT   subunit Va.";
RL   Nucleic Acids Res. 17:6723-6723(1989).
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-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   PROTEIN SEQUENCE OF 69-83 AND 95-103, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: This is the heme A-containing chain of cytochrome c
CC       oxidase, the terminal oxidase in mitochondrial electron transport.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 5A family.
CC   -----------------------------------------------------------------------
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DR   EMBL; X15963; CAA34085.1; -; mRNA.
DR   EMBL; AK018723; BAB31369.1; -; mRNA.
DR   EMBL; BC034302; AAH34302.1; -; mRNA.
DR   IPI; IPI00120719; -.
DR   PIR; S05495; S05495.
DR   RefSeq; NP_031773.2; NM_007747.2.
DR   UniGene; Mm.273403; -.
DR   ProteinModelPortal; P12787; -.
DR   SMR; P12787; 42-146.
DR   STRING; P12787; -.
DR   PhosphoSite; P12787; -.
DR   SWISS-2DPAGE; P12787; -.
DR   UCD-2DPAGE; P12787; -.
DR   PRIDE; P12787; -.
DR   Ensembl; ENSMUST00000000090; ENSMUSP00000000090; ENSMUSG00000000088.
DR   GeneID; 12858; -.
DR   KEGG; mmu:12858; -.
DR   CTD; 12858; -.
DR   MGI; MGI:88474; Cox5a.
DR   eggNOG; roNOG17446; -.
DR   GeneTree; ENSGT00390000001424; -.
DR   HOGENOM; HBG381551; -.
DR   HOVERGEN; HBG051088; -.
DR   InParanoid; P12787; -.
DR   OMA; HHEETFE; -.
DR   OrthoDB; EOG4D7Z71; -.
DR   PhylomeDB; P12787; -.
DR   NextBio; 282416; -.
DR   ArrayExpress; P12787; -.
DR   Bgee; P12787; -.
DR   CleanEx; MM_COX5A; -.
DR   Genevestigator; P12787; -.
DR   GermOnline; ENSMUSG00000000088; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR003204; Cyt_c_oxidase_su5A.
DR   Gene3D; G3DSA:1.25.40.40; Cyt_c_ox5A; 1.
DR   PANTHER; PTHR14200; Cyt_c_ox5A; 1.
DR   Pfam; PF02284; COX5A; 1.
DR   SUPFAM; SSF48479; Cyt_c_ox5A; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Iron; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; Transit peptide.
FT   TRANSIT       1     37       Mitochondrion.
FT   CHAIN        38    146       Cytochrome c oxidase subunit 5A,
FT                                mitochondrial.
FT                                /FTId=PRO_0000006101.
FT   CONFLICT     11     11       Missing (in Ref. 1; CAA34085).
SQ   SEQUENCE   146 AA;  16101 MW;  8F6AFF91B5C6160F CRC64;
     MLAAALRRCT AAAAARGLLH PASAPSPAAA VCSIRCYSHG SHETDEEFDA RWVTYFNKPD
     IDAWELRKGM NTLVGYDLVP EPKIIDAALR ACRRLNDFAS AVRILEVVKD KAGPHKEIYP
     YVIQELRPTL NELGISTPEE LGLDKV
//
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   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   AT1B1_MOUSE             Reviewed;         304 AA.
AC   P14094;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   08-MAR-2011, entry version 105.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit beta-1;
DE   AltName: Full=Sodium/potassium-dependent ATPase subunit beta-1;
GN   Name=Atp1b1; Synonyms=Atp4b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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=90098791; PubMed=2557580;
RA   Gloor S.;
RT   "Cloning and nucleotide sequence of the mouse Na,K-ATPase beta-
RT   subunit.";
RL   Nucleic Acids Res. 17:10117-10117(1989).
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   PROTEIN SEQUENCE OF 15-21; 72-107; 171-179; 205-217; 225-249 AND
RP   279-291, 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 33-304.
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   INTERACTION WITH NKAIN1, NKAIN2, AND NKAIN4.
RC   STRAIN=C57BL/6;
RX   PubMed=17606467; DOI=10.1093/hmg/ddm167;
RA   Gorokhova S., Bibert S., Geering K., Heintz N.;
RT   "A novel family of transmembrane proteins interacting with beta
RT   subunits of the Na,K-ATPase.";
RL   Hum. Mol. Genet. 16:2394-2410(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-101, 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   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-158; ASN-163 AND ASN-266,
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: This is the non-catalytic component of the active
CC       enzyme, which catalyzes the hydrolysis of ATP coupled with the
CC       exchange of Na(+) and K(+) ions across the plasma membrane. The
CC       beta subunit regulates, through assembly of alpha/beta
CC       heterodimers, the number of sodium pumps transported to the plasma
CC       membrane.
CC   -!- SUBUNIT: Composed of three subunits: alpha (catalytic), beta and
CC       gamma. Interacts with NKAIN1, NKAIN2 and NKAIN4.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta
CC       family.
CC   -----------------------------------------------------------------------
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DR   EMBL; X16646; CAA34639.1; -; mRNA.
DR   EMBL; BC027319; AAH27319.1; -; mRNA.
DR   EMBL; X61433; CAA43675.1; -; mRNA.
DR   IPI; IPI00121550; -.
DR   PIR; S09601; S09601.
DR   RefSeq; NP_033851.1; NM_009721.5.
DR   UniGene; Mm.4550; -.
DR   ProteinModelPortal; P14094; -.
DR   SMR; P14094; 18-304.
DR   STRING; P14094; -.
DR   PhosphoSite; P14094; -.
DR   PRIDE; P14094; -.
DR   Ensembl; ENSMUST00000027863; ENSMUSP00000027863; ENSMUSG00000026576.
DR   GeneID; 11931; -.
DR   KEGG; mmu:11931; -.
DR   UCSC; uc007dip.1; mouse.
DR   CTD; 11931; -.
DR   MGI; MGI:88108; Atp1b1.
DR   eggNOG; roNOG16210; -.
DR   HOGENOM; HBG446583; -.
DR   HOVERGEN; HBG050603; -.
DR   InParanoid; P14094; -.
DR   OMA; GFKPKPP; -.
DR   OrthoDB; EOG4M3998; -.
DR   PhylomeDB; P14094; -.
DR   NextBio; 280017; -.
DR   ArrayExpress; P14094; -.
DR   Bgee; P14094; -.
DR   CleanEx; MM_ATP1B1; -.
DR   CleanEx; MM_ATP4B; -.
DR   Genevestigator; P14094; -.
DR   GermOnline; ENSMUSG00000026576; Mus musculus.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0005391; F:sodium:potassium-exchanging ATPase activity; IEA:InterPro.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   InterPro; IPR000402; ATPase_P-typ_cation-exchng_bsu.
DR   InterPro; IPR015565; ATPase_P-typ_Na/K-dep_b1su.
DR   PANTHER; PTHR11523; ATPase_H_Na/K_b; 1.
DR   PANTHER; PTHR11523:SF10; Na/K_ATPaseBeta1; 1.
DR   Pfam; PF00287; Na_K-ATPase; 1.
DR   TIGRFAMs; TIGR01107; Na_K_ATPase_bet; 1.
DR   PROSITE; PS00390; ATPASE_NA_K_BETA_1; 1.
DR   PROSITE; PS00391; ATPASE_NA_K_BETA_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Ion transport; Membrane; Phosphoprotein; Potassium;
KW   Potassium transport; Signal-anchor; Sodium; Sodium transport;
KW   Sodium/potassium transport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    304       Sodium/potassium-transporting ATPase
FT                                subunit beta-1.
FT                                /FTId=PRO_0000219098.
FT   TOPO_DOM      1     34       Cytoplasmic (Potential).
FT   TRANSMEM     35     62       Helical; Signal-anchor for type II
FT                                membrane protein; (Potential).
FT   TOPO_DOM     63    304       Extracellular (Potential).
FT   MOD_RES     101    101       Phosphotyrosine.
FT   CARBOHYD    158    158       N-linked (GlcNAc...).
FT   CARBOHYD    163    163       N-linked (GlcNAc...).
FT   CARBOHYD    193    193       N-linked (GlcNAc...) (By similarity).
FT   CARBOHYD    266    266       N-linked (GlcNAc...).
FT   DISULFID    126    149       By similarity.
FT   DISULFID    159    175       By similarity.
FT   DISULFID    214    277       By similarity.
SQ   SEQUENCE   304 AA;  35195 MW;  8E15D8F860932680 CRC64;
     MARGKAKEEG SWKKFIWNSE KKEFLGRTGG SWFKILLFYV IFYGCLAGIF IGTIQVMLLT
     ISELKPTYQD RVAPPGLTQI PQIQKTEISF RPNDPKSYEA YVLNIIRFLE KYKDSAQKDD
     MIFEDCGNVP SEPKERGDIN HERGERKVCR FKLDWLGNCS GLNDDSYGYR EGKPCIIIKL
     NRVLGFKPKP PKNESLETYP LMMKYNPNVL PVQCTGKRDE DKDKVGNIEY FGMGGYYGFP
     LQYYPYYGKL LQPKYLQPLL AVQFTNLTVD TEIRVECKAY GENIGYSEKD RFQGRFDVKI
     EIKS
//
ID   INSR_MOUSE              Reviewed;        1372 AA.
AC   P15208;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   08-MAR-2011, entry version 130.
DE   RecName: Full=Insulin receptor;
DE            Short=IR;
DE            EC=2.7.10.1;
DE   AltName: CD_antigen=CD220;
DE   Contains:
DE     RecName: Full=Insulin receptor subunit alpha;
DE   Contains:
DE     RecName: Full=Insulin receptor subunit beta;
DE   Flags: Precursor;
GN   Name=Insr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=90094325; PubMed=2557333;
RA   Flores-Riveros J.R., Sibley E., Kastelic T., Lane M.D.;
RT   "Substrate phosphorylation catalyzed by the insulin receptor tyrosine
RT   kinase. Kinetic correlation to autophosphorylation of specific sites
RT   in the beta subunit.";
RL   J. Biol. Chem. 264:21557-21572(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
RX   MEDLINE=90099338; PubMed=2602374; DOI=10.1073/pnas.86.24.9732;
RA   Sibley E., Kastelic T., Kelly T.J., Lane M.D.;
RT   "Characterization of the mouse insulin receptor gene promoter.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:9732-9736(1989).
RN   [3]
RP   INTERACTION WITH SORBS1.
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1179, 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-1179, 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   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-445, 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-445, 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   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   -!- FUNCTION: This receptor binds insulin and has a tyrosine-protein
CC       kinase activity. When present in a hybrid receptor with IGF1R,
CC       binds IGF1.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- COFACTOR: Manganese (By similarity).
CC   -!- ENZYME REGULATION: Autophosphorylation activates the kinase
CC       activity.
CC   -!- SUBUNIT: Tetramer of 2 alpha and 2 beta chains linked by disulfide
CC       bonds. The alpha chains contribute to the formation of the ligand-
CC       binding domain, while the beta chains carry the kinase domain.
CC       Interacts with SORBS1 but dissociates from it following insulin
CC       stimulation. Binds SH2B2. Interacts with the PTB/PID domains of
CC       IRS1 and SHC1 in vitro when autophosphorylated on tyrosine
CC       residues. The sequences surrounding the phosphorylated NPXY motif
CC       contribute differentially to either IRS1 or SHC1 recognition.
CC       Interacts with the SH2 domains of the 85 kDa regulatory subunit of
CC       PI3K (PIK3R1) in vitro, when autophosphorylated on tyrosine
CC       residues. Interacts with SOCS7. Forms a hybrid receptor with
CC       IGF1R, the hybrid is a tetramer consisting of 1 alpha chain and 1
CC       beta chain of INSR and 1 alpha chain and 1 beta chain of IGF1R.
CC       Interacts with CAV2 (tyrosine-phosphorylated form); the
CC       interaction is increased with 'Tyr-27'phosphorylation of CAV2 (By
CC       similarity). Interacts with ARRB2. Interacts with GRB10; this
CC       interaction blocks the association between IRS1/IRS2 and INSR,
CC       significantly reduces insulin-stimulated tyrosine phosphorylation
CC       of IRS1 and IRS2 and thus decreases insulin signaling (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- PTM: Autophosphorylated on tyrosine residues in response to
CC       insulin (By similarity).
CC   -!- PTM: Phosphorylation of Tyr-989 is required for IRS1- and SHC1-
CC       binding (By similarity).
CC   -!- PTM: Dephosphorylated by PTPRE on Tyr-989, Tyr-1175, Tyr-1179 and
CC       Tyr-1180 residues (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Insulin receptor subfamily.
CC   -!- SIMILARITY: Contains 3 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; J05149; AAA39318.1; -; mRNA.
DR   EMBL; M28869; AAA39319.1; -; Genomic_DNA.
DR   IPI; IPI00128358; -.
DR   PIR; A34157; A34157.
DR   RefSeq; NP_034698.2; NM_010568.2.
DR   UniGene; Mm.268003; -.
DR   PDB; 1LK2; X-ray; 1.35 A; P=423-430.
DR   PDBsum; 1LK2; -.
DR   ProteinModelPortal; P15208; -.
DR   SMR; P15208; 31-938, 998-1300.
DR   DIP; DIP-41452N; -.
DR   MINT; MINT-1516207; -.
DR   STRING; P15208; -.
DR   PhosphoSite; P15208; -.
DR   PRIDE; P15208; -.
DR   Ensembl; ENSMUST00000091291; ENSMUSP00000088837; ENSMUSG00000005534.
DR   GeneID; 16337; -.
DR   KEGG; mmu:16337; -.
DR   UCSC; uc009krc.2; mouse.
DR   CTD; 16337; -.
DR   MGI; MGI:96575; Insr.
DR   HOGENOM; HBG316019; -.
DR   HOVERGEN; HBG006134; -.
DR   InParanoid; P15208; -.
DR   OrthoDB; EOG48WC15; -.
DR   BRENDA; 2.7.10.1; 244.
DR   NextBio; 289438; -.
DR   ArrayExpress; P15208; -.
DR   Bgee; P15208; -.
DR   CleanEx; MM_INSR; -.
DR   Genevestigator; P15208; -.
DR   GermOnline; ENSMUSG00000005534; Mus musculus.
DR   GO; GO:0005901; C:caveola; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043559; F:insulin binding; ISS:UniProtKB.
DR   GO; GO:0005009; F:insulin receptor activity; ISS:UniProtKB.
DR   GO; GO:0043560; F:insulin receptor substrate binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISS:UniProtKB.
DR   GO; GO:0051425; F:PTB domain binding; ISS:UniProtKB.
DR   GO; GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:MGI.
DR   GO; GO:0031017; P:exocrine pancreas development; IMP:MGI.
DR   GO; GO:0030238; P:male sex determination; IMP:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR   GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
DR   InterPro; IPR000494; EGF_rcpt_L.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR   InterPro; IPR006212; Furin_repeat.
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; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR016246; Tyr_kinase_insulin-like_rcpt.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   InterPro; IPR002011; Tyr_prot_kinase_rcpt_2_CS.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 4.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF00757; Furin-like; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF01030; Recep_L_domain; 2.
DR   PIRSF; PIRSF000620; Insulin_receptor; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00261; FU; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; FN_III-like; 2.
DR   SUPFAM; SSF57184; Grow_fac_recept; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50853; FN3; 3.
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   3D-structure; Acetylation; ATP-binding;
KW   Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW   Kinase; Manganese; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Receptor; Repeat; Signal; Transferase; Transmembrane;
KW   Transmembrane helix; Tyrosine-protein kinase.
FT   SIGNAL        1     27
FT   CHAIN        28    748       Insulin receptor subunit alpha.
FT                                /FTId=PRO_0000016693.
FT   CHAIN       753   1372       Insulin receptor subunit beta.
FT                                /FTId=PRO_0000016695.
FT   TOPO_DOM    753    946       Extracellular (Potential).
FT   TRANSMEM    947    967       Helical; (Potential).
FT   TOPO_DOM    968   1372       Cytoplasmic (Potential).
FT   DOMAIN      624    697       Fibronectin type-III 1.
FT   DOMAIN      747    832       Fibronectin type-III 2.
FT   DOMAIN      840    936       Fibronectin type-III 3.
FT   DOMAIN     1013   1288       Protein kinase.
FT   NP_BIND    1019   1027       ATP (By similarity).
FT   REGION      986    989       IRS1 and SHC binding (By similarity).
FT   REGION     1351   1354       PIK3R1 binding (By similarity).
FT   ACT_SITE   1149   1149       Proton acceptor (By similarity).
FT   BINDING    1047   1047       ATP.
FT   SITE        989    989       Important for biological activity.
FT   MOD_RES     400    400       Phosphoserine (By similarity).
FT   MOD_RES     401    401       Phosphotyrosine (By similarity).
FT   MOD_RES     407    407       Phosphoserine (By similarity).
FT   MOD_RES     989    989       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1054   1054       Phosphoserine (By similarity).
FT   MOD_RES    1102   1102       N6-acetyllysine (By similarity).
FT   MOD_RES    1175   1175       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1179   1179       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1180   1180       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1338   1338       Phosphoserine (By similarity).
FT   MOD_RES    1345   1345       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1351   1351       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1369   1369       Phosphoserine (By similarity).
FT   CARBOHYD     43     43       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     52     52       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    105    105       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    138    138       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    242    242       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    282    282       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    322    322       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    364    364       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    424    424       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    445    445       N-linked (GlcNAc...).
FT   CARBOHYD    541    541       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    635    635       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    653    653       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    700    700       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    759    759       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    772    772       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    910    910       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    923    923       N-linked (GlcNAc...) (Potential).
FT   DISULFID    219    228       By similarity.
FT   DISULFID    223    234       By similarity.
FT   DISULFID    235    243       By similarity.
FT   DISULFID    239    252       By similarity.
FT   DISULFID    255    264       By similarity.
FT   DISULFID    268    280       By similarity.
FT   DISULFID    286    293       By similarity.
FT   DISULFID    301    311       By similarity.
FT   DISULFID    315    328       By similarity.
FT   DISULFID    331    335       By similarity.
FT   DISULFID    462    495       By similarity.
FT   DISULFID    551    551       Interchain (By similarity).
SQ   SEQUENCE   1372 AA;  155640 MW;  1DA2A0BB74618964 CRC64;
     MGFGRGCETT AVPLLVAVAA LLVGTAGHLY PGEVCPGMDI RNNLTRLHEL ENCSVIEGHL
     QILLMFKTRP EDFRDLSFPK LIMITDYLLL FRVYGLESLK DLFPNLTVIR GSRLFFNYAL
     VIFEMVHLKE LGLYNLMNIT RGSVRIEKNN ELCYLATIDW SRILDSVEDN YIVLNKDDNE
     ECGDVCPGTA KGKTNCPATV INGQFVERCW THSHCQKVCP TICKSHGCTA EGLCCHKECL
     GNCSEPDDPT KCVACRNFYL DGQCVETCPP PYYHFQDWRC VNFSFCQDLH FKCRNSRKPG
     CHQYVIHNNK CIPECPSGYT MNSSNLMCTP CLGPCPKVCQ ILEGEKTIDS VTSAQELRGC
     TVINGSLIIN IRGGNNLAAE LEANLGLIEE ISGFLKIRRS YALVSLSFFR KLHLIRGETL
     EIGNYSFYAL DNQNLRQLWD WSKHNLTITQ GKLFFHYNPK LCLSEIHKME EVSGTKGRQE
     RNDIALKTNG DQASCENELL KFSFIRTSFD KILLRWEPYW PPDFRDLLGF MLFYKEAPYQ
     NVTEFDGQDA CGSNSWTVVD IDPPQRSNDP KSQTPSHPGW LMRGLKPWTQ YAIFVKTLVT
     FSDERRTYGA KSDIIYVQTD ATNPSVPLDP ISVSNSSSQI ILKWKPPSDP NGNITHYLVY
     WERQAEDSEL FELDYCLKGL KLPSRTWSPP FESDDSQKHN QSEYDDSASE CCSCPKTDSQ
     ILKELEESSF RKTFEDYLHN VVFVPRPSRK RRSLEEVGNV TATTLTLPDF PNVSSTIVPT
     SQEEHRPFEK VVNKESLVIS GLRHFTGYRI ELQACNQDSP DERCSVAAYV SARTMPEAKA
     DDIVGPVTHE IFENNVVHLM WQEPKEPNGL IVLYEVSYRR YGDEELHLCV SRKHFALERG
     CRLRGLSPGN YSVRVRATSL AGNGSWTEPT YFYVTDYLDV PSNIAKIIIG PLIFVFLFSV
     VIGSIYLFLR KRQPDGPMGP LYASSNPEYL SASDVFPSSV YVPDEWEVPR EKITLLRELG
     QGSFGMVYEG NAKDIIKGEA ETRVAVKTVN ESASLRERIE FLNEASVMKG FTCHHVVRLL
     GVVSKGQPML VVMELMAHGD LKSHLRSLRP DAENNPGRPP PTLQEMIQMT AEIADGMAYL
     NAKKFVHRDL AARNCMVAHD FTVKIGDFGM TRDIYETDYY RKGGKGLLPV RWMSPESLKD
     GVFTASSDMW SFGVVLWEIT SLAEQPYQGL SNEQVLKFVM DGGYLDPPDN CPERLTDLMR
     MCWQFNPKMR PTFLEIVNLL KDDLHPSFPE VSFFYSEENK APESEELEME FEDMENVPLD
     RSSHCQREEA GGREGGSSLS IKRTYDEHIP YTHMNGGKKN GRVLTLPRSN PS
//
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   SPTA2_MOUSE             Reviewed;        2472 AA.
AC   P16546; A3KGU6; A3KGU8; Q8K380; Q9CT05;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 4.
DT   30-NOV-2010, entry version 114.
DE   RecName: Full=Spectrin alpha chain, brain;
DE   AltName: Full=Alpha-II spectrin;
DE   AltName: Full=Fodrin alpha chain;
DE   AltName: Full=Spectrin, non-erythroid alpha chain;
GN   Name=Sptan1; Synonyms=Spna2, Spta2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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   PROTEIN SEQUENCE OF 8-18; 46-51; 64-81; 85-121; 130-137; 169-227;
RP   251-259; 263-272; 275-295; 321-347; 382-402; 419-439; 442-459;
RP   523-547; 614-627; 686-708; 734-742; 792-801; 813-839; 847-862;
RP   908-930; 990-1002; 1013-1022; 1068-1082; 1197-1209; 1253-1273;
RP   1314-1326; 1350-1359; 1370-1380; 1418-1427; 1501-1519; 1547-1570;
RP   1592-1605; 1608-1619; 1700-1713; 1716-1736; 1772-1781; 1784-1794;
RP   1808-1828; 1830-1844; 1866-1923; 1926-1938; 1985-1995; 2018-2040;
RP   2065-2075; 2088-2098; 2138-2155; 2265-2281; 2354-2382; 2405-2435 AND
RP   2455-2467, 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 995-1396 (ISOFORM 2).
RC   TISSUE=Macrophage;
RX   MEDLINE=90254195; PubMed=2111175; DOI=10.1016/0300-9084(90)90168-G;
RA   Sri Widada J., Asselin J., Colote S., Ferraz C., Trave G., Afshar M.,
RA   Haiech J., Liautard J.-P.;
RT   "Identification of the calmodulin binding domain of alpha-fodrin and
RT   implications for folding.";
RL   Biochimie 72:19-24(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 995-1396 (ISOFORM 2).
RX   MEDLINE=89178662; PubMed=2926814; DOI=10.1016/0022-2836(89)90355-0;
RA   Sri Widada J., Asselin J., Colote S., Marti J., Ferraz C., Trave G.,
RA   Haiech J., Liautard J.-P.;
RT   "Cloning and deletion mutagenesis using direct protein-protein
RT   interaction on an expression vector. Identification of the calmodulin
RT   binding domain of alpha-fodrin.";
RL   J. Mol. Biol. 205:455-458(1989).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1118-2472.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, 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 1819-2472.
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   PROTEIN SEQUENCE OF 2071-2079.
RC   STRAIN=C57BL/6Cr; 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1217, 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-1217, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
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-1029, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., 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 THR-667 AND SER-1217, 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: 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: Interacts with CALM and EMD (By similarity). Like
CC       erythrocyte spectrin, the spectrin-like proteins are capable of
CC       forming dimers which can further associate to tetramers. Interacts
CC       with ACP1. Interacts (via C-terminal spectrin repeats) with TRPC4
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell
CC       cortex.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P16546-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P16546-2; Sequence=VSP_022093;
CC   -!- PTM: Phosphorylation of Tyr-1176 decreases sensitivity to cleavage
CC       by calpain in vitro (By similarity).
CC   -!- SIMILARITY: Belongs to the spectrin family.
CC   -!- SIMILARITY: Contains 3 EF-hand domains.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SIMILARITY: Contains 23 spectrin repeats.
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DR   EMBL; AL928926; CAM46236.1; -; Genomic_DNA.
DR   EMBL; AL928926; CAM46238.1; -; Genomic_DNA.
DR   EMBL; X12801; CAA31289.1; -; mRNA.
DR   EMBL; BC027791; AAH27791.1; -; mRNA.
DR   EMBL; AK011566; BAB27703.1; -; mRNA.
DR   IPI; IPI00753793; -.
DR   IPI; IPI00753815; -.
DR   PIR; A43769; A43769.
DR   PIR; PC7076; PC7076.
DR   UniGene; Mm.204969; -.
DR   ProteinModelPortal; P16546; -.
DR   SMR; P16546; 8-956, 970-1024, 1093-2472.
DR   STRING; P16546; -.
DR   PhosphoSite; P16546; -.
DR   UCD-2DPAGE; P16546; -.
DR   PRIDE; P16546; -.
DR   Ensembl; ENSMUST00000095083; ENSMUSP00000092697; ENSMUSG00000057738.
DR   UCSC; uc008jar.1; mouse.
DR   UCSC; uc008jas.1; mouse.
DR   MGI; MGI:98386; Spna2.
DR   HOVERGEN; HBG059266; -.
DR   ArrayExpress; P16546; -.
DR   Bgee; P16546; -.
DR   CleanEx; MM_SPNA2; -.
DR   Genevestigator; P16546; -.
DR   GermOnline; ENSMUSG00000057738; Mus musculus.
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:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:MGI.
DR   GO; GO:0030507; F:spectrin binding; IDA:MGI.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Acetylation; Actin capping; Actin-binding; Alternative splicing;
KW   Calcium; Calmodulin-binding; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Phosphoprotein; Repeat; SH3 domain.
FT   CHAIN         1   2472       Spectrin alpha chain, brain.
FT                                /FTId=PRO_0000073456.
FT   REPEAT       10     42       Spectrin 1.
FT   REPEAT       44    147       Spectrin 2.
FT   REPEAT      149    253       Spectrin 3.
FT   REPEAT      255    359       Spectrin 4.
FT   REPEAT      361    465       Spectrin 5.
FT   REPEAT      467    571       Spectrin 6.
FT   REPEAT      573    676       Spectrin 7.
FT   REPEAT      678    782       Spectrin 8.
FT   REPEAT      784    888       Spectrin 9.
FT   REPEAT      890    955       Spectrin 10.
FT   DOMAIN      967   1026       SH3.
FT   REPEAT     1062   1089       Spectrin 11.
FT   REPEAT     1091   1161       Spectrin 12.
FT   REPEAT     1208   1231       Spectrin 13.
FT   REPEAT     1233   1337       Spectrin 14.
FT   REPEAT     1339   1443       Spectrin 15.
FT   REPEAT     1445   1549       Spectrin 16.
FT   REPEAT     1551   1656       Spectrin 17.
FT   REPEAT     1658   1762       Spectrin 18.
FT   REPEAT     1764   1868       Spectrin 19.
FT   REPEAT     1870   1974       Spectrin 20.
FT   REPEAT     1976   2081       Spectrin 21.
FT   REPEAT     2091   2195       Spectrin 22.
FT   REPEAT     2205   2310       Spectrin 23.
FT   DOMAIN     2323   2358       EF-hand 1.
FT   DOMAIN     2366   2401       EF-hand 2.
FT   DOMAIN     2404   2439       EF-hand 3.
FT   CA_BIND    2336   2347       1 (Potential).
FT   CA_BIND    2379   2390       2 (Potential).
FT   SITE       1176   1177       Cleavage; by mu-calpain (By similarity).
FT   MOD_RES     592    592       N6-acetyllysine (By similarity).
FT   MOD_RES     613    613       N6-acetyllysine (By similarity).
FT   MOD_RES     637    637       N6-acetyllysine (By similarity).
FT   MOD_RES     667    667       Phosphothreonine.
FT   MOD_RES     779    779       N6-acetyllysine (By similarity).
FT   MOD_RES     976    976       Phosphotyrosine (By similarity).
FT   MOD_RES    1029   1029       Phosphoserine.
FT   MOD_RES    1031   1031       Phosphoserine (By similarity).
FT   MOD_RES    1176   1176       Phosphotyrosine (By similarity).
FT   MOD_RES    1217   1217       Phosphoserine.
FT   MOD_RES    1323   1323       Phosphoserine (By similarity).
FT   MOD_RES    1519   1519       N6-acetyllysine (By similarity).
FT   MOD_RES    2052   2052       N6-acetyllysine (By similarity).
FT   MOD_RES    2421   2421       N6-acetyllysine (By similarity).
FT   MOD_RES    2423   2423       Phosphotyrosine (By similarity).
FT   VAR_SEQ    1053   1072       Missing (in isoform 2).
FT                                /FTId=VSP_022093.
FT   CONFLICT    995    995       T -> A (in Ref. 3; CAA31289).
FT   CONFLICT   1156   1156       D -> G (in Ref. 3; CAA31289).
FT   CONFLICT   1204   1204       T -> S (in Ref. 3; CAA31289).
FT   CONFLICT   1279   1279       E -> D (in Ref. 3; CAA31289).
FT   CONFLICT   1396   1396       Q -> P (in Ref. 3; CAA31289).
FT   CONFLICT   1819   1819       A -> S (in Ref. 6; BAB27703).
SQ   SEQUENCE   2472 AA;  284597 MW;  7D778AC0B32D0AD6 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 DPTNIQSKHQ KHQAFEAELH ANADRIRGVI DMGNSLIERG
     ACAGSEDAVK ARLAALADQW QFLVQKSAEK SQKLKEANKQ QNFNTGIKDF DFWLSEVEAL
     LASEDYGKDL ASVNNLLKKH QLLEADISAH EDRLKDLNSQ ADSLMTSSAF DTSQVKEKRD
     TINGRFQKIK SMATSRRAKL SESHRLHQFF RDMDDEESWI KEKKLLVSSE DYGRDLTGVQ
     NLRKKHKRLE AELAAHEPAI QGVLDTGKKL SDDNTIGQEE IQQRLAQFVE HWKELKQLAA
     ARGQRLEESL EYQQFVANVE EEEAWINEKM TLVASEDYGD TLAAIQGLLK KHEAFETDFT
     VHKDRVNDVC TNGQDLIKKN NHHEENISSK MKGLNGKVSD LEKAAAQRKA KLDENSAFLQ
     FNWKADVVES WIGEKENSLK TDDYGRDLSS VQTLLTKQET FDAGLQAFQQ EGIANITALK
     DQLLAAKHIQ SKAIEARHAS LMKRWTQLLA NSATRKKKLL EAQSHFRKVE DLFLTFAKKA
     SAFNSWFENA EEDLTDPVRC NSLEEIKALR EAHDAFRSSL SSAQADFNQL AELDRQIKSF
     RVASNPYTWF TMEALEETWR NLQKIIKERE LELQKEQRRQ EENDKLRQEF AQHANAFHQW
     IQETRTYLLD GSCMVEESGT LESQLEATKR KHQEIRAMRS QLKKIEDLGA AMEEALILDN
     KYTEHSTVGL AQQWDQLDQL GMRMQHNLEQ QIQARNTTGV TEEALKEFSM MFKHFDKDKS
     GRLNHQEFKS CLRSLGYDLP MVEEGEPDPE FEAILDTVDP NRDGHVSLQE YMAFMISRET
     ENVKSSEEIE SAFRALSSEG KPYVTKEELY QNLTREQADY CVSHMKPYVD GKGRELPTAF
     DYVEFTRSLF VN
//
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.
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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   ATF2_MOUSE              Reviewed;         487 AA.
AC   P16951; Q64089; Q64090; Q64091;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=Cyclic AMP-dependent transcription factor ATF-2;
DE            Short=cAMP-dependent transcription factor ATF-2;
DE   AltName: Full=Activating transcription factor 2;
DE   AltName: Full=MXBP protein;
DE   AltName: Full=cAMP response element-binding protein CRE-BP1;
GN   Name=Atf2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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=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 [MRNA] OF 9-487, AND ALTERNATIVE SPLICING.
RX   MEDLINE=92123199; PubMed=1531087;
RA   Georgopoulos K., Morgan B.A., Moore D.D.;
RT   "Functionally distinct isoforms of the CRE-BP DNA-binding protein
RT   mediate activity of a T-cell-specific enhancer.";
RL   Mol. Cell. Biol. 12:747-757(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 77-487.
RX   MEDLINE=90205841; PubMed=2138707;
RA   Ivashkiv L.B., Liou H.-C., Kara C.J., Lamph W.W., Verma I.M.,
RA   Glimcher L.H.;
RT   "mXBP/CRE-BP2 and c-Jun form a complex which binds to the cyclic AMP,
RT   but not to the 12-O-tetradecanoylphorbol-13-acetate, response
RT   element.";
RL   Mol. Cell. Biol. 10:1609-1621(1990).
RN   [4]
RP   INTERACTION WITH UTF1.
RX   MEDLINE=98190083; PubMed=9524124; DOI=10.1093/emboj/17.7.2019;
RA   Okuda A., Fukushima A., Nishimoto M., Orimo A., Yamagishi T.,
RA   Nabeshima Y., Kuro-o M., Nabeshima Y., Boon K., Keaveney M.,
RA   Stunnenberg H.G., Muramatsu M.;
RT   "UTF1, a novel transcriptional coactivator expressed in pluripotent
RT   embryonic stem cells and extra-embryonic cells.";
RL   EMBO J. 17:2019-2032(1998).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51 AND THR-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   [6]
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).
CC   -!- FUNCTION: Transcriptional activator, probably constitutive, which
CC       binds to the cAMP-responsive element (CRE) (consensus: 5'-
CC       GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular
CC       promoters. Interaction with JUN redirects JUN to bind to CRES
CC       preferentially over the 12-O-tetradecanoylphorbol-13-acetate
CC       response elements (TRES) as part of an ATF2/JUN complex.
CC   -!- SUBUNIT: Binds DNA as a dimer and can form a homodimer in the
CC       absence of DNA. Can form a heterodimer with JUN. Interacts with
CC       SMAD3 and SMAD4. Binds through its N-terminal region to UTF1 which
CC       acts as a coactivator of ATF2 transcriptional activity.
CC   -!- INTERACTION:
CC       O08686:Barx2; NbExp=1; IntAct=EBI-2291130, EBI-2291077;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P16951-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P16951-2; Sequence=VSP_000590;
CC       Name=3;
CC         IsoId=P16951-3; Sequence=VSP_000589;
CC   -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily.
CC   -!- SIMILARITY: Contains 1 bZIP domain.
CC   -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB21128.1; Type=Erroneous initiation;
CC       Sequence=AAB21129.1; Type=Erroneous initiation;
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DR   EMBL; AF483482; AAL90756.1; -; mRNA.
DR   EMBL; AF483483; AAL90757.1; -; mRNA.
DR   EMBL; S76657; AAB21128.1; ALT_INIT; mRNA.
DR   EMBL; S76659; AAB21129.1; ALT_INIT; mRNA.
DR   EMBL; S76655; AAB21127.1; -; mRNA.
DR   EMBL; M31629; AAA39780.1; -; mRNA.
DR   IPI; IPI00110172; -.
DR   IPI; IPI00230233; -.
DR   IPI; IPI00230234; -.
DR   PIR; A42026; A42026.
DR   PIR; C42026; C42026.
DR   RefSeq; NP_001020264.1; NM_001025093.1.
DR   RefSeq; XP_001479554.1; XM_001479504.2.
DR   UniGene; Mm.209903; -.
DR   ProteinModelPortal; P16951; -.
DR   SMR; P16951; 1-38, 336-396.
DR   IntAct; P16951; 1.
DR   MINT; MINT-189465; -.
DR   STRING; P16951; -.
DR   PhosphoSite; P16951; -.
DR   PRIDE; P16951; -.
DR   Ensembl; ENSMUST00000055833; ENSMUSP00000058521; ENSMUSG00000027104.
DR   Ensembl; ENSMUST00000112010; ENSMUSP00000107641; ENSMUSG00000027104.
DR   Ensembl; ENSMUST00000112016; ENSMUSP00000107647; ENSMUSG00000027104.
DR   Ensembl; ENSMUST00000112017; ENSMUSP00000107648; ENSMUSG00000027104.
DR   GeneID; 100047997; -.
DR   GeneID; 11909; -.
DR   KEGG; mmu:100047997; -.
DR   KEGG; mmu:11909; -.
DR   NMPDR; fig|10090.3.peg.6155; -.
DR   UCSC; uc008kde.1; mouse.
DR   CTD; 11909; -.
DR   MGI; MGI:109349; Atf2.
DR   HOGENOM; HBG714930; -.
DR   HOVERGEN; HBG004300; -.
DR   InParanoid; P16951; -.
DR   OMA; PQVTNGD; -.
DR   OrthoDB; EOG45MN5N; -.
DR   PhylomeDB; P16951; -.
DR   NextBio; 461420; -.
DR   ArrayExpress; P16951; -.
DR   Bgee; P16951; -.
DR   CleanEx; MM_ATF2; -.
DR   Genevestigator; P16951; -.
DR   GermOnline; ENSMUSG00000027104; Mus musculus.
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   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    487       Cyclic AMP-dependent transcription factor
FT                                ATF-2.
FT                                /FTId=PRO_0000076578.
FT   DOMAIN      362    390       Leucine-zipper.
FT   ZN_FING       7     31       C2H2-type.
FT   DNA_BIND    333    356       Basic motif.
FT   MOD_RES      51     51       Phosphothreonine; by MAPK14 (By
FT                                similarity).
FT   MOD_RES      53     53       Phosphothreonine; by MAPK14 (By
FT                                similarity).
FT   MOD_RES      72     72       Phosphoserine (By similarity).
FT   MOD_RES      94     94       Phosphoserine.
FT   MOD_RES     310    310       Phosphoserine (By similarity).
FT   VAR_SEQ       1     48       MSDDKPFLCTAPGCGQRFTNEDHLAVHKHKHEMTLKFGPAR
FT                                NDSVIVA -> MHCPWVWP (in isoform 3).
FT                                /FTId=VSP_000589.
FT   VAR_SEQ     132    229       Missing (in isoform 2).
FT                                /FTId=VSP_000590.
FT   CONFLICT    482    487       AQPSGS -> HSPQEVD (in Ref. 1; AAB21128/
FT                                AAB21129).
SQ   SEQUENCE   487 AA;  52298 MW;  F9CDEC3BC3119ACB CRC64;
     MSDDKPFLCT APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RNDSVIVADQ TPTPTRFLKN
     CEEVGLFNEL ASPFENEFKK ASEDDIKKMP LDLSPLATPI IRSKIEEPSV VETTHQDSPL
     PHPESTTSDE KEVPLAQTAQ PTSAIVRPAS LQVPNVLLTS SDSSVIIQQA VPSPTSSTVI
     TQAPSSNRPI VPVPGPFPLL LHLPNGQTMP VAIPASITSS NVHVPAAVPL VRPVTMVPSV
     PGIPGPSSPQ PVQSEAKMRL KAALTQQHPP VTNGDTVKGH GSGLVRTQSE ESRPQSLQQP
     ATSTTETPAS PAHTTPQTQN TSGRRRRAAN EDPDEKRRKF LERNRAAASR CRQKRKVWVQ
     SLEKKAEDLS SLNGQLQSEV TLLRNEVAQL KQLLLAHKDC PVTAMQKKSG YHTADKDDSS
     EDLSVPSSPH TEAIQHSSVS TSNGVSSTSK AEAVATSVLT QMADQSTEPA LSQIVMAPPS
     QAQPSGS
//
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   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   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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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   CYTC_MOUSE              Reviewed;         140 AA.
AC   P21460; Q544Y0;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   08-MAR-2011, entry version 103.
DE   RecName: Full=Cystatin-C;
DE   AltName: Full=Cystatin-3;
DE   Flags: Precursor;
GN   Name=Cst3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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=91054522; PubMed=2241983; DOI=10.1016/0006-291X(90)90767-H;
RA   Solem M., Rawson C., Lindburg K., Barnes D.;
RT   "Transforming growth factor beta regulates cystatin C in serum-free
RT   mouse embryo (SFME) cells.";
RL   Biochem. Biophys. Res. Commun. 172:945-951(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv; TISSUE=Liver;
RX   MEDLINE=95137392; PubMed=7835704; DOI=10.1016/0378-1119(94)00728-B;
RA   Huh C., Nagle J.W., Kozak C.A., Abrahamson M., Karlsson S.;
RT   "Structural organization, expression and chromosomal mapping of the
RT   mouse cystatin-C-encoding gene (Cst3).";
RL   Gene 152:221-226(1995).
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/6J, and DBA/2;
RC   TISSUE=Bone marrow, Head, Hippocampus, Kidney, Mammary gland,
RC   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   [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: As an inhibitor of cysteine proteinases, this protein is
CC       thought to serve an important physiological role as a local
CC       regulator of this enzyme activity.
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- SIMILARITY: Belongs to the cystatin family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M59470; AAA63298.1; -; mRNA.
DR   EMBL; U10098; AAB41056.1; -; Unassigned_DNA.
DR   EMBL; AF483486; AAL90760.1; -; mRNA.
DR   EMBL; AF483487; AAL90761.1; -; mRNA.
DR   EMBL; AK002438; BAB22101.1; -; mRNA.
DR   EMBL; AK013676; BAB28949.1; -; mRNA.
DR   EMBL; AK014368; BAB29303.1; -; mRNA.
DR   EMBL; AK131728; BAE20785.1; -; mRNA.
DR   EMBL; AK146333; BAE27088.1; -; mRNA.
DR   EMBL; AK151160; BAE30165.1; -; mRNA.
DR   EMBL; AK161856; BAE36608.1; -; mRNA.
DR   EMBL; AK166430; BAE38771.1; -; mRNA.
DR   EMBL; BC002072; AAH02072.1; -; mRNA.
DR   IPI; IPI00123744; -.
DR   PIR; A36163; A36163.
DR   RefSeq; NP_034106.2; NM_009976.3.
DR   UniGene; Mm.4263; -.
DR   ProteinModelPortal; P21460; -.
DR   SMR; P21460; 31-140.
DR   IntAct; P21460; 2.
DR   STRING; P21460; -.
DR   MEROPS; I25.004; -.
DR   PRIDE; P21460; -.
DR   Ensembl; ENSMUST00000028938; ENSMUSP00000028938; ENSMUSG00000027447.
DR   GeneID; 13010; -.
DR   KEGG; mmu:13010; -.
DR   UCSC; uc008mtt.1; mouse.
DR   CTD; 13010; -.
DR   MGI; MGI:102519; Cst3.
DR   HOGENOM; HBG717109; -.
DR   HOVERGEN; HBG009556; -.
DR   InParanoid; P21460; -.
DR   OMA; YNRASND; -.
DR   OrthoDB; EOG49GKJ0; -.
DR   PhylomeDB; P21460; -.
DR   NextBio; 282848; -.
DR   ArrayExpress; P21460; -.
DR   Bgee; P21460; -.
DR   CleanEx; MM_CST3; -.
DR   Genevestigator; P21460; -.
DR   GermOnline; ENSMUSG00000027447; Mus musculus.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000010; Prot_inh_cystat.
DR   InterPro; IPR018073; Prot_inh_cystat_CS.
DR   Pfam; PF00031; Cystatin; 1.
DR   SMART; SM00043; CY; 1.
DR   PROSITE; PS00287; CYSTATIN; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Protease inhibitor; Secreted; Signal;
KW   Thiol protease inhibitor.
FT   SIGNAL        1     20
FT   CHAIN        21    140       Cystatin-C.
FT                                /FTId=PRO_0000006642.
FT   MOTIF        75     79       Secondary area of contact.
FT   SITE         31     31       Reactive site.
FT   DISULFID     93    103       By similarity.
FT   DISULFID    117    137       By similarity.
FT   CONFLICT     16     16       A -> G (in Ref. 1; AAA63298).
FT   CONFLICT     84     84       L -> F (in Ref. 1; AAA63298).
SQ   SEQUENCE   140 AA;  15531 MW;  3A563406DD58D0F5 CRC64;
     MASPLRSLLF LLAVLAVAWA ATPKQGPRML GAPEEADANE EGVRRALDFA VSEYNKGSND
     AYHSRAIQVV RARKQLVAGV NYFLDVEMGR TTCTKSQTNL TDCPFHDQPH LMRKALCSFQ
     IYSVPWKGTH SLTKFSCKNA
//
ID   WNT4_MOUSE              Reviewed;         351 AA.
AC   P22724;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Protein Wnt-4;
DE   Flags: Precursor;
GN   Name=Wnt4; Synonyms=Wnt-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=91122634; PubMed=2279700;
RA   Gavin B.J., McMahon J.A., McMahon A.P.;
RT   "Expression of multiple novel Wnt-1/int-1-related genes during fetal
RT   and adult mouse development.";
RL   Genes Dev. 4:2319-2332(1990).
RN   [2]
RP   INTERACTION WITH PORCN.
RX   MEDLINE=20325112; PubMed=10866835;
RX   DOI=10.1046/j.1432-1033.2000.01478.x;
RA   Tanaka K., Okabayashi H., Asashima M., Perrimon N., Kadowaki T.;
RT   "The evolutionarily conserved porcupine gene family is involved in the
RT   processing of the Wnt family.";
RL   Eur. J. Biochem. 267:4300-4311(2000).
CC   -!- FUNCTION: Ligand for members of the frizzled family of seven
CC       transmembrane receptors. May be an intracellular signaling
CC       molecule involved in segmentation of the forebrain. Is likely to
CC       signal over only few cell diameters (By similarity). Seems to be
CC       involved in kidney development.
CC   -!- SUBUNIT: Interacts with PORCN.
CC   -!- INTERACTION:
CC       O35082:Kl; NbExp=1; IntAct=EBI-1570945, EBI-1570828;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- TISSUE SPECIFICITY: In adults in lung and brain.
CC   -!- SIMILARITY: Belongs to the Wnt 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; M89797; AAA40566.1; -; mRNA.
DR   IPI; IPI00131373; -.
DR   PIR; C36470; C36470.
DR   RefSeq; NP_033549.1; NM_009523.1.
DR   UniGene; Mm.20355; -.
DR   ProteinModelPortal; P22724; -.
DR   IntAct; P22724; 2.
DR   STRING; P22724; -.
DR   PRIDE; P22724; -.
DR   Ensembl; ENSMUST00000045747; ENSMUSP00000036580; ENSMUSG00000036856.
DR   GeneID; 22417; -.
DR   KEGG; mmu:22417; -.
DR   UCSC; uc008viv.1; mouse.
DR   CTD; 22417; -.
DR   MGI; MGI:98957; Wnt4.
DR   eggNOG; roNOG09799; -.
DR   HOGENOM; HBG446188; -.
DR   HOVERGEN; HBG001595; -.
DR   InParanoid; P22724; -.
DR   OMA; VERCSCK; -.
DR   OrthoDB; EOG49P9ZP; -.
DR   PhylomeDB; P22724; -.
DR   NextBio; 302837; -.
DR   ArrayExpress; P22724; -.
DR   Bgee; P22724; -.
DR   CleanEx; MM_WNT4; -.
DR   Genevestigator; P22724; -.
DR   GermOnline; ENSMUSG00000036856; Mus musculus.
DR   GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005109; F:frizzled binding; IPI:BHF-UCL.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0016563; F:transcription activator activity; IDA:UniProtKB.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR   GO; GO:0016564; F:transcription repressor activity; IMP:UniProtKB.
DR   GO; GO:0006702; P:androgen biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI.
DR   GO; GO:0060070; P:canonical Wnt receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0061054; P:dermatome development; ISS:UniProtKB.
DR   GO; GO:0001838; P:embryonic epithelial tube formation; IDA:MGI.
DR   GO; GO:0090002; P:establishment of protein localization in plasma membrane; IMP:UniProtKB.
DR   GO; GO:0008585; P:female gonad development; IMP:UniProtKB.
DR   GO; GO:0030237; P:female sex determination; ISS:UniProtKB.
DR   GO; GO:0033080; P:immature T cell proliferation in thymus; IMP:MGI.
DR   GO; GO:0008584; P:male gonad development; ISS:UniProtKB.
DR   GO; GO:0060231; P:mesenchymal to epithelial transition; IMP:MGI.
DR   GO; GO:0072164; P:mesonephric tubule development; IGI:MGI.
DR   GO; GO:0072162; P:metanephric mesenchymal cell differentiation; NAS:UniProtKB.
DR   GO; GO:0072273; P:metanephric nephron morphogenesis; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IGI:MGI.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0045596; P:negative regulation of cell differentiation; IMP:MGI.
DR   GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IGI:MGI.
DR   GO; GO:2000019; P:negative regulation of male gonad development; ISS:UniProtKB.
DR   GO; GO:2000225; P:negative regulation of testosterone biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; ISS:UniProtKB.
DR   GO; GO:0048599; P:oocyte development; IMP:MGI.
DR   GO; GO:0061205; P:paramesonephric duct development; ISS:UniProtKB.
DR   GO; GO:0032349; P:positive regulation of aldosterone biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0030501; P:positive regulation of bone mineralization; ISS:UniProtKB.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISS:UniProtKB.
DR   GO; GO:2000066; P:positive regulation of cortisol biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0043193; P:positive regulation of gene-specific transcription; IDA:MGI.
DR   GO; GO:0045836; P:positive regulation of meiosis; IGI:MGI.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB.
DR   GO; GO:0018345; P:protein palmitoylation; ISS:UniProtKB.
DR   GO; GO:0022407; P:regulation of cell-cell adhesion; IMP:MGI.
DR   GO; GO:0072033; P:renal vesicle formation; IMP:MGI.
DR   GO; GO:0072034; P:renal vesicle induction; IDA:MGI.
DR   GO; GO:0051145; P:smooth muscle cell differentiation; IDA:MGI.
DR   GO; GO:0060126; P:somatotropin secreting cell differentiation; IMP:MGI.
DR   GO; GO:0060748; P:tertiary branching involved in mammary gland duct morphogenesis; IMP:MGI.
DR   GO; GO:0060129; P:thyroid-stimulating hormone-secreting cell differentiation; IMP:MGI.
DR   GO; GO:0007223; P:Wnt receptor signaling pathway, calcium modulating pathway; IEA:InterPro.
DR   InterPro; IPR009142; Wnt4.
DR   InterPro; IPR005816; Wnt_grthfactor.
DR   InterPro; IPR018161; Wnt_grthfactor_CS.
DR   InterPro; IPR005817; Wnt_SF.
DR   PANTHER; PTHR12027; Wnt; 1.
DR   PANTHER; PTHR12027:SF19; Wnt4; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01844; WNT4PROTEIN.
DR   PRINTS; PR01349; WNTPROTEIN.
DR   SMART; SM00097; WNT1; 1.
DR   PROSITE; PS00246; WNT1; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Extracellular matrix; Glycoprotein; Secreted;
KW   Signal; Wnt signaling pathway.
FT   SIGNAL        1     22       Potential.
FT   CHAIN        23    351       Protein Wnt-4.
FT                                /FTId=PRO_0000041422.
FT   CARBOHYD     88     88       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    297    297       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   351 AA;  39050 MW;  7E1C5C739BE939D9 CRC64;
     MSPRSCLRSL RLLVFAVFSA AASNWLYLAK LSSVGSISEE ETCEKLKGLI QRQVQMCKRN
     LEVMDSVRRG AQLAIEECQY QFRNRRWNCS TLDSLPVFGK VVTQGTREAA FVYAISSAGV
     AFAVTRACSS GELEKCGCDR TVHGVSPQGF QWSGCSDNIA YGVAFSQSFV DVRERSKGAS
     SSRALMNLHN NEAGRKAILT HMRVECKCHG VSGSCEVKTC WRAVPPFRQV GHALKEKFDG
     ATEVEPRRVG SSRALVPRNA QFKPHTDEDL VYLEPSPDFC EQDIRSGVLG TRGRTCNKTS
     KAIDGCELLC CGRGFHTAQV ELAERCGCRF HWCCFVKCRQ CQRLVEMHTC R
//
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;
CC   -----------------------------------------------------------------------
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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   KCC2B_MOUSE             Reviewed;         542 AA.
AC   P28652; Q5SVH9;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 114.
DE   RecName: Full=Calcium/calmodulin-dependent protein kinase type II subunit beta;
DE            Short=CaM kinase II subunit beta;
DE            Short=CaMK-II subunit beta;
DE            EC=2.7.11.17;
GN   Name=Camk2b; Synonyms=Camk2d;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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=92334366; PubMed=1321343;
RA   Karls U., Mueller U., Gilbert D.J., Copeland N.G., Jenkins N.A.,
RA   Harbers K.;
RT   "Structure, expression, and chromosome location of the gene for the
RT   beta subunit of brain-specific Ca2+/calmodulin-dependent protein
RT   kinase II identified by transgene integration in an embryonic lethal
RT   mouse mutant.";
RL   Mol. Cell. Biol. 12:3644-3652(1992).
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/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting 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 136-147, 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-315, 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 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-17, 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-367; THR-287 AND
RP   SER-397, 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 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       Interacts with SYNGAP1, CAMK2N2 and MPDZ (By similarity).
CC   -!- INTERACTION:
CC       P11798-2:Camk2a; NbExp=2; IntAct=EBI-397029, EBI-400402;
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; X63615; CAA45160.1; -; mRNA.
DR   EMBL; AK163698; BAE37464.1; -; mRNA.
DR   EMBL; AL611926; CAI24948.1; -; Genomic_DNA.
DR   EMBL; AL645469; CAI24948.1; JOINED; Genomic_DNA.
DR   EMBL; AL645469; CAI25258.1; -; Genomic_DNA.
DR   EMBL; AL611926; CAI25258.1; JOINED; Genomic_DNA.
DR   IPI; IPI00474502; -.
DR   PIR; A45025; A45025.
DR   RefSeq; NP_031621.3; NM_007595.5.
DR   UniGene; Mm.439733; -.
DR   ProteinModelPortal; P28652; -.
DR   SMR; P28652; 11-301, 403-536.
DR   DIP; DIP-31582N; -.
DR   IntAct; P28652; 13.
DR   MINT; MINT-136473; -.
DR   STRING; P28652; -.
DR   PhosphoSite; P28652; -.
DR   PRIDE; P28652; -.
DR   Ensembl; ENSMUST00000109813; ENSMUSP00000105438; ENSMUSG00000057897.
DR   Ensembl; ENSMUST00000109815; ENSMUSP00000105440; ENSMUSG00000057897.
DR   GeneID; 12323; -.
DR   KEGG; mmu:12323; -.
DR   UCSC; uc007hxr.1; mouse.
DR   CTD; 12323; -.
DR   MGI; MGI:88257; Camk2b.
DR   eggNOG; roNOG13785; -.
DR   HOVERGEN; HBG108055; -.
DR   PhylomeDB; P28652; -.
DR   BRENDA; 2.7.11.17; 244.
DR   ArrayExpress; P28652; -.
DR   Bgee; P28652; -.
DR   Genevestigator; P28652; -.
DR   GermOnline; ENSMUSG00000057897; Mus musculus.
DR   GO; GO:0005954; C:calcium- and calmodulin-dependent protein kinase complex; TAS:UniProtKB.
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:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   ATP-binding; Calmodulin-binding; Direct protein sequencing; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN         1    542       Calcium/calmodulin-dependent protein
FT                                kinase type II subunit beta.
FT                                /FTId=PRO_0000086097.
FT   DOMAIN       14    272       Protein kinase.
FT   NP_BIND      20     28       ATP (By similarity).
FT   REGION      291    301       Calmodulin-binding.
FT   ACT_SITE    136    136       Proton acceptor (By similarity).
FT   BINDING      43     43       ATP (By similarity).
FT   MOD_RES      17     17       Phosphotyrosine.
FT   MOD_RES     287    287       Phosphothreonine.
FT   MOD_RES     315    315       Phosphoserine.
FT   MOD_RES     358    358       Phosphoserine (By similarity).
FT   MOD_RES     367    367       Phosphoserine.
FT   MOD_RES     397    397       Phosphoserine.
FT   CONFLICT     19     19       D -> E (in Ref. 1; CAA45160).
SQ   SEQUENCE   542 AA;  60461 MW;  8A7962A6495FD0D0 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 TIEDEDAKAR KQEIIKTTEQ
     LIEAVNNGDF EAYAKICDPG LTSFEPEALG NLVEGMDFHR FYFENLLAKN SKPIHTTILN
     PHVHVIGEDA ACIAYIRLTQ YIDGQGRPRT SQSEETRVWH RRDGKWQNVH FHCSGAPVAP
     LQ
//
ID   NCKP1_MOUSE             Reviewed;        1128 AA.
AC   P28660; Q3UPY6; Q80TX0; Q8CG49; Q99KY0;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Nck-associated protein 1;
DE            Short=NAP 1;
DE   AltName: Full=Brain protein H19;
DE   AltName: Full=MH19;
DE   AltName: Full=Membrane-associated protein HEM-2;
DE   AltName: Full=p125Nap1;
GN   Name=Nckap1; Synonyms=Hem2, Kiaa0587, Nap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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, AND COMPONENT OF WAVE2 COMPLEX.
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   [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] OF 288-935 (ISOFORMS 1/2).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 755-1128 (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 876-1128 (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).
CC   -!- FUNCTION: Is part of lamellipodial complex that controls Rac-
CC       dependent actin remodeling.
CC   -!- SUBUNIT: Associates preferentially with the first SH3 domain of
CC       NCK (By similarity). Component of the WAVE2 complex composed of
CC       ABI1, CYFIP1/SRA1, NCKAP1/NAP1 and WASF2/WAVE2. Also a component
CC       of the WAVE1 complex composed of ABI2, CYFIP2, C3orf10/HSPC300,
CC       NCKAP1 and WASF1/WAVE1. CYFIP2 binds to activated RAC1 which
CC       causes the complex to dissociate, releasing activated WASF1. The
CC       complex can also be activated by NCK1.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein;
CC       Cytoplasmic side. Cell projection, lamellipodium membrane; Single-
CC       pass membrane protein; Cytoplasmic side. Cytoplasm. Note=At the
CC       interface between the lamellipodial actin meshwork and the
CC       membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P28660-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P28660-2; Sequence=VSP_016261, VSP_016262;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: High expression in cerebral cortex, not in
CC       cerebellar cortex.
CC   -!- SIMILARITY: Belongs to the HEM-1/HEM-2 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65600.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AJ534525; CAD58932.1; -; mRNA.
DR   EMBL; AK122318; BAC65600.1; ALT_INIT; Transcribed_RNA.
DR   EMBL; X61453; CAA43693.1; -; mRNA.
DR   EMBL; BC003962; AAH03962.1; -; mRNA.
DR   EMBL; AK143049; BAE25258.1; -; mRNA.
DR   IPI; IPI00319320; -.
DR   IPI; IPI00656204; -.
DR   PIR; S16866; S16866.
DR   RefSeq; NP_058661.1; NM_016965.2.
DR   UniGene; Mm.25203; -.
DR   STRING; P28660; -.
DR   PhosphoSite; P28660; -.
DR   PRIDE; P28660; -.
DR   Ensembl; ENSMUST00000028386; ENSMUSP00000028386; ENSMUSG00000027002.
DR   Ensembl; ENSMUST00000111759; ENSMUSP00000107389; ENSMUSG00000027002.
DR   GeneID; 50884; -.
DR   KEGG; mmu:50884; -.
DR   UCSC; uc008khm.1; mouse.
DR   CTD; 50884; -.
DR   MGI; MGI:1355333; Nckap1.
DR   GeneTree; ENSGT00390000016619; -.
DR   HOVERGEN; HBG006344; -.
DR   OrthoDB; EOG4M0F0V; -.
DR   PhylomeDB; P28660; -.
DR   NextBio; 307869; -.
DR   ArrayExpress; P28660; -.
DR   Bgee; P28660; -.
DR   CleanEx; MM_NCKAP1; -.
DR   Genevestigator; P28660; -.
DR   GermOnline; ENSMUSG00000027002; 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:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045176; P:apical protein localization; IDA:MGI.
DR   GO; GO:0045175; P:basal protein localization; IDA:MGI.
DR   GO; GO:0010172; P:embryonic body 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:0007492; P:endoderm development; IMP:MGI.
DR   GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0030032; P:lamellipodium assembly; IDA:MGI.
DR   GO; GO:0008078; P:mesodermal cell migration; IMP:MGI.
DR   GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR   GO; GO:0048570; P:notochord morphogenesis; IMP:MGI.
DR   GO; GO:0048340; P:paraxial mesoderm morphogenesis; IMP:MGI.
DR   GO; GO:0050821; P:protein stabilization; IMP:MGI.
DR   GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
DR   GO; GO:0001756; P:somitogenesis; IMP:MGI.
DR   GO; GO:0007354; P:zygotic determination of anterior/posterior axis, embryo; IMP:MGI.
DR   InterPro; IPR019137; Nck-associated_protein-1.
DR   Pfam; PF09735; Nckap1; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Cell projection; Cytoplasm;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1   1128       Nck-associated protein 1.
FT                                /FTId=PRO_0000216173.
FT   TRANSMEM    995   1015       Helical; (Potential).
FT   VAR_SEQ     242    263       Missing (in isoform 2).
FT                                /FTId=VSP_016261.
FT   VAR_SEQ    1060   1128       Missing (in isoform 2).
FT                                /FTId=VSP_016262.
FT   CONFLICT    745    745       A -> E (in Ref. 3; CAA43693).
FT   CONFLICT    876    876       V -> F (in Ref. 5; BAE25258).
FT   CONFLICT    934    935       FL -> SS (in Ref. 3; CAA43693).
SQ   SEQUENCE   1128 AA;  128784 MW;  279246384B0F4B77 CRC64;
     MSRSVLQPSQ QKLAEKLTIL NDRGVGMLTR LYNIKKACGD PKAKPSYLID KNLESAVKFI
     VRKFPAVETR NNNQQLAQLQ KEKSEILKNL ALYYFTFVDV MEFKDHVCDL LNTIDVCQVF
     FDITVNFDLT KNYLDLTVTY TTLMILLSRI EERKAIIGLY NYAHEMTHGA SDREYPRLGQ
     MIVDYENPLK KMMEEFVPHS KSLSDALISL QMVYPRRNLS ADQWRNAQLL SLISAPSTML
     NPAQSDTMPC EYLSLDAMEK WIIFGFILCH GMLNTEATAL NLWKLALQSS SCLSLFRDEV
     FHIHKAAEDL FVNIRGYNKR INDIRECKEA AVSHAGSMHR ERRKFLRSAL KELATVLSDQ
     PGLLGPKALF VFMALSFARD EIIWLLRHAD NMPKKSADDF IDKHIAELIF YMEELRAHVR
     KYGPVMQRYY VQYLSGFDAV VLNELVQNLS VCPEDESIIM SSFVNTMTSL SVKQVEDGEV
     FDFRGMRLDW FRLQAYTSVS KASLSLADHR ELGKMMNTII FHTKMVDSLV EMLVETSDLS
     IFCFYSRAFE KMFQQCLELP SQSRYSIAFP LLCTHFMSCT HELCPEERHH IGDRSLSLCN
     MFLDEMAKQA RNLITDICTE QCTLSDQLLP KHCAKTISQA VNKKSKKQTG KKGEPEREKP
     GVESMRKNRL VVTNLDKLHT ALSELCFSIN YVPNMAVWEH TFTPREYLTS HLEIRFTKSI
     VGMTMYNQAT QEIAKPSELL TSVRAYMTVL QSIENYVQID ITRVFNNVLL QQTQHLDSHG
     EPTITSLYTN WYLETLLRQV SNGHIAYFPA MKAFVNLPTE NELTFNAEEY SDISEMRSLS
     ELLGPYGMKF LSESLMWHIS SQVAELKKLV VENVDVLTQM RTSFDKPDQM AALFKRLSSV
     DSVLKRMTII GVILSFRSLA QEALRDVLSY HIPFLVSSIE DFKDHIPRET DMKVAMNVYE
     LSSAAGLPCE IDPALVVALS SQKSENISPE EEYKIACLLM VFVAVSLPTL ASNVMSQYSP
     AIEGHCNNIH CLAKAINQIA AALFTIHKGS IEDRLKEFLA LASSSLLKIG QETDKTTTRN
     RESVYLLLDM IVQESPFLTM DLLESCFPYV LLRNAYHAVY KQSVTSSA
//
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   HEXA_MOUSE              Reviewed;         528 AA.
AC   P29416; Q64246;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Beta-hexosaminidase subunit alpha;
DE            EC=3.2.1.52;
DE   AltName: Full=Beta-N-acetylhexosaminidase subunit alpha;
DE            Short=Hexosaminidase subunit A;
DE   AltName: Full=N-acetyl-beta-glucosaminidase subunit alpha;
DE   Flags: Precursor;
GN   Name=Hexa;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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=92344643; PubMed=1379046;
RA   Beccari T., Hoade J., Orlacchio A., Stirling J.L.;
RT   "Cloning and sequence analysis of a cDNA encoding the alpha-subunit of
RT   mouse beta-N-acetylhexosaminidase and comparison with the human
RT   enzyme.";
RL   Biochem. J. 285:593-596(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95135330; PubMed=7833835;
RA   Bianconi S., Beccari T., Stirling J.L., Sheardown S., Orlacchio A.;
RT   "Organization of the gene for the alpha-subunit of mouse beta-N-
RT   acetylhexosaminidase (HEXa).";
RL   Biochem. Mol. Biol. Int. 34:579-586(1994).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=129/Sv; TISSUE=Liver;
RX   MEDLINE=95203865; PubMed=7896264; DOI=10.1006/geno.1994.1587;
RA   Wakamatsu N., Benoit G., Lamhonwah A.-M., Zhang Z.-X., Trasler J.M.,
RA   Triggs-Raine B.L., Gravel R.A.;
RT   "Structural organization, sequence, and expression of the mouse HEXA
RT   gene encoding the alpha subunit of hexosaminidase A.";
RL   Genomics 24:110-119(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   -!- SUBUNIT: There are 3 forms of beta-hexosaminidase: hexosaminidase
CC       A is a trimer composed of one alpha chain, one beta-A chain and
CC       one beta-B chain; hexosaminidase B is a tetramer of two beta-A and
CC       two beta-B chains; hexosaminidase S is an homodimer of two alpha
CC       chains. The two beta chains are derived from the cleavage of a
CC       precursor chain (By similarity).
CC   -!- SUBCELLULAR LOCATION: Lysosome.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Most abundant in testis, adrenal,
CC       epididymis and heart. Low levels seen in the liver.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
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DR   EMBL; X64331; CAA45615.1; -; mRNA.
DR   EMBL; U05837; AAC53246.1; -; Genomic_DNA.
DR   EMBL; U05824; AAC53246.1; JOINED; Genomic_DNA.
DR   EMBL; U05825; AAC53246.1; JOINED; Genomic_DNA.
DR   EMBL; U05826; AAC53246.1; JOINED; Genomic_DNA.
DR   EMBL; U05827; AAC53246.1; JOINED; Genomic_DNA.
DR   EMBL; U05828; AAC53246.1; JOINED; Genomic_DNA.
DR   EMBL; U05829; AAC53246.1; JOINED; Genomic_DNA.
DR   EMBL; U05830; AAC53246.1; JOINED; Genomic_DNA.
DR   EMBL; U05831; AAC53246.1; JOINED; Genomic_DNA.
DR   EMBL; U05832; AAC53246.1; JOINED; Genomic_DNA.
DR   EMBL; U05833; AAC53246.1; JOINED; Genomic_DNA.
DR   EMBL; U05834; AAC53246.1; JOINED; Genomic_DNA.
DR   EMBL; U05835; AAC53246.1; JOINED; Genomic_DNA.
DR   EMBL; U05836; AAC53246.1; JOINED; Genomic_DNA.
DR   EMBL; U07721; AAA18777.1; -; Unassigned_DNA.
DR   EMBL; U07709; AAA18777.1; JOINED; Unassigned_DNA.
DR   EMBL; U07710; AAA18777.1; JOINED; Unassigned_DNA.
DR   EMBL; U07711; AAA18777.1; JOINED; Unassigned_DNA.
DR   EMBL; U07712; AAA18777.1; JOINED; Unassigned_DNA.
DR   EMBL; U07713; AAA18777.1; JOINED; Unassigned_DNA.
DR   EMBL; U07714; AAA18777.1; JOINED; Unassigned_DNA.
DR   EMBL; U07715; AAA18777.1; JOINED; Unassigned_DNA.
DR   EMBL; U07716; AAA18777.1; JOINED; Unassigned_DNA.
DR   EMBL; U07717; AAA18777.1; JOINED; Unassigned_DNA.
DR   EMBL; U07718; AAA18777.1; JOINED; Unassigned_DNA.
DR   EMBL; U07719; AAA18777.1; JOINED; Unassigned_DNA.
DR   EMBL; U07720; AAA18777.1; JOINED; Unassigned_DNA.
DR   EMBL; U07631; AAA18775.1; -; mRNA.
DR   EMBL; X79061; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X79062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00125522; -.
DR   PIR; I48253; I48253.
DR   RefSeq; NP_034551.2; NM_010421.4.
DR   UniGene; Mm.2284; -.
DR   ProteinModelPortal; P29416; -.
DR   SMR; P29416; 23-527.
DR   STRING; P29416; -.
DR   CAZy; GH20; Glycoside Hydrolase Family 20.
DR   PRIDE; P29416; -.
DR   Ensembl; ENSMUST00000026262; ENSMUSP00000026262; ENSMUSG00000025232.
DR   GeneID; 15211; -.
DR   KEGG; mmu:15211; -.
DR   CTD; 15211; -.
DR   MGI; MGI:96073; Hexa.
DR   eggNOG; roNOG07090; -.
DR   HOGENOM; HBG591688; -.
DR   HOVERGEN; HBG005961; -.
DR   InParanoid; P29416; -.
DR   OrthoDB; EOG42Z4Q7; -.
DR   BRENDA; 3.2.1.52; 244.
DR   ArrayExpress; P29416; -.
DR   Bgee; P29416; -.
DR   CleanEx; MM_HEXA; -.
DR   Genevestigator; P29416; -.
DR   GermOnline; ENSMUSG00000025232; Mus musculus.
DR   GO; GO:0005764; C:lysosome; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IDA:MGI.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; 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:0007040; P:lysosome organization; IMP:MGI.
DR   GO; GO:0042552; P:myelination; IGI:MGI.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IGI:MGI.
DR   GO; GO:0050884; P:neuromuscular process controlling posture; IMP:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; IGI:MGI.
DR   GO; GO:0019953; P:sexual reproduction; IMP: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; Zymogen.
FT   SIGNAL        1     22       By similarity.
FT   PROPEP       23     88       By similarity.
FT                                /FTId=PRO_0000011995.
FT   CHAIN        89    528       Beta-hexosaminidase subunit alpha.
FT                                /FTId=PRO_0000011996.
FT   ACT_SITE    323    323       Proton donor (By similarity).
FT   CARBOHYD    115    115       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    157    157       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    295    295       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    487    487       N-linked (GlcNAc...) (Potential).
FT   DISULFID     58    104       By similarity.
FT   DISULFID    277    328       By similarity.
FT   DISULFID    504    521       By similarity.
FT   CONFLICT     56     56       G -> A (in Ref. 3 and 4).
FT   CONFLICT    237    237       Q -> E (in Ref. 4).
FT   CONFLICT    455    455       E -> Q (in Ref. 4).
SQ   SEQUENCE   528 AA;  60599 MW;  5C723B82DAEC3B43 CRC64;
     MAGCRLWVSL LLAAALACLA TALWPWPQYI QTYHRRYTLY PNNFQFRYHV SSAAQGGCVV
     LDEAFRRYRN LLFGSGSWPR PSFSNKQQTL GKNILVVSVV TAECNEFPNL ESVENYTLTI
     NDDQCLLASE TVWGALRGLE TFSQLVWKSA EGTFFINKTK IKDFPRFPHR GVLLDTSRHY
     LPLSSILDTL DVMAYNKFNV FHWHLVDDSS FPYESFTFPE LTRKGSFNPV THIYTAQDVK
     EVIEYARLRG IRVLAEFDTP GHTLSWGPGA PGLLTPCYSG SHLSGTFGPV NPSLNSTYDF
     MSTLFLEISS VFPDFYLHLG GDEVDFTCWK SNPNIQAFMK KKGFTDFKQL ESFYIQTLLD
     IVSDYDKGYV VWQEVFDNKV KVRPDTIIQV WREEMPVEYM LEMQDITRAG FRALLSAPWY
     LNRVKYGPDW KDMYKVEPLA FHGTPEQKAL VIGGEACMWG EYVDSTNLVP RLWPRAGAVA
     ERLWSSNLTT NIDFAFKRLS HFRCELVRRG IQAQPISVGY CEQEFEQT
//
ID   AIMP1_MOUSE             Reviewed;         310 AA.
AC   P31230; Q60659;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   18-OCT-2001, sequence version 2.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Aminoacyl tRNA synthase complex-interacting multifunctional protein 1;
DE   AltName: Full=Multisynthase complex auxiliary component p43;
DE   Contains:
DE     RecName: Full=Endothelial monocyte-activating polypeptide 2;
DE              Short=EMAP-2;
DE     AltName: Full=Endothelial monocyte-activating polypeptide II;
DE              Short=EMAP-II;
DE     AltName: Full=Small inducible cytokine subfamily E member 1;
GN   Name=Aimp1; Synonyms=Emap2, Scye1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=95014290; PubMed=7929199;
RA   Kao J., Houck K., Fan Y., Haehnel I., Libutti S.K., Kayton M.L.,
RA   Grikscheit T., Chabot J., Nowygrod R., Greenberg S., Kuang W.J.,
RA   Leung D.W., Hayward J.R., Kisiel W., Heath M., Brett J., Stern D.M.;
RT   "Characterization of a novel tumor-derived cytokine. Endothelial-
RT   monocyte activating polypeptide II.";
RL   J. Biol. Chem. 269:25106-25119(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   PROTEIN SEQUENCE OF 145-164, AND FUNCTION.
RX   MEDLINE=93015897; PubMed=1400342;
RA   Kao J., Ryan J., Brett G., Chen J., Shen H., Fan Y.-G., Godman G.,
RA   Familletti P.C., Wang F., Pan Y.-C.E., Stern D., Clauss M.;
RT   "Endothelial monocyte-activating polypeptide II. A novel tumor-derived
RT   polypeptide that activates host-response mechanisms.";
RL   J. Biol. Chem. 267:20239-20247(1992).
RN   [4]
RP   FUNCTION.
RX   MEDLINE=94193665; PubMed=7545917;
RA   Kao J., Fan Y., Haehnel I., Brett J., Greenberg S., Clauss M.,
RA   Kayton M., Houck K., Kisiel W., Seljelid R., Burnier J., Stern D.;
RT   "A peptide derived from the amino terminus of endothelial-monocyte-
RT   activating polypeptide II modulates mononuclear and polymorphonuclear
RT   leukocyte functions, defines an apparently novel cellular interaction
RT   site, and induces an acute inflammatory response.";
RL   J. Biol. Chem. 269:9774-9782(1994).
RN   [5]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=9770485; DOI=10.1073/pnas.95.21.12322;
RA   Knies U.E., Behrensdorf H.A., Mitchell C.A., Deutsch U., Risau W.,
RA   Drexler H.C.A., Clauss M.;
RT   "Regulation of endothelial monocyte-activating polypeptide II release
RT   by apoptosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:12322-12327(1998).
RN   [6]
RP   CLEAVAGE.
RX   PubMed=11306575; DOI=10.1074/jbc.M100489200;
RA   Shalak V., Kaminska M., Mitnacht-Kraus R., Vandenabeele P., Clauss M.,
RA   Mirande M.;
RT   "The EMAPII cytokine is released from the mammalian multisynthetase
RT   complex after cleavage of its p43/proEMAPII component.";
RL   J. Biol. Chem. 276:23769-23776(2001).
RN   [7]
RP   FUNCTION.
RX   PubMed=15681823;
RA   Park S.G., Shin H., Shin Y.K., Lee Y., Choi E.-C., Park B.-J., Kim S.;
RT   "The novel cytokine p43 stimulates dermal fibroblast proliferation and
RT   wound repair.";
RL   Am. J. Pathol. 166:387-398(2005).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=17001013; DOI=10.1073/pnas.0602045103;
RA   Park S.G., Kang Y.S., Kim J.Y., Lee C.S., Ko Y.G., Lee W.J.,
RA   Lee K.-U., Yeom Y.I., Kim S.;
RT   "Hormonal activity of AIMP1/p43 for glucose homeostasis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14913-14918(2006).
RN   [9]
RP   FUNCTION, INTERACTION WITH HSP90B1, SUBCELLULAR LOCATION, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=17525271;
RA   Han J.M., Park S.G., Liu B., Park B.-J., Kim J.Y., Jin C.H.,
RA   Song Y.W., Li Z., Kim S.;
RT   "Aminoacyl-tRNA synthetase-interacting multifunctional protein 1/p43
RT   controls endoplasmic reticulum retention of heat shock protein gp96:
RT   its pathological implications in lupus-like autoimmune diseases.";
RL   Am. J. Pathol. 170:2042-2054(2007).
RN   [10]
RP   FUNCTION, INTERACTION WITH SMURF2, AND INDUCTION.
RX   PubMed=18448069; DOI=10.1016/j.bbrc.2008.04.099;
RA   Lee Y.S., Han J.M., Son S.H., Choi J.W., Jeon E.J., Bae S.-C.,
RA   Park Y.I., Kim S.;
RT   "AIMP1/p43 downregulates TGF-beta signaling via stabilization of
RT   smurf2.";
RL   Biochem. Biophys. Res. Commun. 371:395-400(2008).
RN   [11]
RP   FUNCTION.
RX   PubMed=18292511;
RA   Kim E., Kim S.H., Kim S., Cho D., Kim T.S.;
RT   "AIMP1/p43 protein induces the maturation of bone marrow-derived
RT   dendritic cells with T helper type 1-polarizing ability.";
RL   J. Immunol. 180:2894-2902(2008).
CC   -!- FUNCTION: Non-catalytic component of the multisynthase complex.
CC       Stimulates the catalytic activity of cytoplasmic arginyl-tRNA
CC       synthase. Binds tRNA. Possesses inflammatory cytokine activity.
CC       Negatively regulates TGF-beta signaling through stabilization of
CC       SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated
CC       degradation. Involved in glucose homeostasis through induction of
CC       glucagon secretion at low glucose levels. Promotes dermal
CC       fibroblast proliferation and wound repair. Regulates KDELR1-
CC       mediated retention of HSP90B1/gp96 in the endoplasmic reticulum.
CC       Plays a role in angiogenesis by inducing endothelial cell
CC       migration at low concentrations and endothelian cell apoptosis at
CC       high concentrations. Induces maturation of dendritic cells and
CC       monocyte cell adhesion. Modulates endothelial cell responses by
CC       degrading HIF-1A through interaction with PSMA7 (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity). Component of the multisynthase
CC       complex which is comprised of a bifunctional glutamyl-prolyl-tRNA
CC       synthase, the monospecific isoleucyl, leucyl, glutaminyl,
CC       methionyl, lysyl, arginyl and aspartyl-tRNA synthases, and three
CC       auxiliary proteins, EEF1E1/p18, AIMP2/p38 and AIMP1/p43. Interacts
CC       (via N-terminus) with RARS (via N-terminus). Interacts (via C-
CC       terminus) with SMURF2. Interacts (via N-terminus) with
CC       HSP90B1/gp96 (via C-terminus). Interacts with PSMA7 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm, cytosol
CC       (By similarity). Cytoplasmic vesicle, secretory vesicle. Secreted.
CC       Endoplasmic reticulum. Golgi apparatus. Note=Enriched in secretory
CC       vesicles of pancreatic alpha cells and secreted from the pancreas
CC       in response to low glucose levels. Also secreted in response to
CC       hypoxia and both apoptotic and necrotic cell death.
CC   -!- TISSUE SPECIFICITY: Highly expressed in salivary glands and
CC       pancreatic alpha cells in the adult (at protein level). In the
CC       embryo, expressed primarily at sites of tissue remodeling such as
CC       ganglia, developing bones and teeth.
CC   -!- INDUCTION: By wounding.
CC   -!- PTM: Cleaved by caspase-7 in response to apoptosis to produce
CC       EMAP-II.
CC   -!- DISRUPTION PHENOTYPE: Increased Hsp90b1 surface expression,
CC       dendritic cell hyperactivation and development of lupus-like
CC       autoimmune phenotypes.
CC   -!- SIMILARITY: Contains 1 tRNA-binding domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; U10118; AAA62203.1; -; mRNA.
DR   EMBL; BC002054; AAH02054.1; -; mRNA.
DR   IPI; IPI00132194; -.
DR   PIR; A55053; A55053.
DR   UniGene; Mm.235137; -.
DR   ProteinModelPortal; P31230; -.
DR   SMR; P31230; 147-310.
DR   STRING; P31230; -.
DR   PhosphoSite; P31230; -.
DR   PRIDE; P31230; -.
DR   Ensembl; ENSMUST00000029663; ENSMUSP00000029663; ENSMUSG00000028029.
DR   MGI; MGI:102774; Aimp1.
DR   eggNOG; roNOG14637; -.
DR   InParanoid; P31230; -.
DR   OrthoDB; EOG483D56; -.
DR   PhylomeDB; P31230; -.
DR   ArrayExpress; P31230; -.
DR   Bgee; P31230; -.
DR   CleanEx; MM_SCYE1; -.
DR   Genevestigator; P31230; -.
DR   GermOnline; ENSMUSG00000028029; Mus musculus.
DR   GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; ISS:HGNC.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0043498; F:cell surface binding; ISS:HGNC.
DR   GO; GO:0005125; F:cytokine activity; IDA:HGNC.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:HGNC.
DR   GO; GO:0000049; F:tRNA binding; ISS:HGNC.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0050900; P:leukocyte migration; IDA:HGNC.
DR   GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISS:HGNC.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR016027; NA-bd_OB-fold-like.
DR   InterPro; IPR002547; tRNA-bd_dom.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Angiogenesis; Apoptosis; Carbohydrate metabolism;
KW   Cell adhesion; Cytokine; Cytoplasm; Cytoplasmic vesicle;
KW   Direct protein sequencing; Endoplasmic reticulum; Glucose metabolism;
KW   Golgi apparatus; Inflammatory response; Nucleus; Protein biosynthesis;
KW   RNA-binding; Secreted; tRNA-binding.
FT   CHAIN         1    310       Aminoacyl tRNA synthase complex-
FT                                interacting multifunctional protein 1.
FT                                /FTId=PRO_0000223395.
FT   CHAIN       145    310       Endothelial monocyte-activating
FT                                polypeptide 2.
FT                                /FTId=PRO_0000019244.
FT   DOMAIN      149    250       tRNA-binding.
FT   REGION        6     46       Required for fibroblast proliferation (By
FT                                similarity).
FT   REGION       54    192       Interaction with HSP90B1.
FT   REGION      101    115       Required for endothelial cell death (By
FT                                similarity).
FT   REGION      115    190       Required for endothelial cell migration
FT                                (By similarity).
FT   MOD_RES      33     33       N6-acetyllysine (By similarity).
SQ   SEQUENCE   310 AA;  33997 MW;  A2F8FF52A33D03A0 CRC64;
     MATNDAVLKR LEQKGAEADQ IIEYLKQQVA LLKEKAILQA TMREEKKLRV ENAKLKKEIE
     ELKQELILAE IHNGVEQVRV RLSTPLQTNC TASESVVQSP SVATTASPAT KEQIKAGEEK
     KVKEKTEKKG EKKEKQQSAA ASTDSKPIDA SRLDLRIGCI VTAKKHPDAD SLYVEEVDVG
     EAAPRTVVSG LVNHVPLEQM QNRMVVLLCN LKPAKMRGVL SQAMVMCASS PEKVEILAPP
     NGSVPGDRIT FDAFPGEPDK ELNPKKKIWE QIQPDLHTNA ECVATYKGAP FEVKGKGVCR
     AQTMANSGIK
//
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.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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.
CC   -----------------------------------------------------------------------
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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   PPM1B_MOUSE             Reviewed;         390 AA.
AC   P36993;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Protein phosphatase 1B;
DE            EC=3.1.3.16;
DE   AltName: Full=Protein phosphatase 2C isoform beta;
DE            Short=PP2C-beta;
GN   Name=Ppm1b; Synonyms=Pp2c2, Pppm1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=94099616; PubMed=8274020; DOI=10.1006/abbi.1993.1598;
RA   Terasawa T., Kobayashi T., Murakami T., Ohnishi M., Kato S.,
RA   Tanaka O., Kondo H., Yamamoto H., Takeuchi T., Tamura S.;
RT   "Molecular cloning of a novel isotype of Mg(2+)-dependent protein
RT   phosphatase beta (type 2C beta) enriched in brain and heart.";
RL   Arch. Biochem. Biophys. 307:342-349(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (BETA-3; BETA-4 AND BETA-5).
RC   TISSUE=Testis;
RX   MEDLINE=95251388; PubMed=7733667; DOI=10.1006/abbi.1995.1244;
RA   Kato S., Terasawa T., Kobayashi T., Ohnishi M., Sasahara Y.,
RA   Kusuda K., Yanagawa Y., Hiraga A., Matsui Y., Tamura S.;
RT   "Molecular cloning and expression of mouse Mg(2+)-dependent protein
RT   phosphatase beta-4 (type 2C beta-4).";
RL   Arch. Biochem. Biophys. 318:387-393(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (BETA-3 AND BETA-4).
RC   TISSUE=Testis;
RX   MEDLINE=94313028; PubMed=8038726;
RA   Hou E.W., Kawai Y., Miyasaka H., Li S.S.;
RT   "Molecular cloning and expression of cDNAs encoding two isoforms of
RT   protein phosphatase 2C beta from mouse testis.";
RL   Biochem. Mol. Biol. Int. 32:773-780(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=99398339; PubMed=10469137;
RX   DOI=10.1046/j.1432-1327.1999.00580.x;
RA   Ohnishi M., Chida N., Kobayashi T., Wang H., Ikeda S., Hanada M.,
RA   Yanagawa Y., Katsura K., Hiraga A., Tamura S.;
RT   "Alternative promoters direct tissue-specific expression of the mouse
RT   protein phosphatase 2Cbeta gene.";
RL   Eur. J. Biochem. 263:736-745(1999).
CC   -!- FUNCTION: Enzyme with a broad specificity.
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: Monomer (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC         Comment=Isoforms only differ in their C-terminus;
CC       Name=Beta-1;
CC         IsoId=P36993-1; Sequence=Displayed;
CC       Name=Beta-2;
CC         IsoId=P36993-2; Sequence=VSP_005089;
CC       Name=Beta-3;
CC         IsoId=P36993-3; Sequence=VSP_005090;
CC       Name=Beta-4;
CC         IsoId=P36993-4; Sequence=VSP_005091;
CC       Name=Beta-5;
CC         IsoId=P36993-5; Sequence=VSP_005092;
CC   -!- TISSUE SPECIFICITY: Beta-1 is expressed ubiquitously; beta-2 is
CC       expressed exclusively in brain and heart; beta-4 is expressed
CC       exclusively in brain and intestine; beta-3 and beta-5 are
CC       expressed exclusively in testis and intestine.
CC   -!- SIMILARITY: Belongs to the PP2C family.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; D17411; BAA04233.1; -; mRNA.
DR   EMBL; D17412; BAA04234.1; -; mRNA.
DR   EMBL; D45859; BAA08293.1; -; mRNA.
DR   EMBL; D45860; BAA08294.1; -; mRNA.
DR   EMBL; D45861; BAA08295.1; -; mRNA.
DR   EMBL; U09218; AAB60442.1; -; mRNA.
DR   EMBL; AB007798; BAA84471.1; -; Genomic_DNA.
DR   IPI; IPI00222989; -.
DR   IPI; IPI00399550; -.
DR   IPI; IPI00466073; -.
DR   IPI; IPI00854950; -.
DR   IPI; IPI00876176; -.
DR   PIR; I49016; I49016.
DR   PIR; S65672; S65672.
DR   RefSeq; NP_001152969.1; NM_001159497.1.
DR   RefSeq; NP_001152970.1; NM_001159498.1.
DR   RefSeq; NP_035281.1; NM_011151.2.
DR   UniGene; Mm.249695; -.
DR   ProteinModelPortal; P36993; -.
DR   SMR; P36993; 2-373.
DR   STRING; P36993; -.
DR   PhosphoSite; P36993; -.
DR   PRIDE; P36993; -.
DR   Ensembl; ENSMUST00000080217; ENSMUSP00000079107; ENSMUSG00000061130.
DR   Ensembl; ENSMUST00000112304; ENSMUSP00000107923; ENSMUSG00000061130.
DR   Ensembl; ENSMUST00000112305; ENSMUSP00000107924; ENSMUSG00000061130.
DR   Ensembl; ENSMUST00000112306; ENSMUSP00000107925; ENSMUSG00000061130.
DR   Ensembl; ENSMUST00000112307; ENSMUSP00000107926; ENSMUSG00000061130.
DR   GeneID; 19043; -.
DR   KEGG; mmu:19043; -.
DR   UCSC; uc008dtf.1; mouse.
DR   UCSC; uc008dth.1; mouse.
DR   UCSC; uc008dti.1; mouse.
DR   UCSC; uc008dtj.1; mouse.
DR   UCSC; uc008dtk.1; mouse.
DR   CTD; 19043; -.
DR   MGI; MGI:101841; Ppm1b.
DR   eggNOG; roNOG12189; -.
DR   GeneTree; ENSGT00550000074492; -.
DR   HOVERGEN; HBG053647; -.
DR   OrthoDB; EOG4BP1BZ; -.
DR   PhylomeDB; P36993; -.
DR   BRENDA; 3.1.3.16; 244.
DR   NextBio; 461936; -.
DR   ArrayExpress; P36993; -.
DR   Bgee; P36993; -.
DR   Genevestigator; P36993; -.
DR   GermOnline; ENSMUSG00000061130; 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: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   Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Protein phosphatase.
FT   CHAIN         1    390       Protein phosphatase 1B.
FT                                /FTId=PRO_0000057747.
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       243    243       Manganese 2 (By similarity).
FT   METAL       286    286       Manganese 2 (By similarity).
FT   VAR_SEQ     379    390       GAGDLEDSLVAL -> VSLHLFPKYLK (in isoform
FT                                Beta-2).
FT                                /FTId=VSP_005089.
FT   VAR_SEQ     379    390       GAGDLEDSLVAL -> FYQPSIAYSDNVFLL (in
FT                                isoform Beta-3).
FT                                /FTId=VSP_005090.
FT   VAR_SEQ     379    390       GAGDLEDSLVAL -> MADLSTSICKPS (in isoform
FT                                Beta-4).
FT                                /FTId=VSP_005091.
FT   VAR_SEQ     388    390       VAL -> FYQPSIAYSDNVFLL (in isoform Beta-
FT                                5).
FT                                /FTId=VSP_005092.
SQ   SEQUENCE   390 AA;  42795 MW;  255C97B4276189FD CRC64;
     MGAFLDKPKT EKHNAHGAGN GLRYGLSSMQ GWRVEMEDAH TAVVGIPHGL DNWSFFAVYD
     GHAGSRVANY CSTHLLEHIT TNEDFRAADK SGSALEPSVE SVKTGIRTGF LKIDEYMRNF
     SDLRNGMDRS GSTAVGVMVS PTHMYFINCG DSRAVLCRNG QVCFSTQDHK PCNPVEKERI
     QNAGGSVMIQ RVNGSLAVSR ALGDYDYKCV DGKGPTEQLV SPEPEVYEIV RAEEDEFVVL
     ACDGIWDVMS NEELCEFVKS RLEVSDDLEN VCNWVVDTCL HKGSRDNMSV VLVCFSNAPK
     VSEEAVKRDS ELDKHLESRV EEIMQKSGEE GMPDLAHVMR ILSAENIPNL PPGGGLAGKR
     HVIEAVYSRL NPHKDNDGGA GDLEDSLVAL
//
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   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   -----------------------------------------------------------------------
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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   CX6A1_MOUSE             Reviewed;         111 AA.
AC   P43024;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Cytochrome c oxidase subunit 6A1, mitochondrial;
DE   AltName: Full=Cytochrome c oxidase polypeptide VIa-liver;
DE   Flags: Precursor;
GN   Name=Cox6a1; Synonyms=Cox6al;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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=95178562; PubMed=7873616; DOI=10.1016/0167-4781(94)00232-R;
RA   Grossman L.I., Rosenthal N.H., Akamatsu M., Erickson R.P.;
RT   "Cloning, sequence analysis, and expression of a mouse cDNA encoding
RT   cytochrome c oxidase subunit VIa liver isoform.";
RL   Biochim. Biophys. Acta 1260:361-364(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2-111.
RC   STRAIN=BALB/c;
RA   Newton D., Bowman L.H.;
RL   Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 63-80 AND 83-111, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-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 subunit 6A family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA17836.1; Type=Erroneous initiation;
CC       Sequence=AAA53066.1; Type=Erroneous initiation;
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DR   EMBL; L06465; AAA53066.1; ALT_INIT; mRNA.
DR   EMBL; U08440; AAA17836.1; ALT_INIT; mRNA.
DR   IPI; IPI00121443; -.
DR   RefSeq; NP_031774.1; NM_007748.3.
DR   UniGene; Mm.43415; -.
DR   ProteinModelPortal; P43024; -.
DR   SMR; P43024; 27-109.
DR   STRING; P43024; -.
DR   SWISS-2DPAGE; P43024; -.
DR   PRIDE; P43024; -.
DR   Ensembl; ENSMUST00000040154; ENSMUSP00000047661; ENSMUSG00000041697.
DR   GeneID; 12861; -.
DR   KEGG; mmu:12861; -.
DR   UCSC; uc008zdt.1; mouse.
DR   CTD; 12861; -.
DR   MGI; MGI:103099; Cox6a1.
DR   eggNOG; roNOG17101; -.
DR   HOVERGEN; HBG060482; -.
DR   InParanoid; P43024; -.
DR   OMA; RIRSKRF; -.
DR   OrthoDB; EOG4N04GG; -.
DR   PhylomeDB; P43024; -.
DR   NextBio; 282424; -.
DR   ArrayExpress; P43024; -.
DR   Bgee; P43024; -.
DR   CleanEx; MM_COX6A1; -.
DR   Genevestigator; P43024; -.
DR   GermOnline; ENSMUSG00000041697; Mus musculus.
DR   GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:InterPro.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR   InterPro; IPR001349; Cyt_c_oxidase_su6a.
DR   InterPro; IPR018507; Cyt_c_oxidase_su6a_CS.
DR   Gene3D; G3DSA:4.10.95.10; COX6A; 1.
DR   PANTHER; PTHR11504; COX6A; 1.
DR   Pfam; PF02046; COX6A; 1.
DR   PIRSF; PIRSF000277; COX6A1; 1.
DR   ProDom; PD006036; Cyt_c_oxidase_su6a; 1.
DR   SUPFAM; SSF81411; COX6A; 1.
DR   PROSITE; PS01329; COX6A; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Transit peptide.
FT   TRANSIT       1     26       Mitochondrion (By similarity).
FT   CHAIN        27    111       Cytochrome c oxidase subunit 6A1,
FT                                mitochondrial.
FT                                /FTId=PRO_0000006120.
SQ   SEQUENCE   111 AA;  12352 MW;  76D5EDA5F79EC5E7 CRC64;
     MASAVLSASR VSRPLGRALP GLRRPMSSGA HGEEGSARMW KALTYFVALP GVGVSMLNVF
     LKSRHEEHER PPFVAYPHLR IRTKPFPWGD GNHTLFHNPH VNPLPTGYED E
//
ID   RAD52_MOUSE             Reviewed;         420 AA.
AC   P43352;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=DNA repair protein RAD52 homolog;
GN   Name=Rad52;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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=95130108; PubMed=7829098; DOI=10.1006/geno.1994.1503;
RA   Bendixen C., Sunjevaric I., Bauchwitz R., Rothstein R.;
RT   "Identification of a mouse homologue of the Saccharomyces cerevisiae
RT   recombination and repair gene, RAD52.";
RL   Genomics 23:300-303(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C3H;
RX   MEDLINE=95293373; PubMed=7774919; DOI=10.1016/0888-7543(95)80126-7;
RA   Shen Z., Denison K., Lobb R., Gatewood J.M., Chen D.J.;
RT   "The human and mouse homologs of the yeast RAD52 gene: cDNA cloning,
RT   sequence analysis, assignment to human chromosome 12p12.2-p13, and
RT   mRNA expression in mouse tissues.";
RL   Genomics 25:199-206(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X CBA; TISSUE=Thymus;
RX   MEDLINE=95059179; PubMed=7526206; DOI=10.1016/0921-8777(94)90040-X;
RA   Muris D.F., Bezzubova O., Buerstedde J.-M., Vreeken K., Balajee A.S.,
RA   Osgood C.J., Troelstra C., Hoeijmakers J.H., Ostermann K., Schmidt H.,
RA   Natarajan A.T., Eeken J.C.J., Lohman P.H.M., Pastink A.;
RT   "Cloning of human and mouse genes homologous to RAD52, a yeast gene
RT   involved in DNA repair and recombination.";
RL   Mutat. Res. 315:295-305(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Sunjevaric I., Bendixen C., Mortensen U.H., Miljkovic V.,
RA   Rothstein R.;
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in double-stranded break repair. Plays a
CC       central role in genetic recombination and DNA repair by promoting
CC       the annealing of complementary single-stranded DNA and by
CC       stimulation of the RAD51 recombinase (By similarity).
CC   -!- SUBUNIT: Forms a undecameric ring (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- SIMILARITY: Belongs to the RAD52 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; U06837; AAA75441.1; -; mRNA.
DR   EMBL; U12135; AAA85794.1; -; mRNA.
DR   EMBL; Z32767; CAA83659.1; -; mRNA.
DR   EMBL; AF004854; AAB69174.1; -; Genomic_DNA.
DR   IPI; IPI00119277; -.
DR   PIR; A55727; A55727.
DR   PIR; A56529; A56529.
DR   RefSeq; NP_001159853.1; NM_001166381.1.
DR   UniGene; Mm.149; -.
DR   ProteinModelPortal; P43352; -.
DR   SMR; P43352; 25-210.
DR   STRING; P43352; -.
DR   PhosphoSite; P43352; -.
DR   PRIDE; P43352; -.
DR   Ensembl; ENSMUST00000032269; ENSMUSP00000032269; ENSMUSG00000030166.
DR   GeneID; 19365; -.
DR   KEGG; mmu:19365; -.
DR   UCSC; uc009dmp.1; mouse.
DR   CTD; 19365; -.
DR   MGI; MGI:101949; Rad52.
DR   eggNOG; roNOG04433; -.
DR   HOVERGEN; HBG054676; -.
DR   InParanoid; P43352; -.
DR   OMA; EMWDLTP; -.
DR   OrthoDB; EOG451DR1; -.
DR   PhylomeDB; P43352; -.
DR   ArrayExpress; P43352; -.
DR   Bgee; P43352; -.
DR   CleanEx; MM_RAD52; -.
DR   Genevestigator; P43352; -.
DR   GermOnline; ENSMUSG00000030166; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:MGI.
DR   InterPro; IPR004585; DNA_recomb/repair_Rad52.
DR   InterPro; IPR007232; Rad52_Rad22.
DR   PANTHER; PTHR12132; Rad52_Rad22; 1.
DR   Pfam; PF04098; Rad52_Rad22; 1.
DR   TIGRFAMs; TIGR00607; rad52; 1.
PE   2: Evidence at transcript level;
KW   DNA damage; DNA recombination; DNA repair; Nucleus; Phosphoprotein.
FT   CHAIN         1    420       DNA repair protein RAD52 homolog.
FT                                /FTId=PRO_0000173882.
FT   MOD_RES     200    200       Phosphoserine (By similarity).
FT   MOD_RES     339    339       Phosphothreonine (By similarity).
FT   CONFLICT    195    195       E -> K (in Ref. 2; AAA85794).
FT   CONFLICT    300    300       Missing (in Ref. 2; AAA85794).
FT   CONFLICT    352    352       A -> G (in Ref. 1 and 4).
FT   CONFLICT    401    401       Missing (in Ref. 1 and 4).
FT   CONFLICT    418    418       D -> N (in Ref. 3; CAA83659).
SQ   SEQUENCE   420 AA;  46910 MW;  84514C8579072F98 CRC64;
     MAGPEEAVHR GCDNHPPFVG GKSVLLFGQS QYTADEYQAI QKALRQRLGP EYISSRMAGG
     GQKVCYIEGH RVINLANEMF GYNGWAHSIT QQNVDFVDLN NGKFYVGVCA FVKVQLKDGS
     YHEDVGYGVS EGLRSKALSL EKARKEAVTD GLKRALRSFG NALGNCILDK DYLRSLNKLP
     RQLPLDVDLT KTKREDFEPS VEQARYNSCR QNEALGLPKP QEVTSPCRSS PPHDSNIKLQ
     GAKDISSSCS LAATLESDAT HQRKLRKLRQ KQLQQQFREQ METRRQSHAP AEEVAAKHAA
     VLPAPPKHST PVTAASELLQ EKVVFPDNLE ENLEMWDLTP DLEDIIKPLC RAEPAQTSAT
     RTFNNQDSVP HIHCHQKPQE KPGPGHLQTC NTNQHVLGSR EDSEPHRKSQ DLKKRKLDPS
//
ID   CBP_MOUSE               Reviewed;        2441 AA.
AC   P45481;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   08-MAR-2011, entry version 123.
DE   RecName: Full=CREB-binding protein;
DE            EC=2.3.1.48;
GN   Name=Crebbp; Synonyms=Cbp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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=94019866; PubMed=8413673; DOI=10.1038/365855a0;
RA   Chrivia J.C., Kwok R.P.S., Lamb N., Hagiwara M., Montminy M.R.,
RA   Goodman R.H.;
RT   "Phosphorylated CREB binds specifically to the nuclear protein CBP.";
RL   Nature 365:855-859(1993).
RN   [2]
RP   INTERACTION WITH NCOA1.
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   [3]
RP   INTERACTION WITH CREB1, AND MUTAGENESIS OF ARG-600.
RX   PubMed=8552098;
RA   Parker D., Ferreri K., Nakajima T., LaMorte V.J., Evans R.,
RA   Koerber S.C., Hoeger C., Montminy M.R.;
RT   "Phosphorylation of CREB at Ser-133 induces complex formation with
RT   CREB-binding protein via a direct mechanism.";
RL   Mol. Cell. Biol. 16:694-703(1996).
RN   [4]
RP   INTERACTION WITH NCOA3.
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   [5]
RP   INTERACTION WITH CARM1, METHYLATION AT ARG-600 AND ARG-624, AND
RP   FUNCTION.
RX   MEDLINE=21625315; PubMed=11701890; DOI=10.1126/science.1065961;
RA   Xu W., Chen H., Du K., Asahara H., Tini M., Emerson B.M., Montminy M.,
RA   Evans R.M.;
RT   "A transcriptional switch mediated by cofactor methylation.";
RL   Science 294:2507-2511(2001).
RN   [6]
RP   INTERACTION WITH CITED4.
RX   PubMed=12504852; DOI=10.1006/geno.2002.7005;
RA   Yahata T., Takedatsu H., Dunwoodie S.L., Braganca J., Swingler T.,
RA   Withington S.L., Hur J., Coser K.R., Isselbacher K.J.,
RA   Bhattacharya S., Shioda T.;
RT   "Cloning of mouse Cited4, a member of the CITED family p300/CBP-
RT   binding transcriptional coactivators: induced expression in mammary
RT   epithelial cells.";
RL   Genomics 80:601-613(2002).
RN   [7]
RP   INTERACTION WITH MAF.
RX   PubMed=11943779; DOI=10.1074/jbc.M201821200;
RA   Chen Q., Dowhan D.H., Liang D., Moore D.D., Overbeek P.A.;
RT   "CREB-binding protein/p300 co-activation of crystallin gene
RT   expression.";
RL   J. Biol. Chem. 277:24081-24089(2002).
RN   [8]
RP   SUMOYLATION AT LYS-999; LYS-1015; LYS-1034 AND LYS-1057, INTERACTION
RP   WITH DAXX, FUNCTION, AND MUTAGENESIS OF LYS-999; LYS-1015; LYS-1034;
RP   LYS-1043; LYS-1053; LYS-1057 AND LYS-1061.
RX   PubMed=16287980; DOI=10.1073/pnas.0504460102;
RA   Kuo H.-Y., Chang C.-C., Jeng J.-C., Hu H.-M., Lin D.-Y., Maul G.G.,
RA   Kwok R.P.S., Shih H.-M.;
RT   "SUMO modification negatively modulates the transcriptional activity
RT   of CREB-binding protein via the recruitment of Daxx.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:16973-16978(2005).
RN   [9]
RP   INTERACTION WITH ZCCHC12.
RX   PubMed=18160706; DOI=10.1128/MCB.01038-07;
RA   Cho G., Lim Y., Zand D., Golden J.A.;
RT   "Sizn1 is a novel protein that functions as a transcriptional
RT   coactivator of bone morphogenic protein signaling.";
RL   Mol. Cell. Biol. 28:1565-1572(2008).
CC   -!- FUNCTION: Acetylates histones, giving a specific tag for
CC       transcriptional activation. Also acetylates non-histone proteins,
CC       like NCOA3 coactivator. Binds specifically to phosphorylated CREB
CC       and enhances its transcriptional activity toward cAMP-responsive
CC       genes. Acts as a coactivator of ALX1 in the presence of EP300 (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + [histone] = CoA + acetyl-
CC       [histone].
CC   -!- SUBUNIT: Found in a complex containing NCOA2; NCOA3; IKKA; IKKB
CC       and IKBKG. Probably part of a complex with HIF1A and EP300.
CC       Interacts with phosphorylated CREB1. Interacts with the C-terminal
CC       region of CITED4. The TAZ-type 1 domain interacts with HIF1A.
CC       Interacts with SRCAP, CARM1, ELF3, MLLT7/FOXO4, N4BP2, NCOA1,
CC       NCOA3, NCOA6, PCAF, PELP1, PML, SMAD1, SMAD2, SMAD3, SPIB, TRERF1
CC       and ZCCHC12. Interacts with KLF1; the interaction results in
CC       acetylation and enhancement of transcriptional activity of KLF1
CC       (By similarity). Interacts with DAXX; the interaction is dependent
CC       on CBP sumoylation and results in suppression of the
CC       transcriptional activity via recruitment of HDAC2 to DAAX.
CC       Interacts with MAF. Interacts with MTDH (By similarity). Interacts
CC       with MAFG; the interaction acetylates MAFG in the basic region and
CC       stimulates NFE2 transcriptional activity through increasing its
CC       DNA-binding activity. Interacts with IRF2; the interaction
CC       acetylates IRF2 and regulates its activity on the H4 promoter.
CC       Interacts (via N-terminus) with SS18L1/CREST (via C-terminus) (By
CC       similarity). Interacts with MECOM (By similarity).
CC   -!- INTERACTION:
CC       P88946:- (xeno); NbExp=4; IntAct=EBI-296306, EBI-936023;
CC       P16220:CREB1 (xeno); NbExp=1; IntAct=EBI-296306, EBI-711855;
CC       Q60749:Khdrbs1; NbExp=3; IntAct=EBI-296306, EBI-519077;
CC       P10242:MYB (xeno); NbExp=1; IntAct=EBI-296306, EBI-298355;
CC       Q04207:Rela; NbExp=1; IntAct=EBI-296306, EBI-644400;
CC       P36956-1:SREBF1 (xeno); NbExp=1; IntAct=EBI-296306, EBI-948328;
CC       P04637:TP53 (xeno); NbExp=2; IntAct=EBI-296306, EBI-366083;
CC       Q64451:Trp53; NbExp=1; IntAct=EBI-296306, EBI-493476;
CC       Q9EPK5:Wwtr1; NbExp=1; IntAct=EBI-296306, EBI-1211920;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus.
CC       Note=Recruited to nuclear bodies by SS18L1/CREST. In the presence
CC       of ALX1 relocalizes from the cytoplasm to the nucleus (By
CC       similarity).
CC   -!- PTM: Methylation of the KIX domain by CARM1 blocks association
CC       with CREB. This results in the blockade of CREB signaling, and in
CC       activation of apoptotic response.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- PTM: Sumoylation negatively regulates transcriptional activity via
CC       the recruitment of DAAX.
CC   -!- SIMILARITY: Contains 1 bromo domain.
CC   -!- SIMILARITY: Contains 1 KIX domain.
CC   -!- SIMILARITY: Contains 2 TAZ-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 ZZ-type zinc finger.
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DR   EMBL; S66385; AAB28651.1; -; mRNA.
DR   IPI; IPI00875480; -.
DR   PIR; S39161; S39161.
DR   UniGene; Mm.132238; -.
DR   UniGene; Mm.392384; -.
DR   PDB; 1F81; NMR; -; A=1764-1849.
DR   PDB; 1JJS; NMR; -; A=2067-2112.
DR   PDB; 1KBH; NMR; -; B=2059-2117.
DR   PDB; 1KDX; NMR; -; A=586-666.
DR   PDB; 1L8C; NMR; -; A=345-439.
DR   PDB; 1R8U; NMR; -; B=340-439.
DR   PDB; 1SB0; NMR; -; A=586-672.
DR   PDB; 1TOT; NMR; -; A=1700-1751.
DR   PDB; 1U2N; NMR; -; A=340-439.
DR   PDB; 2AGH; NMR; -; B=586-672.
DR   PDB; 2C52; NMR; -; A=2059-2117.
DR   PDB; 2KA4; NMR; -; A=340-439.
DR   PDB; 2KA6; NMR; -; A=1764-1855.
DR   PDB; 2KKJ; NMR; -; A=2059-2117.
DR   PDB; 2L14; NMR; -; A=2059-2117.
DR   PDBsum; 1F81; -.
DR   PDBsum; 1JJS; -.
DR   PDBsum; 1KBH; -.
DR   PDBsum; 1KDX; -.
DR   PDBsum; 1L8C; -.
DR   PDBsum; 1R8U; -.
DR   PDBsum; 1SB0; -.
DR   PDBsum; 1TOT; -.
DR   PDBsum; 1U2N; -.
DR   PDBsum; 2AGH; -.
DR   PDBsum; 2C52; -.
DR   PDBsum; 2KA4; -.
DR   PDBsum; 2KA6; -.
DR   PDBsum; 2KKJ; -.
DR   PDBsum; 2L14; -.
DR   ProteinModelPortal; P45481; -.
DR   SMR; P45481; 340-439, 586-666, 1082-1198, 1278-1314, 1324-1751, 1764-1849, 2059-2117.
DR   DisProt; DP00348; -.
DR   DIP; DIP-5974N; -.
DR   IntAct; P45481; 28.
DR   MINT; MINT-203452; -.
DR   STRING; P45481; -.
DR   PhosphoSite; P45481; -.
DR   PRIDE; P45481; -.
DR   Ensembl; ENSMUST00000080297; ENSMUSP00000079177; ENSMUSG00000022521.
DR   MGI; MGI:1098280; Crebbp.
DR   eggNOG; roNOG05886; -.
DR   GeneTree; ENSGT00550000074306; -.
DR   HOVERGEN; HBG000185; -.
DR   BRENDA; 2.3.1.48; 244.
DR   ArrayExpress; P45481; -.
DR   Bgee; P45481; -.
DR   CleanEx; MM_CREBBP; -.
DR   Genevestigator; P45481; -.
DR   GermOnline; ENSMUSG00000022521; Mus musculus.
DR   GO; GO:0000940; C:condensed chromosome outer kinetochore; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000123; C:histone acetyltransferase complex; IDA:MGI.
DR   GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
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; ISS:UniProtKB.
DR   GO; GO:0051577; F:MyoD binding; ISS:UniProtKB.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030718; P:germ-line stem cell maintenance; IMP:MGI.
DR   GO; GO:0016573; P:histone acetylation; ISS:UniProtKB.
DR   GO; GO:0018076; P:N-terminal peptidyl-lysine acetylation; ISS:UniProtKB.
DR   GO; GO:0051091; P:positive regulation of transcription factor activity; TAS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA: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   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Bromodomain; Cytoplasm;
KW   Isopeptide bond; Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW   Repeat; Transcription; Transcription regulation; Transferase;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   2441       CREB-binding protein.
FT                                /FTId=PRO_0000211191.
FT   DOMAIN      586    665       KIX.
FT   DOMAIN     1104   1176       Bromo.
FT   ZN_FING     346    432       TAZ-type 1.
FT   ZN_FING    1702   1745       ZZ-type.
FT   ZN_FING    1766   1847       TAZ-type 2.
FT   REGION      226    409       Interaction with SRCAP (By similarity).
FT   COMPBIAS   1062   1065       Poly-Glu.
FT   COMPBIAS   1556   1563       Poly-Glu.
FT   COMPBIAS   1944   1949       Poly-Pro.
FT   COMPBIAS   1968   1971       Poly-Gln.
FT   COMPBIAS   2082   2086       Poly-Gln.
FT   COMPBIAS   2200   2216       Poly-Gln.
FT   COMPBIAS   2296   2299       Poly-Gln.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     120    120       Phosphoserine (By similarity).
FT   MOD_RES     273    273       Phosphoserine (By similarity).
FT   MOD_RES     600    600       Omega-N-methylated arginine (Probable).
FT   MOD_RES     624    624       Omega-N-methylated arginine (Probable).
FT   MOD_RES    1015   1015       N6-acetyllysine (By similarity).
FT   MOD_RES    1031   1031       Phosphoserine (By similarity).
FT   MOD_RES    1073   1073       Phosphoserine (By similarity).
FT   MOD_RES    1217   1217       N6-acetyllysine (By similarity).
FT   MOD_RES    1584   1584       N6-acetyllysine (By similarity).
FT   MOD_RES    1589   1589       N6-acetyllysine (By similarity).
FT   MOD_RES    1592   1592       N6-acetyllysine (By similarity).
FT   MOD_RES    1593   1593       N6-acetyllysine (By similarity).
FT   MOD_RES    1596   1596       N6-acetyllysine (By similarity).
FT   MOD_RES    1598   1598       N6-acetyllysine (By similarity).
FT   MOD_RES    1742   1742       N6-acetyllysine (By similarity).
FT   MOD_RES    1745   1745       N6-acetyllysine (By similarity).
FT   MOD_RES    1756   1756       Phosphoserine (By similarity).
FT   MOD_RES    2064   2064       Phosphoserine (By similarity).
FT   MOD_RES    2077   2077       Phosphoserine (By similarity).
FT   MOD_RES    2080   2080       Phosphoserine (By similarity).
FT   CROSSLNK    999    999       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO-1).
FT   CROSSLNK   1034   1034       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO-1).
FT   CROSSLNK   1057   1057       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO-1).
FT   MUTAGEN     600    600       R->N: Abolishes binding to CREB.
FT   MUTAGEN     999    999       K->R: Enhanced transcriptional activity.
FT                                No sumoylation, loss of recruitment of
FT                                HDAC2 to DAAX and greatly enhanced
FT                                transcritional activity; when associated
FT                                with R-1034 and R-1057.
FT   MUTAGEN    1015   1015       K->R: No change in sumoylation.
FT   MUTAGEN    1034   1034       K->R: Enhanced transcriptional activity.
FT                                No sumoylation, loss of recruitment of
FT                                HDAC2 to DAAX and greatly enhanced
FT                                transcritional activity; when associated
FT                                with R-999 and R-1057.
FT   MUTAGEN    1043   1043       K->R: No change in sumoylation.
FT   MUTAGEN    1053   1053       K->R: No change in sumoylation.
FT   MUTAGEN    1057   1057       K->R: Enhanced transcriptional activity.
FT                                No sumoylation, loss of recruitment of
FT                                HDAC2 to DAAX and greatly enhanced
FT                                transcritional activity; when associated
FT                                with R-999 and R-1034.
FT   MUTAGEN    1061   1061       K->R: No change in sumoylation.
FT   MUTAGEN    1087   1087       K->R: No change in sumoylation.
FT   HELIX       347    372
FT   HELIX       384    396
FT   HELIX       400    402
FT   HELIX       406    420
FT   HELIX       429    433
FT   TURN        587    590
FT   HELIX       591    594
FT   HELIX       597    611
FT   HELIX       617    621
FT   HELIX       623    640
FT   HELIX       646    662
FT   TURN        663    665
FT   TURN        667    671
FT   TURN       1709   1711
FT   STRAND     1713   1726
FT   HELIX      1731   1737
FT   STRAND     1741   1746
FT   HELIX      1765   1785
FT   HELIX      1794   1808
FT   HELIX      1812   1815
FT   HELIX      1818   1833
FT   HELIX      1844   1849
FT   STRAND     2061   2064
FT   HELIX      2068   2075
FT   STRAND     2076   2079
FT   HELIX      2088   2091
FT   HELIX      2097   2100
FT   HELIX      2102   2104
FT   STRAND     2106   2108
SQ   SEQUENCE   2441 AA;  265474 MW;  0ABB028C3112F419 CRC64;
     MAENLLDGPP NPKRAKLSSP GFSANDNTDF GSLFDLENDL PDELIPNGEL SLLNSGNLVP
     DAASKHKQLS ELLRGGSGSS INPGIGNVSA SSPVQQGLGG QAQGQPNSTN MASLGAMGKS
     PLNQGDSSTP NLPKQAASTS GPTPPASQAL NPQAQKQVGL VTSSPATSQT GPGICMNANF
     NQTHPGLLNS NSGHSLMNQA QQGQAQVMNG SLGAAGRGRG AGMPYPAPAM QGATSSVLAE
     TLTQVSPQMA GHAGLNTAQA GGMTKMGMTG TTSPFGQPFS QTGGQQMGAT GVNPQLASKQ
     SMVNSLPAFP TDIKNTSVTT VPNMSQLQTS VGIVPTQAIA TGPTADPEKR KLIQQQLVLL
     LHAHKCQRRE QANGEVRACS LPHCRTMKNV LNHMTHCQAP KACQVAHCAS SRQIISHWKN
     CTRHDCPVCL PLKNASDKRN QQTILGSPAS GIQNTIGSVG AGQQNATSLS NPNPIDPSSM
     QRAYAALGLP YMNQPQTQLQ PQVPGQQPAQ PPAHQQMRTL NALGNNPMSV PAGGITTDQQ
     PPNLISESAL PTSLGATNPL MNDGSNSGNI GSLSTIPTAA PPSSTGVRKG WHEHVTQDLR
     SHLVHKLVQA IFPTPDPAAL KDRRMENLVA YAKKVEGDMY ESANSRDEYY HLLAEKIYKI
     QKELEEKRRT RLHKQGILGN QPALPASGAQ PPVIPPAQSV RPPNGPLPLP VNRMQVSQGM
     NSFNPMSLGN VQLPQAPMGP RAASPMNHSV QMNSMASVPG MAISPSRMPQ PPNMMGTHAN
     NIMAQAPTQN QFLPQNQFPS SSGAMSVNSV GMGQPAAQAG VSQGQEPGAA LPNPLNMLAP
     QASQLPCPPV TQSPLHPTPP PASTAAGMPS LQHPTAPGMT PPQPAAPTQP STPVSSGQTP
     TPTPGSVPSA AQTQSTPTVQ AAAQAQVTPQ PQTPVQPPSV ATPQSSQQQP TPVHTQPPGT
     PLSQAAASID NRVPTPSTVT SAETSSQQPG PDVPMLEMKT EVQTDDAEPE PTESKGEPRS
     EMMEEDLQGS SQVKEETDTT EQKSEPMEVE EKKPEVKVEA KEEEENSSND TASQSTSPSQ
     PRKKIFKPEE LRQALMPTLE ALYRQDPESL PFRQPVDPQL LGIPDYFDIV KNPMDLSTIK
     RKLDTGQYQE PWQYVDDVRL MFNNAWLYNR KTSRVYKFCS KLAEVFEQEI DPVMQSLGYC
     CGRKYEFSPQ TLCCYGKQLC TIPRDAAYYS YQNRYHFCGK CFTEIQGENV TLGDDPSQPQ
     TTISKDQFEK KKNDTLDPEP FVDCKECGRK MHQICVLHYD IIWPSGFVCD NCLKKTGRPR
     KENKFSAKRL QTTRLGNHLE DRVNKFLRRQ NHPEAGEVFV RVVASSDKTV EVKPGMKSRF
     VDSGEMSESF PYRTKALFAF EEIDGVDVCF FGMHVQDTAL IAPHQIQGCV YISYLDSIHF
     FRPRCLRTAV YHEILIGYLE YVKKLVYVTA HIWACPPSEG DDYIFHCHPP DQKIPKPKRL
     QEWYKKMLDK AFAERIINDY KDIFKQANED RLTSAKELPY FEGDFWPNVL EESIKELEQE
     EEERKKEEST AASETPEGSQ GDSKNAKKKN NKKTNKNKSS ISRANKKKPS MPNVSNDLSQ
     KLYATMEKHK EVFFVIHLHA GPVISTQPPI VDPDPLLSCD LMDGRDAFLT LARDKHWEFS
     SLRRSKWSTL CMLVELHTQG QDRFVYTCNE CKHHVETRWH CTVCEDYDLC INCYNTKSHT
     HKMVKWGLGL DDEGSSQGEP QSKSPQESRR LSIQRCIQSL VHACQCRNAN CSLPSCQKMK
     RVVQHTKGCK RKTNGGCPVC KQLIALCCYH AKHCQENKCP VPFCLNIKHN VRQQQIQHCL
     QQAQLMRRRM ATMNTRNVPQ QSLPSPTSAP PGTPTQQPST PQTPQPPAQP QPSPVNMSPA
     GFPNVARTQP PTIVSAGKPT NQVPAPPPPA QPPPAAVEAA RQIEREAQQQ QHLYRANINN
     GMPPGRDGMG TPGSQMTPVG LNVPRPNQVS GPVMSSMPPG QWQQAPIPQQ QPMPGMPRPV
     MSMQAQAAVA GPRMPNVQPN RSISPSALQD LLRTLKSPSS PQQQQQVLNI LKSNPQLMAA
     FIKQRTAKYV ANQPGMQPQP GLQSQPGMQP QPGMHQQPSL QNLNAMQAGV PRPGVPPPQP
     AMGGLNPQGQ ALNIMNPGHN PNMTNMNPQY REMVRRQLLQ HQQQQQQQQQ QQQQQQNSAS
     LAGGMAGHSQ FQQPQGPGGY APAMQQQRMQ QHLPIQGSSM GQMAAPMGQL GQMGQPGLGA
     DSTPNIQQAL QQRILQQQQM KQQIGSPGQP NPMSPQQHML SGQPQASHLP GQQIATSLSN
     QVRSPAPVQS PRPQSQPPHS SPSPRIQPQP SPHHVSPQTG TPHPGLAVTM ASSMDQGHLG
     NPEQSAMLPQ LNTPNRSALS SELSLVGDTT GDTLEKFVEG L
//
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.
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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   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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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   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.
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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   INPP_MOUSE              Reviewed;         396 AA.
AC   P49442; Q8R3L1;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 2.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Inositol polyphosphate 1-phosphatase;
DE            Short=IPP;
DE            Short=IPPase;
DE            EC=3.1.3.57;
GN   Name=Inpp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=96163893; PubMed=8586440; DOI=10.1006/geno.1995.0030;
RA   Okabe I., Nussbaum R.L.;
RT   "Identification and chromosomal mapping of the mouse inositol
RT   polyphosphate 1-phosphatase gene.";
RL   Genomics 30:358-360(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 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: 1D-myo-inositol 1,4-bisphosphate + H(2)O = 1D-
CC       myo-inositol 4-phosphate + phosphate.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: Inhibited by Li(+) (By similarity).
CC   -!- PATHWAY: Signal transduction; phosphatidylinositol signaling
CC       pathway.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase family.
CC   -----------------------------------------------------------------------
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DR   EMBL; U27295; AAA97574.1; -; mRNA.
DR   EMBL; AK078382; BAC37245.1; -; mRNA.
DR   EMBL; BC025072; AAH25072.1; -; mRNA.
DR   IPI; IPI00114801; -.
DR   RefSeq; NP_032410.2; NM_008384.2.
DR   UniGene; Mm.917; -.
DR   ProteinModelPortal; P49442; -.
DR   SMR; P49442; 1-395.
DR   STRING; P49442; -.
DR   PhosphoSite; P49442; -.
DR   UCD-2DPAGE; P49442; -.
DR   PRIDE; P49442; -.
DR   Ensembl; ENSMUST00000027271; ENSMUSP00000027271; ENSMUSG00000026102.
DR   GeneID; 16329; -.
DR   KEGG; mmu:16329; -.
DR   UCSC; uc007ayo.1; mouse.
DR   CTD; 16329; -.
DR   MGI; MGI:104848; Inpp1.
DR   eggNOG; roNOG15512; -.
DR   GeneTree; ENSGT00390000014061; -.
DR   HOGENOM; HBG443765; -.
DR   HOVERGEN; HBG006163; -.
DR   InParanoid; P49442; -.
DR   OMA; TFKWDSC; -.
DR   OrthoDB; EOG41C6WB; -.
DR   PhylomeDB; P49442; -.
DR   BRENDA; 3.1.3.57; 244.
DR   NextBio; 289410; -.
DR   ArrayExpress; P49442; -.
DR   Bgee; P49442; -.
DR   CleanEx; MM_INPP1; -.
DR   Genevestigator; P49442; -.
DR   GermOnline; ENSMUSG00000026102; Mus musculus.
DR   GO; GO:0004441; F:inositol-1,4-bisphosphate 1-phosphatase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   Hydrolase; Lithium; Magnesium; Metal-binding; Phosphoprotein.
FT   CHAIN         1    396       Inositol polyphosphate 1-phosphatase.
FT                                /FTId=PRO_0000142511.
FT   REGION      155    158       Substrate binding (By similarity).
FT   METAL        79     79       Magnesium 1 (By similarity).
FT   METAL       153    153       Magnesium 1 (By similarity).
FT   METAL       153    153       Magnesium 2 (By similarity).
FT   METAL       155    155       Magnesium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       156    156       Magnesium 2 (By similarity).
FT   METAL       313    313       Magnesium 2 (By similarity).
FT   BINDING     119    119       Substrate (By similarity).
FT   BINDING     313    313       Substrate (By similarity).
FT   MOD_RES     314    314       Phosphoserine (By similarity).
FT   CONFLICT     10     10       C -> R (in Ref. 1; AAA97574).
FT   CONFLICT    276    276       V -> A (in Ref. 1; AAA97574).
SQ   SEQUENCE   396 AA;  43346 MW;  799D555B153FC975 CRC64;
     MSDILLELLC VSEKAANIAR ACRQQETLFQ LLIEEKKGAE KNKKFAADFK TLADVLVQEV
     IKQNMENKFP GLGKKVFGEE SNEFTNDLGE KITVELQSTE EETAELLSKV LNGNMPASEA
     LAQVVHEDVD LTDPTLESLD ISIPHESLGI WVDPIDSTYQ YIKGSANVKS NQGIFPSGLQ
     CVTILIGVYD LQTGLPLMGV INQPFASQNL TTLRWKGQCY WGLSYMGTNI HSLQLAISKS
     DSETQTENSD REFSSPFSAV ISTSEKDTIK AALSRVCGGS VFPAAGAGYK SLCVIQGLAD
     IYIFSEDTTY KWDSCAAHAI LRAMGGGIVD MKECLERSPD TGLDLPQLLY HVENKGASGV
     ELWANKGGLI AYRSRNRLDT FLSRLIQNLG PVKTQA
//
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   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   Distributed under the Creative Commons Attribution-NoDerivs License
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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   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.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   ATPB_MOUSE              Reviewed;         529 AA.
AC   P56480; Q0QEP4; Q3TFD7; Q3TIP9; Q3TK44; Q3TWD5; Q3TX28; Q3U6U4;
AC   Q3U774; Q3UB69; Q3UF69; Q8CI65; Q8VEJ5; Q9CTI7; Q9CWX7;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2002, sequence version 2.
DT   08-MAR-2011, entry version 114.
DE   RecName: Full=ATP synthase subunit beta, mitochondrial;
DE            EC=3.6.3.14;
DE   Flags: Precursor;
GN   Name=Atp5b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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=20125578; PubMed=10657236; DOI=10.1042/0264-6021:3460033;
RA   Andersson U., Antonicka H., Houstek J., Cannon B.;
RT   "A novel principle for conferring selectivity to poly(A)-binding
RT   proteins: interdependence of two ATP synthase beta-subunit mRNA-
RT   binding proteins.";
RL   Biochem. J. 346:33-39(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, and C57BL/6J;
RC   TISSUE=Amnion, Bone marrow, Embryonic stem cell, Heart, Kidney, Liver,
RC   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   STRAIN=Czech II, and FVB/N;
RC   TISSUE=Mammary tumor, 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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 65-509.
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   [5]
RP   PROTEIN SEQUENCE OF 95-121; 125-155; 162-198; 202-239; 242-259;
RP   265-279; 282-345; 352-422; 433-456 AND 463-489, 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   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-259 AND LYS-522,
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).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529, 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: 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.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
CC       H(+)(Out).
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       Note=Peripheral membrane protein.
CC   -!- PTM: Acetylation of Lys-133 is observed in liver mitochondria from
CC       fasted mice but not from fed mice.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH37127.1; 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; AF030559; AAB86421.1; -; mRNA.
DR   EMBL; AK003460; BAB22802.1; -; mRNA.
DR   EMBL; AK010314; BAB26846.1; -; mRNA.
DR   EMBL; AK084009; BAC39095.1; -; mRNA.
DR   EMBL; AK145684; BAE26587.1; -; mRNA.
DR   EMBL; AK148891; BAE28692.1; -; mRNA.
DR   EMBL; AK150599; BAE29691.1; -; mRNA.
DR   EMBL; AK151081; BAE30095.1; -; mRNA.
DR   EMBL; AK151600; BAE30540.1; -; mRNA.
DR   EMBL; AK152788; BAE31497.1; -; mRNA.
DR   EMBL; AK152976; BAE31630.1; -; mRNA.
DR   EMBL; AK153099; BAE31720.1; -; mRNA.
DR   EMBL; AK159444; BAE35088.1; -; mRNA.
DR   EMBL; AK159737; BAE35331.1; -; mRNA.
DR   EMBL; AK159978; BAE35529.1; -; mRNA.
DR   EMBL; AK160199; BAE35689.1; -; mRNA.
DR   EMBL; AK160608; BAE35911.1; -; mRNA.
DR   EMBL; AK164383; BAE37764.1; -; mRNA.
DR   EMBL; AK166525; BAE38829.1; -; mRNA.
DR   EMBL; AK166603; BAE38888.1; -; mRNA.
DR   EMBL; AK166979; BAE39161.1; -; mRNA.
DR   EMBL; AK167119; BAE39267.1; -; mRNA.
DR   EMBL; AK167160; BAE39301.1; -; mRNA.
DR   EMBL; AK167728; BAE39769.1; -; mRNA.
DR   EMBL; AK167764; BAE39797.1; -; mRNA.
DR   EMBL; AK168692; BAE40537.1; -; mRNA.
DR   EMBL; AK168941; BAE40749.1; -; mRNA.
DR   EMBL; AK169184; BAE40961.1; -; mRNA.
DR   EMBL; BC018392; AAH18392.1; -; mRNA.
DR   EMBL; BC037127; AAH37127.1; ALT_INIT; mRNA.
DR   EMBL; BC046616; AAH46616.1; -; mRNA.
DR   EMBL; DQ403100; ABD77233.1; -; mRNA.
DR   IPI; IPI00468481; -.
DR   RefSeq; NP_058054.2; NM_016774.3.
DR   UniGene; Mm.238973; -.
DR   ProteinModelPortal; P56480; -.
DR   SMR; P56480; 51-527.
DR   IntAct; P56480; 26.
DR   STRING; P56480; -.
DR   PhosphoSite; P56480; -.
DR   SWISS-2DPAGE; P56480; -.
DR   COMPLUYEAST-2DPAGE; P56480; -.
DR   REPRODUCTION-2DPAGE; IPI00468481; -.
DR   REPRODUCTION-2DPAGE; P56480; -.
DR   UCD-2DPAGE; P56480; -.
DR   PRIDE; P56480; -.
DR   Ensembl; ENSMUST00000026459; ENSMUSP00000026459; ENSMUSG00000025393.
DR   GeneID; 11947; -.
DR   KEGG; mmu:11947; -.
DR   NMPDR; fig|10090.3.peg.23008; -.
DR   UCSC; uc007hle.1; mouse.
DR   CTD; 11947; -.
DR   MGI; MGI:107801; Atp5b.
DR   eggNOG; roNOG07745; -.
DR   GeneTree; ENSGT00550000074800; -.
DR   HOVERGEN; HBG004307; -.
DR   InParanoid; P56480; -.
DR   OMA; IGQEHYD; -.
DR   OrthoDB; EOG4ZCT4C; -.
DR   PhylomeDB; P56480; -.
DR   BRENDA; 3.6.3.14; 244.
DR   NextBio; 280061; -.
DR   ArrayExpress; P56480; -.
DR   Bgee; P56480; -.
DR   Genevestigator; P56480; -.
DR   GermOnline; ENSMUSG00000025393; Mus musculus.
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:0008553; F:hydrogen-exporting ATPase activity, phosphorylative mechanism; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
DR   GO; GO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; IMP:MGI.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR000194; ATPase_a/bsu_nucl-bd.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR005722; ATPase_F1-cplx_bsu.
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   PANTHER; PTHR15184:SF8; ATPase_F1_b; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF00306; ATP-synt_ab_C; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF47917; ATPase_a/b_C; 1.
DR   SUPFAM; SSF50615; ATPase_a/b_N; 1.
DR   TIGRFAMs; TIGR01039; atpD; 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; Hydrolase;
KW   Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Nucleotide-binding; Phosphoprotein; Transit peptide; Transport.
FT   TRANSIT       1     46       Mitochondrion (By similarity).
FT   CHAIN        47    529       ATP synthase subunit beta, mitochondrial.
FT                                /FTId=PRO_0000002444.
FT   NP_BIND     206    213       ATP (By similarity).
FT   MOD_RES     133    133       N6-acetyllysine.
FT   MOD_RES     198    198       N6-acetyllysine (By similarity).
FT   MOD_RES     259    259       N6-acetyllysine.
FT   MOD_RES     426    426       N6-acetyllysine (By similarity).
FT   MOD_RES     485    485       N6-acetyllysine (By similarity).
FT   MOD_RES     522    522       N6-acetyllysine.
FT   MOD_RES     529    529       Phosphoserine.
FT   CONFLICT     25     25       A -> V (in Ref. 1; AAB86421).
FT   CONFLICT     43     43       A -> V (in Ref. 2; BAE35088).
FT   CONFLICT     76     76       D -> G (in Ref. 2; BAE40961).
FT   CONFLICT     92     92       D -> E (in Ref. 1; AAB86421).
FT   CONFLICT    134    134       I -> V (in Ref. 2; BAE31497).
FT   CONFLICT    239    239       R -> K (in Ref. 1; AAB86421).
FT   CONFLICT    271    271       Q -> R (in Ref. 2; BAE38888/BAE39301).
FT   CONFLICT    279    280       RA -> PT (in Ref. 1; AAB86421).
FT   CONFLICT    288    288       T -> A (in Ref. 2; BAE31497/BAE31630).
FT   CONFLICT    375    375       T -> N (in Ref. 2; BAE30095).
FT   CONFLICT    383    383       T -> S (in Ref. 2; BAB22802).
FT   CONFLICT    433    434       SL -> FF (in Ref. 1; AAB86421).
FT   CONFLICT    466    466       Q -> H (in Ref. 2; BAB22802).
FT   CONFLICT    469    469       Q -> R (in Ref. 2; BAE39797).
FT   CONFLICT    518    518       A -> V (in Ref. 2; BAE35331).
SQ   SEQUENCE   529 AA;  56300 MW;  F3E1100C390A78A7 CRC64;
     MLSLVGRVAS ASASGALRGL SPSAALPQAQ LLLRAAPAGV HPARDYAAQA SAAPKAGTAT
     GRIVAVIGAV VDVQFDEGLP PILNALEVQG RDSRLVLEVA QHLGESTVRT IAMDGTEGLV
     RGQKVLDSGA PIKIPVGPET LGRIMNVIGE PIDERGPIKT KQFAPIHAEA PEFIEMSVEQ
     EILVTGIKVV DLLAPYAKGG KIGLFGGAGV GKTVLIMELI NNVAKAHGGY SVFAGVGERT
     REGNDLYHEM IESGVINLKD ATSKVALVYG QMNEPPGARA RVALTGLTVA EYFRDQEGQD
     VLLFIDNIFR FTQAGSEVSA LLGRIPSAVG YQPTLATDMG TMQERITTTK KGSITSVQAI
     YVPADDLTDP APATTFAHLD ATTVLSRAIA ELGIYPAVDP LDSTSRIMDP NIVGNEHYDV
     ARGVQKILQD YKSLQDIIAI LGMDELSEED KLTVSRARKI QRFLSQPFQV AEVFTGHMGK
     LVPLKETIKG FQQILAGEYD HLPEQAFYMV GPIEEAVAKA DKLAEEHGS
//
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.
CC   -----------------------------------------------------------------------
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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;
CC   -----------------------------------------------------------------------
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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   GMEB2_MOUSE             Reviewed;         530 AA.
AC   P58929; Q6PCY0;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 2.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Glucocorticoid modulatory element-binding protein 2;
DE            Short=GMEB-2;
GN   Name=Gmeb2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; 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).
CC   -!- FUNCTION: Trans-acting factor that binds to glucocorticoid
CC       modulatory elements (GME) present in the TAT (tyrosine
CC       aminotransferase) promoter and increases sensitivity to low
CC       concentrations of glucocorticoids. Binds also to the transferrin
CC       receptor promoter (By similarity).
CC   -!- SUBUNIT: Homodimer, and heterodimer of GMEB1 and GMEB2. Interacts
CC       with the glucocorticoid receptor (NR3C1). May interact with CREB-
CC       binding protein (CBP) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity). Note=May be also cytoplasmic (By similarity).
CC   -!- SIMILARITY: Contains 1 SAND domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC029763; AAH29763.1; -; mRNA.
DR   EMBL; BC059066; AAH59066.1; -; mRNA.
DR   IPI; IPI00118393; -.
DR   RefSeq; NP_937812.1; NM_198169.2.
DR   UniGene; Mm.220423; -.
DR   ProteinModelPortal; P58929; -.
DR   SMR; P58929; 87-176.
DR   STRING; P58929; -.
DR   PhosphoSite; P58929; -.
DR   PRIDE; P58929; -.
DR   Ensembl; ENSMUST00000049032; ENSMUSP00000037075; ENSMUSG00000038705.
DR   GeneID; 229004; -.
DR   KEGG; mmu:229004; -.
DR   UCSC; uc008olr.1; mouse.
DR   CTD; 229004; -.
DR   MGI; MGI:2652836; Gmeb2.
DR   HOGENOM; HBG445559; -.
DR   HOVERGEN; HBG051742; -.
DR   InParanoid; P58929; -.
DR   OMA; ALEQQCD; -.
DR   OrthoDB; EOG45B1FC; -.
DR   PhylomeDB; P58929; -.
DR   NextBio; 379305; -.
DR   ArrayExpress; P58929; -.
DR   Bgee; P58929; -.
DR   Genevestigator; P58929; -.
DR   GermOnline; ENSMUSG00000038705; Mus musculus.
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: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   InterPro; IPR000770; SAND_dom.
DR   InterPro; IPR010919; SAND_dom-like.
DR   Gene3D; G3DSA:3.10.390.10; SAND; 1.
DR   Pfam; PF01342; SAND; 1.
DR   SMART; SM00258; SAND; 1.
DR   SUPFAM; SSF63763; SAND_like; 1.
DR   PROSITE; PS50864; SAND; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Transcription; Transcription regulation; Zinc.
FT   CHAIN         1    530       Glucocorticoid modulatory element-binding
FT                                protein 2.
FT                                /FTId=PRO_0000074093.
FT   DOMAIN       81    163       SAND.
FT   COILED      245    270       Potential.
FT   COILED      304    344       Potential.
FT   COMPBIAS     13     16       Poly-Val.
FT   COMPBIAS     57     64       Poly-Ala.
FT   METAL       110    110       Zinc (By similarity).
FT   METAL       167    167       Zinc (By similarity).
FT   METAL       171    171       Zinc (By similarity).
FT   METAL       175    175       Zinc (By similarity).
FT   BINDING     136    136       DNA (By similarity).
FT   BINDING     140    140       DNA (By similarity).
FT   BINDING     143    143       DNA (By similarity).
FT   BINDING     154    154       DNA (By similarity).
FT   MOD_RES     373    373       Phosphoserine (By similarity).
SQ   SEQUENCE   530 AA;  56631 MW;  9CFF4660A1CB97ED CRC64;
     MATPDVSVHM EEVVVVTTPD TAVDGSGVEE VKTVLVTTNL APHGGDLTED NMETENAAAA
     AAAAFTASSQ LKEAVLVKMA EEGENLEAEI VYPITCGDSR ANLIWRKFVC PGINVKCVQY
     DEHVISPKEF VHLAGKSTLK DWKRAIRMNG IMLRKIMDSG ELDFYQHDKV CSNTCRSTKI
     DLSGARVSLS SPTSTEYIPL TPAAADVNGS PATITIETCE DPGDWTTTIG DDTFAFWRGL
     KDAGLLDEVI QEFQQELEET MKGLQQRVQD PPLQLRDAVL LNNIVQNFGM LDLVKKVLAS
     HKCQMDRSRE QYARDLAALE QQCDEHRRRA KELKHKSQHL SNVLMTLTPV PLPSPMKRPR
     LARATSGPAA MASQVLTQSA QIALSPGMPV SQLTSVPLGK VVSTLPSTVL GKGSPQAAPA
     SSPASPLLGG YTVLASSGST FPNAVEIHPD TSSLTVLSTA AMQDGSTVLK VVSPLQLLTL
     PGLGPTLQNV AQASPAGSTI VTMPTATATG PEEHTATIEV AAVAEDHEQK
//
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   MKL2_MOUSE              Reviewed;        1080 AA.
AC   P59759;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2003, sequence version 1.
DT   08-FEB-2011, entry version 67.
DE   RecName: Full=MKL/myocardin-like protein 2;
DE   AltName: Full=Myocardin-related transcription factor B;
DE            Short=MRTF-B;
GN   Name=Mkl2; Synonyms=Mrtfb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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 INTERACTION WITH SRF.
RC   STRAIN=C57BL/6; TISSUE=Embryo;
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   [2]
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   [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).
CC   -!- FUNCTION: Acts as a transcriptional coactivator of serum response
CC       factor (SRF). Required for skeletal myogenic differentiation.
CC   -!- SUBUNIT: Interacts with MKL1 and SRF.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed. High expression in heart,
CC       brain and testis. Lower expression in lung, liver and kidney.
CC   -!- DEVELOPMENTAL STAGE: Detected throughout the embryo at 10.5 dpc.
CC       High expression in epithelial cells of the lung, kidney, bladder,
CC       colon, testis, in the smooth muscle of the colon and small
CC       intestines, and in the mesenchymal cells adjacent to the olfactory
CC       epithelium at 15.5 dpc.
CC   -!- DOMAIN: The N-terminal region is required for nuclear localization
CC       and the C-terminal region mediates transcriptional activity (By
CC       similarity).
CC   -!- PTM: O-glycosylated.
CC   -!- SIMILARITY: Contains 3 RPEL repeats.
CC   -!- SIMILARITY: Contains 1 SAP domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AF532598; AAN33042.1; -; mRNA.
DR   IPI; IPI00858150; -.
DR   RefSeq; NP_705816.2; NM_153588.3.
DR   UniGene; Mm.270643; -.
DR   ProteinModelPortal; P59759; -.
DR   SMR; P59759; 38-65, 79-108, 375-427.
DR   STRING; P59759; -.
DR   PhosphoSite; P59759; -.
DR   PRIDE; P59759; -.
DR   Ensembl; ENSMUST00000009713; ENSMUSP00000009713; ENSMUSG00000009569.
DR   GeneID; 239719; -.
DR   KEGG; mmu:239719; -.
DR   UCSC; uc007yga.1; mouse.
DR   CTD; 239719; -.
DR   MGI; MGI:3050795; Mkl2.
DR   GeneTree; ENSGT00530000063195; -.
DR   HOGENOM; HBG443837; -.
DR   HOVERGEN; HBG036493; -.
DR   InParanoid; P59759; -.
DR   NextBio; 384249; -.
DR   ArrayExpress; P59759; -.
DR   Bgee; P59759; -.
DR   CleanEx; MM_MKL2; -.
DR   Genevestigator; P59759; -.
DR   GermOnline; ENSMUSG00000009569; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR   GO; GO:0003779; F:actin binding; IDA:MGI.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR   GO; GO:0048514; P:blood vessel morphogenesis; IMP:MGI.
DR   GO; GO:0048738; P:cardiac muscle tissue development; IMP:MGI.
DR   GO; GO:0048568; P:embryonic organ development; 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:0001889; P:liver development; IMP:MGI.
DR   GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR   GO; GO:0045844; P:positive regulation of striated muscle tissue development; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0051145; P:smooth muscle cell differentiation; IMP: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   Activator; Coiled coil; Developmental protein; Differentiation;
KW   Glycoprotein; Myogenesis; Nucleus; Phosphoprotein; Repeat;
KW   Transcription; Transcription regulation.
FT   CHAIN         1   1080       MKL/myocardin-like protein 2.
FT                                /FTId=PRO_0000126629.
FT   REPEAT       40     65       RPEL 1.
FT   REPEAT       84    109       RPEL 2.
FT   REPEAT      128    153       RPEL 3.
FT   DOMAIN      383    417       SAP.
FT   REGION      557    585       Required for interaction with itself and
FT                                with MKL1 (By similarity).
FT   COILED      539    594       Potential.
FT   COMPBIAS    320    346       Gln-rich.
FT   COMPBIAS    665    806       Gln-rich.
FT   MOD_RES      66     66       Phosphoserine.
FT   MOD_RES     913    913       Phosphoserine (By similarity).
SQ   SEQUENCE   1080 AA;  117547 MW;  1781D8EF34517DAC CRC64;
     MIDSSKKQPQ GFPEILTAED FEPFKEKECL EGSNQKSLKE VLQLRLQQRR TREQLVDQGI
     MPPLKSPAAF HEQIKSLERA RTENFLKHKI RSRPDRSELV RMHILEETFA EPSLQATQMK
     LKRARLADDL NEKIAQRPGP MELVEKNILP VDSSVKEAII GVVKEDYPHT HGEFSFDEDS
     SDALSPDQPA SQESQGSAAS PSEPKVSASP PPVTASTPAQ FTSVSPAVPE FLKTPLTADQ
     PPTRSTAPVL PTNTVSSAKS GPMLVKQSHP KNPNDKHRSK KCKDPKPRVK KLKYHQYIPP
     NQKGEKSEPQ MDSNYARLLQ QQQLFLQLQI LSQQQQQQQQ QHYNYQTILP APIKTDKNSS
     SGSNSGSSSS MPARRPGPLP SSLDDLKVSE LKTELKLRGL PVSGTKPDLI ERLKPYQEVT
     SSNLATGSIV AVSSATIVTS NPEVTVALPV TTLHNAVTSS VSTFKADLAL PATSSVPHVE
     NAHSPLPISP SPSEQSSLST DDTNMTDTFT EIMTMMSPSQ LLCSSPLRVV SHDDSLSPSS
     STLSTLELDA AEKDRKLQEK EKQIEELKRK LEQEQKLVEV LKMQLEVEKR GQQRPPDPQP
     SDPPHPFNTS DPKHGSVGSS IKDEASLPDC SSPQQPITVP GHSVGQPIST GSQTLVAKKT
     VVVKQEVPMA QAEQQNVVSQ FYLSSQGQPP ALVAQPQALL TTQTTQLLLP VSIQGSNVTS
     VQLPVGSLQL QTPAQGRVQA QPHVAAATQV PAAALPSALT SALPQKQEAF PQHVLGQPQP
     VRKVFTNSAP NTVLQYQRQP GPTNQQPFVS KTSNPALQSR TAPLAPLQNG PSLASKPSSP
     PPPQQFVVQH SLFATPITKT KDPPRYEEAI KQTRSTQPAL PEVSSVHSQQ MDDLFDILIK
     SGEISFPIKE EPSPISKMKP VTASITTMPV NTVVSRPPPQ VQIAPPVSLE PVNSLSASLE
     NQLEAFLDGT LPSATDTGPL QNSSEDRESF SLIEDLQNDL LSHSSMLYQS HSPMETSEAQ
     LVSGTPCLSL DLSDSNLDNM EWLDITMPTT SSGLTPLSTT APSMFSADFL DPQDLPLPWD
//
ID   DOCK4_MOUSE             Reviewed;        1978 AA.
AC   P59764;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   03-JUL-2003, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Dedicator of cytokinesis protein 4;
GN   Name=Dock4; Synonyms=Kiaa0716;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; 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   DISEASE.
RX   MEDLINE=22515525; PubMed=12628187; DOI=10.1016/S0092-8674(03)00155-7;
RA   Yajnik V., Paulding C., Sordella R., McClatchey A.I., Saito M.,
RA   Wahrer D.C.R., Reynolds P., Bell D.W., Lake R., van den Heuvel S.,
RA   Settleman J., Haber D.A.;
RT   "DOCK4, a GTPase activator, is disrupted during tumorigenesis.";
RL   Cell 112:673-684(2003).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-167, 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-1629, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
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 regulation of adherens junction between
CC       cells. Functions as a guanine nucleotide exchange factor (GEF),
CC       which activates Rap1 small GTPase by exchanging bound GDP for free
CC       GTP (By similarity).
CC   -!- SUBUNIT: Interacts with the SH3 domain of CRK. Interacts with
CC       nucleotide-free Rap1. Interacts with FASLG (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane
CC       protein (By similarity).
CC   -!- DOMAIN: The DHR-2 domain probably mediates the GEF activity (By
CC       similarity).
CC   -!- DISEASE: Note=Defects in Dock4 are involved in the cause of some
CC       cancers, which are probably due to lack of Rap1 activation.
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; AK122353; BAC65635.1; -; mRNA.
DR   IPI; IPI00223070; -.
DR   RefSeq; NP_766391.2; NM_172803.2.
DR   UniGene; Mm.341423; -.
DR   ProteinModelPortal; P59764; -.
DR   SMR; P59764; 1-165, 401-576.
DR   STRING; P59764; -.
DR   PhosphoSite; P59764; -.
DR   PRIDE; P59764; -.
DR   Ensembl; ENSMUST00000037488; ENSMUSP00000047387; ENSMUSG00000035954.
DR   GeneID; 238130; -.
DR   KEGG; mmu:238130; -.
DR   UCSC; uc007nlh.1; mouse.
DR   CTD; 238130; -.
DR   MGI; MGI:1918006; Dock4.
DR   eggNOG; roNOG05095; -.
DR   HOGENOM; HBG356771; -.
DR   HOVERGEN; HBG051389; -.
DR   InParanoid; P59764; -.
DR   OMA; EKAVNPT; -.
DR   OrthoDB; EOG4K0QMG; -.
DR   NextBio; 383672; -.
DR   ArrayExpress; P59764; -.
DR   Bgee; P59764; -.
DR   CleanEx; MM_DOCK4; -.
DR   Genevestigator; P59764; -.
DR   GermOnline; ENSMUSG00000035954; Mus musculus.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0032420; C:stereocilium; IDA:HGNC.
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; 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   1: Evidence at protein level;
KW   Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW   SH3 domain; SH3-binding.
FT   CHAIN         1   1978       Dedicator of cytokinesis protein 4.
FT                                /FTId=PRO_0000189991.
FT   DOMAIN        6     67       SH3.
FT   DOMAIN      398    629       DHR-1.
FT   DOMAIN     1093   1635       DHR-2.
FT   MOTIF      1797   1803       SH3-binding (Potential).
FT   COMPBIAS   1642   1863       Ser-rich.
FT   COMPBIAS   1875   1960       Pro-rich.
FT   MOD_RES     167    167       Phosphotyrosine.
FT   MOD_RES    1623   1623       Phosphoserine (By similarity).
FT   MOD_RES    1627   1627       Phosphoserine (By similarity).
FT   MOD_RES    1629   1629       Phosphoserine.
FT   MOD_RES    1840   1840       Phosphotyrosine (By similarity).
SQ   SEQUENCE   1978 AA;  226550 MW;  4A1FC9C71C5A5719 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 PNLSAPEKAV NPTPSSWSLD SGKEAKNMSD SGKLISPPVP
     PRPTQTASPA RHTTSVSPSP AGRSPLKGSV QSFTPSPVEY NSPGLSSNSP VLSGSYSSGI
     SSLSRCSTSE TSGFENQANE QSVPVPVPVP VPVPVPSFSG SEEPVRKESK TPPPYSVYER
     TLRRPVPLPH SLSIPVTSEP PALPPKPLAA RSSHLENGTR RTEPGPRPRP LPRKVSQL
//
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
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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   LIPA3_MOUSE             Reviewed;        1043 AA.
AC   P60469;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 1.
DT   08-FEB-2011, entry version 67.
DE   RecName: Full=Liprin-alpha-3;
DE   AltName: Full=Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-3;
DE            Short=PTPRF-interacting protein alpha-3;
GN   Name=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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, 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-494 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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357; SER-494 AND
RP   THR-563, 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-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).
CC   -!- FUNCTION: 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. Binds RIMS1, RIMS2, RIMS3 and RIMS4 (By
CC       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.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; BC058404; AAH58404.1; -; mRNA.
DR   IPI; IPI00399905; -.
DR   RefSeq; NP_084017.2; NM_029741.2.
DR   UniGene; Mm.277235; -.
DR   ProteinModelPortal; P60469; -.
DR   SMR; P60469; 34-117, 681-748, 799-867.
DR   PhosphoSite; P60469; -.
DR   PRIDE; P60469; -.
DR   Ensembl; ENSMUST00000003961; ENSMUSP00000003961; ENSMUSG00000003863.
DR   GeneID; 76787; -.
DR   KEGG; mmu:76787; -.
DR   UCSC; uc009gut.1; mouse.
DR   CTD; 76787; -.
DR   MGI; MGI:1924037; Ppfia3.
DR   eggNOG; roNOG06814; -.
DR   GeneTree; ENSGT00550000074230; -.
DR   HOVERGEN; HBG052330; -.
DR   PhylomeDB; P60469; -.
DR   NextBio; 345807; -.
DR   ArrayExpress; P60469; -.
DR   Bgee; P60469; -.
DR   Genevestigator; P60469; -.
DR   GermOnline; ENSMUSG00000003863; Mus musculus.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Phosphoprotein; Repeat.
FT   CHAIN         1   1043       Liprin-alpha-3.
FT                                /FTId=PRO_0000191030.
FT   DOMAIN      687    753       SAM 1.
FT   DOMAIN      802    866       SAM 2.
FT   DOMAIN      890    959       SAM 3.
FT   COILED       26    133       Potential.
FT   COILED      171    350       Potential.
FT   COILED      445    493       Potential.
FT   COILED      863    889       Potential.
FT   MOD_RES      17     17       Phosphoserine.
FT   MOD_RES     357    357       Phosphoserine.
FT   MOD_RES     494    494       Phosphoserine.
FT   MOD_RES     532    532       Phosphoserine.
FT   MOD_RES     563    563       Phosphothreonine.
FT   MOD_RES     567    567       Phosphothreonine (By similarity).
FT   MOD_RES    1013   1013       Phosphoserine (By similarity).
SQ   SEQUENCE   1043 AA;  116280 MW;  226331BC61954E31 CRC64;
     MMCEVMPTIS EDGRRGSALG PDEAGGELER LMVTMLTERE RLLETLREAQ DGLATAQLRL
     RELGHEKDSL QRQLSIALPQ EFAALTKELN LCREQLLERE EEIAELKAER NNTRLLLEHL
     ECLVSRHERS LRMTVVKRQA QSPGGVSSEV EVLKALKSLF EHHKALDEKV RERLRMALEN
     ELASKESLYR QSEEKSRQLA EWLDDAKQKL QQTLQKAETL PEIEAQLAQR VAALNKAEER
     HGNFEERLRQ LEAQLEEKNQ ELQRARQREK MNDDHNKRLS ETVDKLLSES NERLQLHLKE
     RMGALEEKNS LSEEIANMKK LQDELLLNKE QLLAEMERMQ MEIDQLRGRP PSSYSRSLPG
     SALELRYSQA PTLPSGAPLD PYGAGSGRAG KRGRWSGAKD ESSKDWDRSA PAGSIPPPFP
     GELDGSDEEE AEGMFGAELL SPSGQADVQT LAIMLQEQLE AINKEIKLIQ EEKETTEQRA
     EELESRVSSS GLDSLGRYRS SCSLPPSLTT STLASPSPPS SGHSTPRLAP PSPAREGTDK
     TNHVSKEEAG VPRGEGPAVP GDTPPPTPRS ARLERMAQAL ALQAGSPEDG APPRGSESTP
     DSLHKAPKRK SIKSSIGRLF GKKEKGRMGP PGRESVSLAG TPSDETLATD PLGLAKLTGP
     GDKDRRNKRK HELLEEACRQ GLPFAAWDGP TVVSWLELWV GMPAWYVAAC RANVKSGAIM
     ANLSDTEIQR EIGISNPLHR LKLRLAIQEM VSLTSPSAPA SSRTPTGNVW MTHEEMESLT
     AATKPETKEI SWEQILAYGD MNHEWVGNDW LPSLGLPQYR SYFMESLVDA RMLDHLNKKE
     LRGQLKMVDS FHRVSLHYGI MCLKRLNYDR KDLERRREES QTQIRDVMVW SNERVMGWVS
     GLGLKEFATN LTESGVHGAL LALDETFDYS DLALLLQIPT QNAQARQLLE KEFSNLISLG
     TDRRLDEDSA KSFSRSPSWR KMFREKDLRG VTPDSAEMLP PNFRSAAAGA LGSPGLPLRK
     LQPEGQTSGS SRADGVSVRT YSC
//
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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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   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   CAH10_MOUSE             Reviewed;         328 AA.
AC   P61215;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Carbonic anhydrase-related protein 10;
DE   AltName: Full=Carbonic anhydrase-related protein X;
DE            Short=CA-RP X;
DE            Short=CARP X;
GN   Name=Ca10; Synonyms=Car10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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   Taniuchi K., Nishimori I.;
RT   "Divelopmental expression of murine carbonic anhydrase-related protein
RT   VIII, X, and XI.";
RL   Submitted (MAR-2002) 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).
CC   -!- FUNCTION: Does not have a catalytic activity.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
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DR   EMBL; AB080741; BAC11853.1; -; mRNA.
DR   EMBL; BC017606; AAH17606.1; -; mRNA.
DR   IPI; IPI00411133; -.
DR   RefSeq; NP_082572.1; NM_028296.3.
DR   UniGene; Mm.342160; -.
DR   ProteinModelPortal; P61215; -.
DR   SMR; P61215; 29-303.
DR   STRING; P61215; -.
DR   PhosphoSite; P61215; -.
DR   PRIDE; P61215; -.
DR   Ensembl; ENSMUST00000042943; ENSMUSP00000035585; ENSMUSG00000056158.
DR   Ensembl; ENSMUST00000107863; ENSMUSP00000103495; ENSMUSG00000056158.
DR   GeneID; 72605; -.
DR   KEGG; mmu:72605; -.
DR   UCSC; uc007kxi.1; mouse.
DR   CTD; 72605; -.
DR   MGI; MGI:1919855; Car10.
DR   eggNOG; roNOG08799; -.
DR   HOGENOM; HBG717384; -.
DR   HOVERGEN; HBG097666; -.
DR   InParanoid; P61215; -.
DR   OMA; QVSGTMY; -.
DR   PhylomeDB; P61215; -.
DR   NextBio; 336579; -.
DR   ArrayExpress; P61215; -.
DR   Bgee; P61215; -.
DR   CleanEx; MM_CAR10; -.
DR   Genevestigator; P61215; -.
DR   GermOnline; ENSMUSG00000056158; Mus musculus.
DR   InterPro; IPR018423; Carbonic_anhydrase-RP_CA10.
DR   InterPro; IPR001148; Carbonic_anhydrase_a-class_cat.
DR   Gene3D; G3DSA:3.10.200.10; Euk_COanhd; 1.
DR   PANTHER; PTHR18952:SF11; Carbonic_anhydrase-RP_CA10; 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   2: Evidence at transcript level;
KW   Phosphoprotein.
FT   CHAIN         1    328       Carbonic anhydrase-related protein 10.
FT                                /FTId=PRO_0000077438.
FT   MOD_RES     299    299       Phosphothreonine (By similarity).
SQ   SEQUENCE   328 AA;  37563 MW;  B20BFEC1800422B4 CRC64;
     MEIVWEVLFL LQANFIVCIS AQQNSPKIHE GWWAYKEVVQ GSFVPVPSFW GLVNSAWNLC
     SVGKRQSPVN IETSHMIFDP FLTPLRINTG GRKVSGTMYN TGRHVSLRLD KEHLVNISGG
     PMTYSHRLEE IRLHFGSEDS QGSEHLLNGQ AFSGEVQLIH YNHELYTNVT EAAKSPNGLV
     VVSIFIKVSD SSNPFLNRML NRDTITRITY KNDAYLLQGL NIEELYPETS SFITYDGSMT
     IPPCYETASW IIMNKPVYIT RMQMHSLRLL SQNQPSQIFL SMSDNFRPVQ PLNNRCIRTN
     INFSLQGKDC PNNRAQKLQY RVNEWLLK
//
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
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   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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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   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   -----------------------------------------------------------------------
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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   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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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.
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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   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   EBP_MOUSE               Reviewed;         230 AA.
AC   P70245; Q9CSP4;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase;
DE            EC=5.3.3.5;
DE   AltName: Full=Cholestenol Delta-isomerase;
DE   AltName: Full=Delta(8)-Delta(7) sterol isomerase;
DE            Short=D8-D7 sterol isomerase;
DE   AltName: Full=Emopamil-binding protein;
GN   Name=Ebp; Synonyms=Msi;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=96394301; PubMed=8798407; DOI=10.1074/jbc.271.37.22434;
RA   Silve S., Dupuy P.H., Labit-Lebouteiller C., Kaghad M., Chalon P.,
RA   Rahier A., Taton M., Lupker J., Shire D., Loison G.;
RT   "Emopamil-binding protein, a mammalian protein that binds a series of
RT   structurally diverse neuroprotective agents, exhibits delta8-delta7
RT   sterol isomerase activity in yeast.";
RL   J. Biol. Chem. 271:22434-22440(1996).
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=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and 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 2-14; 53-62 AND 210-221, CLEAVAGE OF INITIATOR
RP   METHIONINE, ACETYLATION AT THR-2, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Liver;
RA   Kanor S., Bienvenut W.V.;
RL   Submitted (OCT-2005) to UniProtKB.
RN   [5]
RP   VARIANT TD ARG-107.
RX   MEDLINE=99318102; PubMed=10391218; DOI=10.1038/10350;
RA   Derry J.M.J., Gormally E., Means G.D., Zhao W., Meindl A.,
RA   Kelley R.I., Boyd Y., Herman G.E.;
RT   "Mutations in a delta(8)-delta(7) sterol isomerase in the tattered
RT   mouse and X-linked dominant chondrodysplasia punctata.";
RL   Nat. Genet. 22:286-290(1999).
CC   -!- FUNCTION: Catalyzes the conversion of Delta(8)-sterols to their
CC       corresponding Delta(7)-isomers.
CC   -!- CATALYTIC ACTIVITY: 5-alpha-cholest-7-en-3-beta-ol = 5-alpha-
CC       cholest-8-en-3-beta-ol.
CC   -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
CC   -!- DISEASE: Note=Defects in Ebp are a cause of 'Tattered' (Td) which
CC       is an X-linked, semidominant mouse mutation associated with
CC       prenatal male lethality. Heterozygous females are small and at 4
CC       to 5 days of age develop patches of hyperkeratotic skin where no
CC       hair grows, resulting in a striping of the coat in adults.
CC       Craniofacial anomalies and twisted toes have also been observed in
CC       some affected females.
CC   -!- MISCELLANEOUS: Binds to the phenylalkylamine calcium-ion
CC       antagonist emopamil, an anti-ischemic drug.
CC   -!- SIMILARITY: Belongs to the EBP family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X97755; CAA66350.1; -; mRNA.
DR   EMBL; AK012266; BAB28129.1; -; mRNA.
DR   EMBL; AK027977; BAC25686.1; -; mRNA.
DR   EMBL; BC004703; AAH04703.1; -; mRNA.
DR   EMBL; BC004620; AAH04620.1; -; mRNA.
DR   IPI; IPI00137471; -.
DR   RefSeq; NP_031924.1; NM_007898.2.
DR   UniGene; Mm.27183; -.
DR   STRING; P70245; -.
DR   PhosphoSite; P70245; -.
DR   PRIDE; P70245; -.
DR   Ensembl; ENSMUST00000033509; ENSMUSP00000033509; ENSMUSG00000031168.
DR   GeneID; 13595; -.
DR   KEGG; mmu:13595; -.
DR   UCSC; uc009soi.1; mouse.
DR   CTD; 13595; -.
DR   MGI; MGI:107822; Ebp.
DR   GeneTree; ENSGT00530000063715; -.
DR   HOGENOM; HBG590959; -.
DR   HOVERGEN; HBG018176; -.
DR   InParanoid; P70245; -.
DR   OMA; PTWHILA; -.
DR   OrthoDB; EOG45490D; -.
DR   PhylomeDB; P70245; -.
DR   BRENDA; 5.3.3.5; 244.
DR   NextBio; 284216; -.
DR   ArrayExpress; P70245; -.
DR   Bgee; P70245; -.
DR   Genevestigator; P70245; -.
DR   GermOnline; ENSMUSG00000031168; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000247; F:C-8 sterol isomerase activity; IDA:MGI.
DR   GO; GO:0047750; F:cholestenol delta-isomerase activity; IEA:EC.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR   InterPro; IPR007905; EBP.
DR   PANTHER; PTHR14207; EBP; 1.
DR   Pfam; PF05241; EBP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cholesterol biosynthesis; Direct protein sequencing;
KW   Disease mutation; Endoplasmic reticulum; Isomerase; Lipid synthesis;
KW   Membrane; Steroid biosynthesis; Sterol biosynthesis; Transmembrane;
KW   Transmembrane helix.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    230       3-beta-hydroxysteroid-Delta(8),Delta(7)-
FT                                isomerase.
FT                                /FTId=PRO_0000174343.
FT   TRANSMEM     29     49       Helical; (Potential).
FT   TRANSMEM     66     86       Helical; (Potential).
FT   TRANSMEM    121    141       Helical; (Potential).
FT   TRANSMEM    185    205       Helical; (Potential).
FT   MOD_RES       2      2       N-acetylthreonine.
FT   VARIANT     107    107       G -> R (in Td).
SQ   SEQUENCE   230 AA;  26215 MW;  26752EEE59F098A7 CRC64;
     MTTNTVPLHP YWPRHLKLDN FVPNDLPTSH ILVGLFSISG GLIVITWLLS SRASVVPLGA
     GRRLALCWFA VCTFIHLVIE GWFSLYNGIL LEDQAFLSQL WKEYSKGDSR YILSDSFVVC
     METVTACLWG PLSLWVVIAF LRQQPFRFVL QLVVSMGQIY GDVLYFLTEL HEGLQHGEIG
     HPVYFWFYFV FLNAVWLVIP SILVLDAIKH LTSAQSVLDS KVMKIKSKHN
//
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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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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   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   NUCB2_MOUSE             Reviewed;         420 AA.
AC   P81117;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2001, sequence version 2.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Nucleobindin-2;
DE   AltName: Full=DNA-binding protein NEFA;
DE   Flags: Precursor;
GN   Name=Nucb2; Synonyms=Nefa;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=20493539; PubMed=10915798; DOI=10.1074/jbc.M005103200;
RA   Taniguchi N., Taniura H., Niinobe M., Takayama C.,
RA   Tominaga-Yoshino K., Ogura A., Yoshikawa K.;
RT   "The postmitotic growth suppressor necdin interacts with a calcium-
RT   binding protein (NEFA) in neuronal cytoplasm.";
RL   J. Biol. Chem. 275:31674-31681(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster / NIH; TISSUE=Embryo;
RA   Hoefig K., Barnikol-Watanabe S., Barnikol H.U., Hilschmann N.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
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: Calcium-binding protein. May have a role in calcium
CC       homeostasis.
CC   -!- SUBUNIT: Binds to the postmitotic growth suppressor necdin; co-
CC       expression abolishes Nucb2 secretion.
CC   -!- SUBCELLULAR LOCATION: Perikaryon. Endoplasmic reticulum. Nucleus
CC       envelope. Note=In dendrites and perikarya of brain neurons.
CC       Abundant in the ER cisternae and nuclear envelope, but not
CC       detected in Golgi, mitochondria or nucleoplasm. In cell culture,
CC       cytoplasmic and secreted.
CC   -!- TISSUE SPECIFICITY: Found in liver, heart, thymus, muscle,
CC       intestine, kidney, lung, spleen and throughout the brain, in
CC       cerebral cortex, hippocampus, hypothalamus and medulla oblongata.
CC       Nucb2 and necdin levels were higher in postmitotic neurons.
CC   -!- SIMILARITY: Belongs to the nucleobindin 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; AJ222586; CAA10858.1; -; mRNA.
DR   EMBL; BC010459; AAH10459.1; -; mRNA.
DR   IPI; IPI00309704; -.
DR   RefSeq; NP_001123951.1; NM_001130479.1.
DR   UniGene; Mm.9901; -.
DR   ProteinModelPortal; P81117; -.
DR   SMR; P81117; 229-327.
DR   STRING; P81117; -.
DR   PhosphoSite; P81117; -.
DR   PRIDE; P81117; -.
DR   Ensembl; ENSMUST00000032895; ENSMUSP00000032895; ENSMUSG00000030659.
DR   GeneID; 53322; -.
DR   KEGG; mmu:53322; -.
DR   UCSC; uc009jjk.1; mouse.
DR   CTD; 53322; -.
DR   MGI; MGI:1858179; Nucb2.
DR   eggNOG; roNOG09966; -.
DR   HOGENOM; HBG713576; -.
DR   HOVERGEN; HBG052685; -.
DR   InParanoid; P81117; -.
DR   OMA; DQHFREK; -.
DR   OrthoDB; EOG4N04F6; -.
DR   PhylomeDB; P81117; -.
DR   ArrayExpress; P81117; -.
DR   Bgee; P81117; -.
DR   CleanEx; MM_NUCB2; -.
DR   Genevestigator; P81117; -.
DR   GermOnline; ENSMUSG00000030659; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0005640; C:nuclear outer membrane; IDA:MGI.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; TAS: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; 1.
DR   SMART; SM00054; EFh; 2.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   1: Evidence at protein level;
KW   Calcium; DNA-binding; Endoplasmic reticulum; Nucleus; Repeat; Signal.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25    420       Nucleobindin-2.
FT                                /FTId=PRO_0000004166.
FT   DOMAIN      241    276       EF-hand 1.
FT   DOMAIN      293    328       EF-hand 2.
FT   DNA_BIND    171    223       By similarity.
FT   CA_BIND     254    265       1.
FT   CA_BIND     306    317       2.
FT   REGION      213    420       Binds to necdin.
FT   COMPBIAS    284    293       Asp/Glu-rich (acidic).
FT   CONFLICT     18     18       M -> T (in Ref. 2; CAA10858).
SQ   SEQUENCE   420 AA;  50304 MW;  0DEBD51724CB7E72 CRC64;
     MRWRIIQVQY CFLLVPCMLT ALEAVPIDVD KTKVHNTEPV ENARIEPPDT GLYYDEYLKQ
     VIEVLETDPH FREKLQKADI EEIRSGRLSQ ELDLVSHKVR TRLDELKRQE VGRLRMLIKA
     KLDALQDTGM NHHLLLKQFE HLNHQNPNTF ESRDLDMLIK AATADLEQYD RTRHEEFKKY
     EMMKEHERRE YLKTLSEEKR KEEESKFEEM KRKHEDHPKV NHPGSKDQLK EVWEETDGLD
     PNDFDPKTFF KLHDVNNDGF LDEQELEALF TRELEKVYNP QNAEDDMIEM EEERLRMREH
     VMSEIDNNKD RLVTLEEFLR ATEKKEFLEP DSWETLDQQQ LFTEDELKEY ESIIAIQENE
     LKKRAEELQK QKEDLQRQHD HLEAQKQEYH QAVQHLEQKK LQQGIAPSGP AGELKFEPHT
//
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.
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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   ATF1_MOUSE              Reviewed;         269 AA.
AC   P81269;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Cyclic AMP-dependent transcription factor ATF-1;
DE            Short=cAMP-dependent transcription factor ATF-1;
DE   AltName: Full=Activating transcription factor 1;
DE   AltName: Full=TCR-ATF1;
GN   Name=Atf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=92176656; PubMed=1531847;
RA   Lee M.-R., Chung C.-S., Liou M.-L., Wu M., Li W.-F., Hsueh Y.-P.,
RA   Lai M.-Z.;
RT   "Isolation and characterization of nuclear proteins that bind to T
RT   cell receptor V beta decamer motif.";
RL   J. Immunol. 148:1906-1912(1992).
CC   -!- FUNCTION: Binds the cAMP response element (CRE) (consensus: 5'-
CC       GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular
CC       promoters. Binds to the Tax-responsive element (TRE) of HTLV-I.
CC       Mediates PKA-induced stimulation of CRE-reporter genes (By
CC       similarity).
CC   -!- SUBUNIT: Binds DNA as a dimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily.
CC   -!- SIMILARITY: Contains 1 bZIP domain.
CC   -!- SIMILARITY: Contains 1 KID (kinase-inducible) domain.
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DR   EMBL; M63725; AAA40395.1; -; mRNA.
DR   IPI; IPI00119123; -.
DR   PIR; A46490; A46490.
DR   RefSeq; NP_031523.3; NM_007497.3.
DR   UniGene; Mm.473546; -.
DR   UniGene; Mm.676; -.
DR   ProteinModelPortal; P81269; -.
DR   SMR; P81269; 49-76, 213-267.
DR   STRING; P81269; -.
DR   PhosphoSite; P81269; -.
DR   PRIDE; P81269; -.
DR   Ensembl; ENSMUST00000023769; ENSMUSP00000023769; ENSMUSG00000023027.
DR   GeneID; 11908; -.
DR   KEGG; mmu:11908; -.
DR   UCSC; uc007xqs.1; mouse.
DR   CTD; 11908; -.
DR   MGI; MGI:1298366; Atf1.
DR   eggNOG; roNOG10978; -.
DR   HOGENOM; HBG446032; -.
DR   HOVERGEN; HBG011077; -.
DR   InParanoid; P81269; -.
DR   OMA; EDSHKST; -.
DR   OrthoDB; EOG4TB4C8; -.
DR   PhylomeDB; P81269; -.
DR   NextBio; 460856; -.
DR   ArrayExpress; P81269; -.
DR   Bgee; P81269; -.
DR   CleanEx; MM_ATF1; -.
DR   Genevestigator; P81269; -.
DR   GermOnline; ENSMUSG00000023027; Mus musculus.
DR   GO; GO:0005667; C:transcription factor complex; IDA:MGI.
DR   InterPro; IPR011616; bZIP_1.
DR   InterPro; IPR003102; Coactivator_CBP_pKID.
DR   InterPro; IPR001630; Leuzip_CREB.
DR   InterPro; IPR004827; TF_bZIP.
DR   Pfam; PF00170; bZIP_1; 1.
DR   Pfam; PF02173; pKID; 1.
DR   PRINTS; PR00041; LEUZIPPRCREB.
DR   SMART; SM00338; BRLZ; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
DR   PROSITE; PS50953; KID; 1.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    269       Cyclic AMP-dependent transcription factor
FT                                ATF-1.
FT                                /FTId=PRO_0000076576.
FT   DOMAIN       31     90       KID.
FT   DOMAIN      239    260       Leucine-zipper.
FT   DNA_BIND    214    233       Basic motif.
FT   MOD_RES      63     63       Phosphoserine; by CaMK1 (By similarity).
FT   MOD_RES     196    196       Phosphoserine (By similarity).
SQ   SEQUENCE   269 AA;  29238 MW;  9885265159D64A0C CRC64;
     MEDSHKSNTT ETASQPGSTV AGPHVSQIVH QVSSLSESEE SQDSSDSIGS SQKAHGILAR
     RPSYRKILKD LSSEDTRGRK GEGENPSISA ITSMSVPAPI YQTSSGQYIA IAPNGALQLA
     SPSTDGVQAL QTLTMTNSSS TQQGTILQYA QTSDGQQILV PSNQVVVQTA SGDMQTYQIR
     TTPSATSLPQ TVVMTSPVTL ASQTTKTDDP QLRREIRLMK NREAARECRR KKKEYVKCLE
     NRVAVLENQN KTLIEELKTL KDLYSHKSV
//
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   NPTN_MOUSE              Reviewed;         397 AA.
AC   P97300; Q3U519; Q8C637; Q8C6H8;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 3.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Neuroplastin;
DE   AltName: Full=Stromal cell-derived receptor 1;
DE            Short=SDR-1;
DE   Flags: Precursor;
GN   Name=Nptn; Synonyms=Sdfr1, Sdr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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=97092876; PubMed=8938438; DOI=10.1006/geno.1996.0560;
RA   Shirozu M., Tada H., Tashiro K., Nakamura T., Lopez N.D., Nazarea M.,
RA   Hamada T., Sato T., Nakano T., Honjo T.;
RT   "Characterization of novel secreted and membrane proteins isolated by
RT   the signal sequence trap method.";
RL   Genomics 37:273-280(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC   STRAIN=NOD; TISSUE=Brain, 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/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting 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 150-159 AND 260-271, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RA   Lopez N.D., Kinoshita A., Taniwaki M., Tada H., Shirozu M., Nakano T.,
RA   Tashiro K., Honjo T.;
RT   "Isoform specific expression of the SDR-1 protein, alpha and beta in
RT   subregions of adult rodent brain.";
RL   Biomed. Res. 20:43-49(1999).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-283, 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-186; ASN-196; ASN-199;
RP   ASN-228; ASN-275 AND ASN-283, 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-228; ASN-275 AND ASN-283,
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: Probable homophilic and heterophilic cell adhesion
CC       molecule involved in long term potentiation at hippocampal
CC       excitatory synapses through activation of p38MAPK. May also
CC       regulate neurite outgrowth by activating the FGFR1 signaling
CC       pathway. May play a role in synaptic plasticity (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein (Potential). Note=Enriched at post-synaptic density (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=2; Synonyms=SDR-1beta;
CC         IsoId=P97300-2; Sequence=Displayed;
CC       Name=1; Synonyms=SDR-1alpha;
CC         IsoId=P97300-1; Sequence=VSP_039255;
CC       Name=3;
CC         IsoId=P97300-3; Sequence=VSP_039255, VSP_039257;
CC       Name=4;
CC         IsoId=P97300-4; Sequence=VSP_039254, VSP_039256;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are widely expressed
CC       with variable levels in brain. Isoform 1 is expressed in
CC       cerebellum and midbrain. Isoform 1 and isoform 2 are expressed in
CC       cerebral cortex, hipoccampus and striatum. Isoform 2 is more
CC       abundant in the cerebral cortex than isoform 1.
CC   -!- DOMAIN: Some isoforms lack the first Ig-like domain which may
CC       confer homophilic adhesion activity. However, they can bind and
CC       activate FGFR1 (By similarity).
CC   -!- PTM: N-glycosylated (By similarity).
CC   -!- SIMILARITY: Contains 3 Ig-like (immunoglobulin-like) domains.
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DR   EMBL; D50463; BAA09054.1; -; mRNA.
DR   EMBL; AK075610; BAC35855.1; -; mRNA.
DR   EMBL; AK076624; BAC36420.1; -; mRNA.
DR   EMBL; AK153930; BAE32261.1; -; mRNA.
DR   EMBL; CT030640; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00123831; -.
DR   IPI; IPI00459329; -.
DR   IPI; IPI00662285; -.
DR   IPI; IPI00757771; -.
DR   RefSeq; NP_033171.2; NM_009145.2.
DR   UniGene; Mm.15125; -.
DR   ProteinModelPortal; P97300; -.
DR   SMR; P97300; 27-333.
DR   STRING; P97300; -.
DR   PRIDE; P97300; -.
DR   Ensembl; ENSMUST00000034887; ENSMUSP00000034887; ENSMUSG00000032336.
DR   Ensembl; ENSMUST00000074429; ENSMUSP00000074030; ENSMUSG00000032336.
DR   Ensembl; ENSMUST00000114121; ENSMUSP00000109756; ENSMUSG00000032336.
DR   GeneID; 20320; -.
DR   KEGG; mmu:20320; -.
DR   NMPDR; fig|10090.3.peg.20301; -.
DR   UCSC; uc009pxd.1; mouse.
DR   UCSC; uc009pxe.1; mouse.
DR   UCSC; uc009pxf.1; mouse.
DR   CTD; 20320; -.
DR   MGI; MGI:108077; Nptn.
DR   eggNOG; roNOG10704; -.
DR   GeneTree; ENSGT00390000010516; -.
DR   HOVERGEN; HBG008120; -.
DR   OrthoDB; EOG4W0XD9; -.
DR   NextBio; 298115; -.
DR   ArrayExpress; P97300; -.
DR   Bgee; P97300; -.
DR   CleanEx; MM_NPTN; -.
DR   Genevestigator; P97300; -.
DR   GermOnline; ENSMUSG00000032336; 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:0042734; C:presynaptic membrane; ISS:HGNC.
DR   GO; GO:0050839; F:cell adhesion molecule binding; ISS:HGNC.
DR   GO; GO:0005105; F:type 1 fibroblast growth factor receptor binding; ISS:UniProtKB.
DR   GO; GO:0007204; P:elevation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR   GO; GO:0007156; P:homophilic cell adhesion; ISS:HGNC.
DR   GO; GO:0060291; P:long-term synaptic potentiation; ISS:UniProtKB.
DR   GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; ISS:HGNC.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; 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; IPR003598; Ig_sub2.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3.
DR   Pfam; PF07679; I-set; 2.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 2.
DR   PROSITE; PS50835; IG_LIKE; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cell membrane;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Neurogenesis; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     28       By similarity.
FT   CHAIN        29    397       Neuroplastin.
FT                                /FTId=PRO_0000394471.
FT   TOPO_DOM     29    338       Extracellular (Potential).
FT   TRANSMEM    339    359       Helical; (Potential).
FT   TOPO_DOM    360    397       Cytoplasmic (Potential).
FT   DOMAIN       29    134       Ig-like 1.
FT   DOMAIN      148    234       Ig-like 2.
FT   DOMAIN      237    327       Ig-like 3.
FT   REGION      149    161       Narpin; mediates binding with FGFR1 and
FT                                has antidepressant-like activity (By
FT                                similarity).
FT   CARBOHYD    170    170       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    186    186       N-linked (GlcNAc...).
FT   CARBOHYD    196    196       N-linked (GlcNAc...).
FT   CARBOHYD    199    199       N-linked (GlcNAc...).
FT   CARBOHYD    228    228       N-linked (GlcNAc...).
FT   CARBOHYD    275    275       N-linked (GlcNAc...).
FT   CARBOHYD    283    283       N-linked (GlcNAc...).
FT   CARBOHYD    295    295       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    316    316       N-linked (GlcNAc...) (Potential).
FT   DISULFID     52    116       By similarity.
FT   DISULFID    169    217       By similarity.
FT   DISULFID    258    315       By similarity.
FT   VAR_SEQ       1    226       Missing (in isoform 4).
FT                                /FTId=VSP_039254.
FT   VAR_SEQ      31    147       AGFVKSPMSETKLTGDAFELYCDVVGSPTPEIQWWYAEVNR
FT                                AESFRQLWDGARKRRVTVNTAYGSNGVSVLRITRLTLEDSG
FT                                TYECRASNDPKRNDLRQNPSITWIRAQATISVLQK -> E
FT                                (in isoform 1 and isoform 3).
FT                                /FTId=VSP_039255.
FT   VAR_SEQ     227    235       ANATIEVKA -> MSVVDLPNS (in isoform 4).
FT                                /FTId=VSP_039256.
FT   VAR_SEQ     371    374       Missing (in isoform 3).
FT                                /FTId=VSP_039257.
FT   CONFLICT    245    245       S -> C (in Ref. 2; BAE32261).
FT   CONFLICT    246    246       E -> R (in Ref. 2; BAC35855).
FT   CONFLICT    386    386       H -> P (in Ref. 1; BAA09054).
SQ   SEQUENCE   397 AA;  44373 MW;  E9C19EE0BD3A324A CRC64;
     MSGSSLPGAL ALSLLLVSGS LLPGPGAAQN AGFVKSPMSE TKLTGDAFEL YCDVVGSPTP
     EIQWWYAEVN RAESFRQLWD GARKRRVTVN TAYGSNGVSV LRITRLTLED SGTYECRASN
     DPKRNDLRQN PSITWIRAQA TISVLQKPRI VTSEEVIIRE SLLPVTLQCN LTSSSHTLMY
     SYWTRNGVEL TATRKNASNM EYRINKPRAE DSGEYHCVYH FVSAPKANAT IEVKAAPDIT
     GHKRSENKNE GQDAMMYCKS VGYPHPEWIW RKKENGVFEE ISNSSGRFFI TNKENYTELS
     IVNLQITEDP GEYECNATNS IGSASVSTVL RVRSHLAPLW PFLGILAEII ILVVIIVVYE
     KRKRPDEVPD DDEPAGPMKT NSTNNHKDKN LRQRNTN
//
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.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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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   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   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   ATP5J_MOUSE             Reviewed;         108 AA.
AC   P97450;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=ATP synthase-coupling factor 6, mitochondrial;
DE            Short=ATPase subunit F6;
DE   Flags: Precursor;
GN   Name=Atp5j;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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   Rocha D., Anderson E., Botcherby M., Jordan B., Carrier A.;
RL   Submitted (NOV-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=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-84 AND LYS-99, 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 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. Also involved in the restoration
CC       of oligomycin-sensitive ATPase activity to depleted F1-F0
CC       complexes.
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 eukaryotic ATPase subunit F6 family.
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DR   EMBL; U77128; AAB19213.1; -; mRNA.
DR   EMBL; AK078484; BAC37301.1; -; mRNA.
DR   EMBL; BC010766; AAH10766.1; -; mRNA.
DR   IPI; IPI00125460; -.
DR   PIR; PD0444; PD0444.
DR   RefSeq; NP_058035.1; NM_016755.2.
DR   UniGene; Mm.353; -.
DR   ProteinModelPortal; P97450; -.
DR   SMR; P97450; 36-101.
DR   STRING; P97450; -.
DR   PhosphoSite; P97450; -.
DR   SWISS-2DPAGE; P97450; -.
DR   PRIDE; P97450; -.
DR   Ensembl; ENSMUST00000023608; ENSMUSP00000023608; ENSMUSG00000022890.
DR   Ensembl; ENSMUST00000114191; ENSMUSP00000109829; ENSMUSG00000022890.
DR   Ensembl; ENSMUST00000114193; ENSMUSP00000109831; ENSMUSG00000022890.
DR   GeneID; 11957; -.
DR   KEGG; mmu:11957; -.
DR   UCSC; uc007zth.1; mouse.
DR   CTD; 11957; -.
DR   MGI; MGI:107777; Atp5j.
DR   eggNOG; roNOG16374; -.
DR   HOGENOM; HBG717361; -.
DR   HOVERGEN; HBG062261; -.
DR   InParanoid; P97450; -.
DR   OMA; DMNTFPN; -.
DR   OrthoDB; EOG4FN4K5; -.
DR   PhylomeDB; P97450; -.
DR   NextBio; 280077; -.
DR   ArrayExpress; P97450; -.
DR   Bgee; P97450; -.
DR   Genevestigator; P97450; -.
DR   GermOnline; ENSMUSG00000022890; 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; IPR008387; ATPase_F0-cplx_f6su_mt.
DR   InterPro; IPR016349; ATPase_F0-cplx_f6su_mt_subgr.
DR   PANTHER; PTHR12441; ATPase_F0_F6_mt; 1.
DR   Pfam; PF05511; ATP-synt_F6; 1.
DR   PIRSF; PIRSF002455; ATP_synthase_coupling_factor_6; 1.
DR   SUPFAM; SSF111357; ATPase_F0_F6_mt; 1.
PE   1: Evidence at protein level;
KW   Acetylation; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Transit peptide;
KW   Transport.
FT   TRANSIT       1     32       Mitochondrion (By similarity).
FT   CHAIN        33    108       ATP synthase-coupling factor 6,
FT                                mitochondrial.
FT                                /FTId=PRO_0000002529.
FT   MOD_RES      41     41       N6-acetyllysine (By similarity).
FT   MOD_RES      46     46       N6-acetyllysine (By similarity).
FT   MOD_RES      84     84       N6-acetyllysine.
FT   MOD_RES      99     99       N6-acetyllysine.
FT   MOD_RES     105    105       N6-acetyllysine (By similarity).
SQ   SEQUENCE   108 AA;  12496 MW;  E2A2E63F7F23CEBF CRC64;
     MVLQRIFRLS SVLRSAVSVH LKRNIGVTAV AFNKELDPVQ KLFVDKIREY KSKRQASGGP
     VDIGPEYQQD LDRELYKLKQ MYGKGEMDTF PTFKFDDPKF EVIDKPQS
//
ID   AMD_MOUSE               Reviewed;         979 AA.
AC   P97467;
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=Peptidyl-glycine alpha-amidating monooxygenase;
DE            Short=PAM;
DE   Includes:
DE     RecName: Full=Peptidylglycine alpha-hydroxylating monooxygenase;
DE              Short=PHM;
DE              EC=1.14.17.3;
DE   Includes:
DE     RecName: Full=Peptidyl-alpha-hydroxyglycine alpha-amidating lyase;
DE              EC=4.3.2.5;
DE     AltName: Full=Peptidylamidoglycolate lyase;
DE              Short=PAL;
DE   Flags: Precursor;
GN   Name=Pam;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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   Jeong J.H., Baek S.J., Park D.H.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-924 AND SER-925, 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-948 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: Bifunctional enzyme that catalyzes 2 sequential steps in
CC       C-terminal alpha-amidation of peptides. The monooxygenase part
CC       produces an unstable peptidyl(2-hydroxyglycine) intermediate that
CC       is dismutated to glyoxylate and the corresponding desglycine
CC       peptide amide by the lyase part. C-terminal amidation of peptides
CC       such as neuropeptides is essential for full biological activity
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Peptidylglycine + ascorbate + O(2) =
CC       peptidyl(2-hydroxyglycine) + dehydroascorbate + H(2)O.
CC   -!- CATALYTIC ACTIVITY: Peptidylamidoglycolate = peptidyl amide +
CC       glyoxylate.
CC   -!- COFACTOR: Zinc; for the lyase reaction (By similarity).
CC   -!- COFACTOR: Binds 2 copper ions per subunit; For the monoxygenase
CC       reaction (By similarity).
CC   -!- SUBUNIT: Monomer. Interacts with RASSF9 (By similarity).
CC   -!- INTERACTION:
CC       P97924:Kalrn (xeno); NbExp=1; IntAct=EBI-1397216, EBI-1397166;
CC       Q63285:Uhmk1 (xeno); NbExp=1; IntAct=EBI-1397216, EBI-1397144;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC       membrane; Single-pass membrane protein (By similarity).
CC       Note=Secretory granules.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidyl-
CC       alpha-hydroxyglycine alpha-amidating lyase family.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the copper type
CC       II ascorbate-dependent monooxygenase family.
CC   -!- SIMILARITY: Contains 5 NHL repeats.
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DR   EMBL; U79523; AAB38364.1; -; mRNA.
DR   IPI; IPI00323974; -.
DR   RefSeq; NP_038654.2; NM_013626.3.
DR   UniGene; Mm.441453; -.
DR   UniGene; Mm.5121; -.
DR   ProteinModelPortal; P97467; -.
DR   SMR; P97467; 44-355, 498-823.
DR   IntAct; P97467; 2.
DR   STRING; P97467; -.
DR   PhosphoSite; P97467; -.
DR   PRIDE; P97467; -.
DR   Ensembl; ENSMUST00000058762; ENSMUSP00000057112; ENSMUSG00000026335.
DR   GeneID; 18484; -.
DR   KEGG; mmu:18484; -.
DR   UCSC; uc007cfo.1; mouse.
DR   CTD; 18484; -.
DR   MGI; MGI:97475; Pam.
DR   HOGENOM; HBG443653; -.
DR   HOVERGEN; HBG004218; -.
DR   InParanoid; P97467; -.
DR   BRENDA; 1.14.17.3; 244.
DR   BRENDA; 4.3.2.5; 244.
DR   NextBio; 294198; -.
DR   ArrayExpress; P97467; -.
DR   Bgee; P97467; -.
DR   CleanEx; MM_PAM; -.
DR   Genevestigator; P97467; -.
DR   GermOnline; ENSMUSG00000026335; Mus musculus.
DR   GO; GO:0005829; C:cytosol; TAS:MGI.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:MGI.
DR   GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0004598; F:peptidylamidoglycolate lyase activity; IEA:EC.
DR   GO; GO:0004504; F:peptidylglycine monooxygenase activity; TAS:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0006518; P:peptide metabolic process; TAS:MGI.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR014784; Cu2_ascorb_mOase-like_C.
DR   InterPro; IPR020611; Cu2_ascorb_mOase_CS-1.
DR   InterPro; IPR014783; Cu2_ascorb_mOase_CS-2.
DR   InterPro; IPR000323; Cu2_ascorb_mOase_N.
DR   InterPro; IPR001258; NHL_repeat.
DR   InterPro; IPR013017; NHL_repeat_subgr.
DR   InterPro; IPR000720; Pep_amidat_mOase.
DR   InterPro; IPR008977; PHM_PNGase_F-fold_dom.
DR   Gene3D; G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 1.
DR   Gene3D; G3DSA:2.60.120.230; Cu2_ascorb_mOase_core; 1.
DR   Gene3D; G3DSA:2.60.120.310; Cu2_ascorb_mOase_core; 1.
DR   Pfam; PF01082; Cu2_monooxygen; 1.
DR   Pfam; PF01436; NHL; 4.
DR   PRINTS; PR00790; PAMONOXGNASE.
DR   SUPFAM; SSF49742; PHM_PNGase_F; 2.
DR   PROSITE; PS00084; CU2_MONOOXYGENASE_1; 1.
DR   PROSITE; PS00085; CU2_MONOOXYGENASE_2; 1.
DR   PROSITE; PS51125; NHL; 5.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Copper; Cytoplasmic vesicle;
KW   Disulfide bond; Glycoprotein; Lyase; Membrane; Metal-binding;
KW   Monooxygenase; Multifunctional enzyme; Oxidoreductase; Phosphoprotein;
KW   Repeat; Signal; Transmembrane; Transmembrane helix; Vitamin C; Zinc.
FT   SIGNAL        1     24       By similarity.
FT   PROPEP       25     34       By similarity.
FT                                /FTId=PRO_0000006363.
FT   CHAIN        35    979       Peptidyl-glycine alpha-amidating
FT                                monooxygenase.
FT                                /FTId=PRO_0000006364.
FT   TOPO_DOM     35    869       Intragranular (Potential).
FT   TRANSMEM    870    893       Helical; (Potential).
FT   TOPO_DOM    894    979       Cytoplasmic (Potential).
FT   REPEAT      501    544       NHL 1.
FT   REPEAT      570    611       NHL 2.
FT   REPEAT      620    665       NHL 3.
FT   REPEAT      673    717       NHL 4.
FT   REPEAT      769    812       NHL 5.
FT   REGION        1    497       Peptidylglycine alpha-hydroxylating
FT                                monooxygenase (By similarity).
FT   REGION      498    823       Peptidyl-alpha-hydroxyglycine alpha-
FT                                amidating lyase (By similarity).
FT   REGION      931    948       Interaction with RASSF9 (By similarity).
FT   METAL       106    106       Copper A (By similarity).
FT   METAL       107    107       Copper A (By similarity).
FT   METAL       171    171       Copper A (By similarity).
FT   METAL       241    241       Copper B (By similarity).
FT   METAL       243    243       Copper B (By similarity).
FT   METAL       313    313       Copper B (By similarity).
FT   MOD_RES     924    924       Phosphoserine.
FT   MOD_RES     925    925       Phosphoserine.
FT   MOD_RES     935    935       Phosphoserine (By similarity).
FT   MOD_RES     948    948       Phosphoserine.
FT   MOD_RES     952    952       Phosphoserine.
FT   MOD_RES     962    962       Phosphoserine (By similarity).
FT   MOD_RES     964    964       Phosphoserine (By similarity).
FT   CARBOHYD    765    765       N-linked (GlcNAc...) (Potential).
FT   DISULFID     46    185       By similarity.
FT   DISULFID     80    125       By similarity.
FT   DISULFID    113    130       By similarity.
FT   DISULFID    226    333       By similarity.
FT   DISULFID    292    314       By similarity.
FT   DISULFID    634    655       By similarity.
FT   DISULFID    702    713       By similarity.
SQ   SEQUENCE   979 AA;  109048 MW;  1F5BED76567A741A CRC64;
     MAGRARSRLL LLLGLLALQS SCLAFRSPLS VFKRFKETTR SFSNECLGTT RPITPIDSSD
     FTLDIRMPGV TPKESDTYFC MSMRLPVDEE AFVIDFKPRA SMDTVHHMLL FGCNMPSSTG
     SYWFCDEGTC TDKANILYAW ARNAPPTRLP KGVGFRVGGE TGSKYFVLQV HYGDISAFRD
     NHKDCSGVSL HLTRVPQPLI AGMYLMMSVN TVIPPGEKVV NSDISCHYKM YPMHVFAYRV
     HTHHLGKVVS GYRVRNGQWT LIGRQSPQLP QAFYPVEHPV DVAFGDILAA RCVFTGEGRT
     EATHIGGTSS DEMCNLYIMY YMEAKHAVSF MTCTQNVAPD MFRTIPEEAN IPIPVKSDMV
     MIHGHHKETE NKEKSALIQQ PKQGEEEAFE QGDFYSLLSK LLGEREDVVH VHKYNPTEKT
     ESGSDLVAEI ANVVQKKDLG RSDAREGAEH EEGGNAILVR DRIHKFHRLE STLRPAESRA
     LSFQQPGEGP WEPELAGDFH VEEALEWPGV YLLPGQVSGV ALDSKNNLVI FHRGDHVWDG
     NSFDSKFVYQ QRGLGPIEED TILVIDPNKA EILQSSGKNL FYLPHGLSID TDGNYWVTDV
     ALHQVFKLEP RSKEGPLLVL GRSMQPGSDQ NHFCQPTDVA VEPSTGAVFV SDGYCNSRIV
     QFSPSGKFIT QWGEESSGSS PKPGQFSVPH SLALVPHLNQ LCVADRENGR IQCFKTDTKE
     FVREIKHASF GRNVFAISYI PGFLFAVNGK PYFGDQEPVQ GFVMNFSSGE IIDVFKPVRK
     HFDMPHDIVA SEDGTVYIGD AHTNTVWKFT LTESRLEVEH RSVKKAGIEV PEIKEAEAVV
     EPKVKNKPTS SELQKMQEKK KLIKDPGSGV PVVLITTLLV IPVVVLLAIA MFIRWKKSRA
     FGDHDRKLES SSGRVLGRLR GKGSSGLNLG NFFASRKGYS RKGFDRVSTE GSDQEKDEDD
     GSESEEEYSR PLPTPAPSS
//
ID   WBP2_MOUSE              Reviewed;         261 AA.
AC   P97765;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=WW domain-binding protein 2;
DE            Short=WBP-2;
GN   Name=Wbp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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 YAP1.
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   [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   INTERACTION WITH NEDD4, DOMAINS, AND MUTAGENESIS OF TYR-170; TYR-200
RP   AND TYR-252.
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).
CC   -!- SUBUNIT: Binds to the WW domain of YAP1, WWP1 and WWP2 (By
CC       similarity). Interacts with NEDD4.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- DOMAIN: The WW-binding 1 motif mediates interaction with NEDD4.
CC   -!- SIMILARITY: Contains 1 GRAM domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; U40826; AAB40893.1; -; mRNA.
DR   EMBL; BC055058; AAH55058.1; -; mRNA.
DR   IPI; IPI00129045; -.
DR   RefSeq; NP_058548.1; NM_016852.2.
DR   UniGene; Mm.284792; -.
DR   ProteinModelPortal; P97765; -.
DR   SMR; P97765; 13-81.
DR   STRING; P97765; -.
DR   PhosphoSite; P97765; -.
DR   PRIDE; P97765; -.
DR   Ensembl; ENSMUST00000074628; ENSMUSP00000074204; ENSMUSG00000034341.
DR   GeneID; 22378; -.
DR   KEGG; mmu:22378; -.
DR   UCSC; uc007mjv.1; mouse.
DR   CTD; 22378; -.
DR   MGI; MGI:104709; Wbp2.
DR   eggNOG; roNOG16701; -.
DR   HOVERGEN; HBG027489; -.
DR   OrthoDB; EOG4ZGPDN; -.
DR   NextBio; 302733; -.
DR   ArrayExpress; P97765; -.
DR   Bgee; P97765; -.
DR   CleanEx; MM_WBP2; -.
DR   Genevestigator; P97765; -.
DR   GermOnline; ENSMUSG00000034341; Mus musculus.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR018826; WW-domain-binding.
DR   Pfam; PF02893; GRAM; 1.
DR   Pfam; PF10349; WWbp; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1    261       WW domain-binding protein 2.
FT                                /FTId=PRO_0000065951.
FT   DOMAIN        1     84       GRAM.
FT   MOTIF       196    200       WW-binding 1.
FT   MOTIF       248    252       WW-binding 2.
FT   COMPBIAS    146    255       Pro-rich.
FT   MOD_RES     232    232       Phosphotyrosine (By similarity).
FT   MUTAGEN     170    170       Y->A: No effect on interaction with
FT                                NEDD4.
FT   MUTAGEN     200    200       Y->A: Abolishes interaction with NEDD4.
FT   MUTAGEN     252    252       Y->A: No effect on interaction with
FT                                NEDD4.
SQ   SEQUENCE   261 AA;  28032 MW;  DA475B184F284380 CRC64;
     MALNKNHSEG GGVIVNNTES ILMSYDHVEL TFNDMKNVPE AFKGTKKGTV YLTPYRVIFL
     SKGKDAMQSF MMPFYLMKDC EIKQPVFGAN FIKGIVKAEA GGGWEGSASY KLTFTAGGAI
     EFGQRMLQVA SQASRGEVPN GAYGYPYMPS GAYVFPPPVA NGMYPCPPGY PYPPPPPEFY
     PGPPMMDGAM GYVQPPPPPY PGPMEPPVSG PSAPATPAAE AKAAEAAASA YYNPGNPHNV
     YMPTSQPPPP PYYPPEDKKT Q
//
ID   PA2G6_MOUSE             Reviewed;         752 AA.
AC   P97819; Q99LA9; Q9JK61;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 2.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=85 kDa calcium-independent phospholipase A2;
DE            Short=CaI-PLA2;
DE            Short=iPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Group VI phospholipase A2;
DE            Short=GVI PLA2;
GN   Name=Pla2g6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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;
RX   MEDLINE=97236816; PubMed=9079688; DOI=10.1074/jbc.272.13.8576;
RA   Balboa M.A., Balsinde J., Jones S.S., Dennis E.A.;
RT   "Identity between the Ca2+-independent phospholipase A2 enzymes from
RT   P388D1 macrophages and Chinese hamster ovary cells.";
RL   J. Biol. Chem. 272:8576-8580(1997).
RN   [2]
RP   SEQUENCE REVISION TO 2-3; 9; 11 AND 211.
RA   Balboa M.A., Balsinde J., Jones S.S., Dennis E.A.;
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=NIH Swiss;
RA   Chiu C.-H., Jackowski S.;
RT   "Ca2+-independent phospholipase A2 (IPLA2) long isoform from mouse.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, 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   [5]
RP   PROTEIN SEQUENCE OF 479-491, 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-533, 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: Phosphatidylcholine + H(2)O = 1-
CC       acylglycerophosphocholine + a carboxylate.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Short;
CC         IsoId=P97819-1; Sequence=Displayed;
CC       Name=2; Synonyms=Long;
CC         IsoId=P97819-2; Sequence=VSP_015736;
CC   -!- SIMILARITY: Contains 7 ANK repeats.
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DR   EMBL; U88624; AAB48511.2; -; mRNA.
DR   EMBL; AF259401; AAF72651.1; -; mRNA.
DR   EMBL; BC003487; AAH03487.1; -; mRNA.
DR   EMBL; BC057209; AAH57209.1; -; mRNA.
DR   IPI; IPI00122327; -.
DR   IPI; IPI00129989; -.
DR   RefSeq; NP_001185952.1; NM_001199023.1.
DR   RefSeq; NP_001185953.1; NM_001199024.1.
DR   RefSeq; NP_001185954.1; NM_001199025.1.
DR   RefSeq; NP_058611.1; NM_016915.4.
DR   UniGene; Mm.155620; -.
DR   ProteinModelPortal; P97819; -.
DR   SMR; P97819; 118-396.
DR   STRING; P97819; -.
DR   PhosphoSite; P97819; -.
DR   PRIDE; P97819; -.
DR   Ensembl; ENSMUST00000047816; ENSMUSP00000044234; ENSMUSG00000042632.
DR   Ensembl; ENSMUST00000109661; ENSMUSP00000105288; ENSMUSG00000042632.
DR   GeneID; 53357; -.
DR   KEGG; mmu:53357; -.
DR   UCSC; uc007wtd.1; mouse.
DR   UCSC; uc007wte.1; mouse.
DR   CTD; 53357; -.
DR   MGI; MGI:1859152; Pla2g6.
DR   eggNOG; roNOG09988; -.
DR   GeneTree; ENSGT00530000063645; -.
DR   HOVERGEN; HBG053482; -.
DR   OMA; VYIHEHR; -.
DR   OrthoDB; EOG46Q6RW; -.
DR   BRENDA; 3.1.1.4; 244.
DR   NextBio; 310173; -.
DR   ArrayExpress; P97819; -.
DR   Bgee; P97819; -.
DR   CleanEx; MM_PLA2G6; -.
DR   Genevestigator; P97819; -.
DR   GermOnline; ENSMUSG00000042632; Mus musculus.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPlipase.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR002641; Patatin/PhospholipaseA2-rel.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 4.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00248; ANK; 6.
DR   SUPFAM; SSF52151; Acyl_Trfase/lysoPlipase; 1.
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;
KW   Direct protein sequencing; Hydrolase; Lipid degradation;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1    752       85 kDa calcium-independent phospholipase
FT                                A2.
FT                                /FTId=PRO_0000067038.
FT   REPEAT      151    181       ANK 1.
FT   REPEAT      185    215       ANK 2.
FT   REPEAT      219    248       ANK 3.
FT   REPEAT      251    281       ANK 4.
FT   REPEAT      286    312       ANK 5.
FT   REPEAT      316    345       ANK 6.
FT   REPEAT      349    378       ANK 7.
FT   ACT_SITE    465    465       Potential.
FT   MOD_RES     533    533       Phosphothreonine.
FT   VAR_SEQ     396    396       Q -> LITRKALLTLLKTVGADHHFPIIQGVSTEQGSAAAT
FT                                HPLFSLDRTQPPAISLNNLE (in isoform 2).
FT                                /FTId=VSP_015736.
SQ   SEQUENCE   752 AA;  83702 MW;  AAC3347B0E1292E9 CRC64;
     MQFFGRLVNT LSSVTNLFSN PFRVKEVSLT DYVSSERVRE EGQLILLQNV SNRTWDCVLV
     SPRNPQSGFR LFQLESEADA LVNFQQFSSQ LPPFYESSVQ VLHVEVLQHL TDLIRNHPSW
     TVTHLAVELG IRECFHHSRI ISCANSTENE EGCTPLHLAC RKGDSEILVE LVQYCHAQMD
     VTDNKGETAF HYAVQGDNPQ VLQLLGKNAS AGLNQVNNQG LTPLHLACKM GKQEMVRVLL
     LCNARCNIMG PGGFPIHTAM KFSQKGCAEM IISMDSNQIH SKDPRYGASP LHWAKNAEMA
     RMLLKRGCDV DSTSSSGNTA LHVAVMRNRF DCVMVLLTYG ANAGARGEHG NTPLHLAMSK
     DNMEMVKALI VFGAEVDTPN DFGETPALIA SKISKQLQDL MPISRARKPA FILSSMRDEK
     RSHDHLLCLD GGGVKGLVII QLLIAIEKAS GVATKDLFDW VAGTSTGGIL ALAILHSKSM
     AYMRGVYFRM KDEVFRGSRP YESGPLEEFL KREFGEHTKM TDVKKPKVML TGTLSDRQPA
     ELHLFRNYDA PEAVREPRCN QNINLKPPTQ PADQLVWRAA RSSGAAPTYF RPNGRFLDGG
     LLANNPTLDA MTEIHEYNQD MIRKGQGNKV KKLSIVVSLG TGKSPQVPVT CVDVFRPSNP
     WELAKTVFGA KELGKMVVDC CTDPDGRAVD RARAWCEMVG IQYFRLNPQL GSDIMLDEVS
     DAVLVNALWE TEVYIYEHRE EFQKLVQLLL SP
//
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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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   C1QA_MOUSE              Reviewed;         245 AA.
AC   P98086;
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=Complement C1q subcomponent subunit A;
DE   Flags: Precursor;
GN   Name=C1qa;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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=Macrophage;
RX   MEDLINE=92043789; PubMed=1940381;
RA   Petry F., Reid K.B.M., Loos M.;
RT   "Gene expression of the A- and B-chain of mouse C1q in different
RT   tissues and the characterization of the recombinant A-chain.";
RL   J. Immunol. 147:3988-3993(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129; TISSUE=Liver;
RX   MEDLINE=96186528; PubMed=8606057; DOI=10.1007/s002510050077;
RA   Petry F., McClive P.J., Botto M., Morley B.J., Morahan G., Loos M.;
RT   "The mouse C1q genes are clustered on chromosome 4 and show
RT   conservation of gene organization.";
RL   Immunogenetics 43:370-376(1996).
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-146, 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).
CC   -!- FUNCTION: C1q associates with the proenzymes C1r and C1s to yield
CC       C1, the first component of the serum complement system. The
CC       collagen-like regions of C1q interact with the Ca(2+)-dependent
CC       C1r(2)C1s(2) proenzyme complex, and efficient activation of C1
CC       takes place on interaction of the globular heads of C1q with the
CC       Fc regions of IgG or IgM antibody present in immune complexes.
CC   -!- SUBUNIT: C1 is a calcium-dependent trimolecular complex of C1q, R
CC       and S in the molar ration of 1:2:2. C1q subcomponent is composed
CC       of nine subunits, six of which are disulfide-linked dimers of the
CC       A and B chains, and three of which are disulfide-linked dimers of
CC       the C chain.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: O-linked glycans consist of Glc-Gal disaccharides bound to
CC       the oxygen atom of post-translationally added hydroxyl groups (By
CC       similarity).
CC   -!- PTM: Hydroxylation on proline residues within the sequence motif,
CC       GXPG, is most likely 4-hydroxy as this fits the requirement for 4-
CC       hydroxylation in vertebrates (By similarity).
CC   -!- SIMILARITY: Contains 1 C1q domain.
CC   -!- SIMILARITY: Contains 1 collagen-like domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; X58861; CAA41664.1; -; mRNA.
DR   IPI; IPI00125310; -.
DR   PIR; S19018; S19018.
DR   UniGene; Mm.439957; -.
DR   ProteinModelPortal; P98086; -.
DR   SMR; P98086; 27-58, 112-244.
DR   STRING; P98086; -.
DR   PhosphoSite; P98086; -.
DR   PRIDE; P98086; -.
DR   Ensembl; ENSMUST00000046285; ENSMUSP00000048836; ENSMUSG00000036887.
DR   MGI; MGI:88223; C1qa.
DR   eggNOG; maNOG20501; -.
DR   HOGENOM; HBG444750; -.
DR   HOVERGEN; HBG108220; -.
DR   InParanoid; P98086; -.
DR   OrthoDB; EOG473PS4; -.
DR   ArrayExpress; P98086; -.
DR   Bgee; P98086; -.
DR   Genevestigator; P98086; -.
DR   GermOnline; ENSMUSG00000036887; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0006958; P:complement activation, classical pathway; IMP:MGI.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   InterPro; IPR001073; C1q.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR008983; Tumour_necrosis_fac-like.
DR   Gene3D; G3DSA:2.60.120.40; Tumour_necrosis_fac-like; 1.
DR   Pfam; PF00386; C1q; 1.
DR   Pfam; PF01391; Collagen; 1.
DR   PRINTS; PR00007; COMPLEMNTC1Q.
DR   SMART; SM00110; C1Q; 1.
DR   SUPFAM; SSF49842; TNF_like; 1.
DR   PROSITE; PS50871; C1Q; 1.
PE   1: Evidence at protein level;
KW   Collagen; Complement pathway; Disulfide bond; Glycoprotein;
KW   Hydroxylation; Immunity; Innate immunity; Repeat; Secreted; Signal.
FT   SIGNAL        1     22       By similarity.
FT   CHAIN        23    245       Complement C1q subcomponent subunit A.
FT                                /FTId=PRO_0000003518.
FT   DOMAIN       31    109       Collagen-like.
FT   DOMAIN      110    245       C1q.
FT   MOD_RES      45     45       4-hydroxyproline (By similarity).
FT   MOD_RES      48     48       5-hydroxylysine (By similarity).
FT   MOD_RES      54     54       4-hydroxyproline (By similarity).
FT   MOD_RES      67     67       5-hydroxylysine (By similarity).
FT   MOD_RES      85     85       4-hydroxyproline (By similarity).
FT   MOD_RES     100    100       5-hydroxylysine (By similarity).
FT   MOD_RES     103    103       5-hydroxylysine (By similarity).
FT   CARBOHYD     48     48       O-linked (Gal...) (By similarity).
FT   CARBOHYD     67     67       O-linked (Gal...) (By similarity).
FT   CARBOHYD    100    100       O-linked (Gal...) (By similarity).
FT   CARBOHYD    146    146       N-linked (GlcNAc...).
FT   DISULFID     26     26       Interchain (with C-29 in B chain) (By
FT                                similarity).
SQ   SEQUENCE   245 AA;  25986 MW;  61310A5D8A517C5A CRC64;
     METSQGWLVA CVLTMILVWT VAEDVCRAPN GKDGAPGNPG RPGRPGLKGE RGEPGAAGIR
     TGIRGFKGDP GESGPPGKPG NVGLPGPSGP LGDSGPQGLK GVKGNPGNIR DQPRPAFSAI
     RQNPMTLGNV VIFDKVLTNQ ESPYQNHTGR FICAVPGFYY FNFQVISKWD LCLFIKSSSG
     GQPRDSLSFS NTNNKGLFQV LAGGTVLQLR RGDEVWIEKD PAKGRIYQGT EADSIFSGFL
     IFPSA
//
ID   IL6RB_MOUSE             Reviewed;         917 AA.
AC   Q00560;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   08-MAR-2011, entry version 105.
DE   RecName: Full=Interleukin-6 receptor subunit beta;
DE            Short=IL-6 receptor subunit beta;
DE            Short=IL-6R subunit beta;
DE            Short=IL-6R-beta;
DE            Short=IL-6RB;
DE   AltName: Full=Interleukin-6 signal transducer;
DE   AltName: Full=Membrane glycoprotein 130;
DE            Short=gp130;
DE   AltName: Full=Oncostatin-M receptor subunit alpha;
DE   AltName: CD_antigen=CD130;
DE   Flags: Precursor;
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 [MRNA].
RC   STRAIN=ICR; TISSUE=Macrophage;
RX   MEDLINE=92291532; PubMed=1602143;
RA   Saito M., Yoshida K., Hibi M., Taga T., Kishimoto T.;
RT   "Molecular cloning of a murine IL-6 receptor-associated signal
RT   transducer, gp130, and its regulated expression in vivo.";
RL   J. Immunol. 148:4066-4071(1992).
RN   [2]
RP   SUBUNIT.
RX   MEDLINE=99120951; PubMed=9920829;
RA   Tanaka M., Hara T., Copeland N.G., Gilbert D.J., Jenkins N.A.,
RA   Miyajima A.;
RT   "Reconstitution of the functional mouse oncostatin M (OSM) receptor:
RT   molecular cloning of the OSM receptor beta subunit.";
RL   Blood 93:804-815(1999).
RN   [3]
RP   INTERACTION WITH INPP5D.
RX   PubMed=17105399; DOI=10.1089/scd.2006.15.641;
RA   Desponts C., Ninos J.M., Kerr W.G.;
RT   "s-SHIP associates with receptor complexes essential for pluripotent
RT   stem cell growth and survival.";
RL   Stem Cells Dev. 15:641-646(2006).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-225, 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: Signal-transducing molecule. The receptor systems for
CC       IL6, LIF, OSM, CNTF, IL11, CTF1 and BSF3 can utilize gp130 for
CC       initiating signal transmission. Binds to IL6/IL6R (alpha chain)
CC       complex, resulting in the formation of high-affinity IL6 binding
CC       sites, and transduces the signal. Does not bind IL6. May have a
CC       role in embryonic development.
CC   -!- SUBUNIT: Component of a hexamer of two molecules each of IL6, IL6R
CC       and IL6ST (By similarity). Forms heterodimers composed of LIPR and
CC       IL6ST (type I OSM receptor). Also forms heterodimers composed of
CC       OSMR and IL6ST (type II OSM receptor). Interacts with
CC       INPP5D/SHIP1.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Found in tissues such as brain, heart, thymus,
CC       spleen, kidney, lung and liver. Found in all the cell lines tested
CC       except BAF-B03. Expression not restricted to IL6-responsive cells.
CC   -!- DEVELOPMENTAL STAGE: In embryonic stem cells it is found from day
CC       6 of gestation. It reaches a peak on day 8 and gradually declines
CC       during the rest of embryogenesis.
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   -!- PTM: Phosphorylation of Ser-780 down-regulates cell surface
CC       expression (By similarity).
CC   -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
CC       subfamily.
CC   -!- SIMILARITY: Contains 5 fibronectin type-III domains.
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; X62646; CAA44515.1; -; mRNA.
DR   EMBL; M83336; AAA37723.1; -; mRNA.
DR   IPI; IPI00120155; -.
DR   PIR; I49699; I49699.
DR   UniGene; Mm.4364; -.
DR   PDB; 2HMH; X-ray; 2.00 A; B=753-763.
DR   PDBsum; 2HMH; -.
DR   ProteinModelPortal; Q00560; -.
DR   SMR; Q00560; 24-610.
DR   DIP; DIP-5782N; -.
DR   MINT; MINT-3382082; -.
DR   STRING; Q00560; -.
DR   PhosphoSite; Q00560; -.
DR   PRIDE; Q00560; -.
DR   Ensembl; ENSMUST00000070731; ENSMUSP00000064205; ENSMUSG00000021756.
DR   MGI; MGI:96560; Il6st.
DR   eggNOG; roNOG14805; -.
DR   HOGENOM; HBG281001; -.
DR   HOVERGEN; HBG052119; -.
DR   InParanoid; Q00560; -.
DR   OrthoDB; EOG42BX7V; -.
DR   ArrayExpress; Q00560; -.
DR   Bgee; Q00560; -.
DR   CleanEx; MM_IL6ST; -.
DR   Genevestigator; Q00560; -.
DR   GermOnline; ENSMUSG00000021756; Mus musculus.
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; IPR003529; Hematopoietin_rcpt_gp130_CS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR010457; IgC2-like_lig-bd.
DR   InterPro; IPR015321; IL6_recept-bd.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 6.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF09240; IL6Ra-bind; 1.
DR   Pfam; PF06328; Lep_receptor_Ig; 1.
DR   SMART; SM00060; FN3; 5.
DR   SUPFAM; SSF49265; FN_III-like; 6.
DR   PROSITE; PS50853; FN3; 5.
DR   PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Membrane; Phosphoprotein; Receptor; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     22       Potential.
FT   CHAIN        23    917       Interleukin-6 receptor subunit beta.
FT                                /FTId=PRO_0000010900.
FT   TOPO_DOM     23    617       Extracellular (Potential).
FT   TRANSMEM    618    639       Helical; (Potential).
FT   TOPO_DOM    640    917       Cytoplasmic (Potential).
FT   DOMAIN       26    120       Ig-like C2-type.
FT   DOMAIN      125    214       Fibronectin type-III 1.
FT   DOMAIN      220    319       Fibronectin type-III 2.
FT   DOMAIN      324    416       Fibronectin type-III 3.
FT   DOMAIN      421    512       Fibronectin type-III 4.
FT   DOMAIN      514    608       Fibronectin type-III 5.
FT   MOTIF       308    312       WSXWS motif.
FT   MOTIF       649    657       Box 1 motif.
FT   COMPBIAS    723    741       Ser-rich.
FT   MOD_RES     665    665       Phosphoserine (By similarity).
FT   MOD_RES     780    780       Phosphoserine (By similarity).
FT   MOD_RES     818    818       Phosphoserine (By similarity).
FT   MOD_RES     827    827       Phosphoserine (By similarity).
FT   CARBOHYD     43     43       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     61     61       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     83     83       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    131    131       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    157    157       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    225    225       N-linked (GlcNAc...).
FT   CARBOHYD    388    388       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    476    476       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    551    551       N-linked (GlcNAc...) (Potential).
FT   DISULFID     28     54       By similarity.
FT   DISULFID     48    103       By similarity.
FT   DISULFID    134    144       By similarity.
FT   DISULFID    172    180       By similarity.
FT   DISULFID    456    464       By similarity.
SQ   SEQUENCE   917 AA;  102452 MW;  FCEFD220BC2466F4 CRC64;
     MSAPRIWLAQ ALLFFLTTES IGQLLEPCGY IYPEFPVVQR GSNFTAICVL KEACLQHYYV
     NASYIVWKTN HAAVPREQVT VINRTTSSVT FTDVVLPSVQ LTCNILSFGQ IEQNVYGVTM
     LSGFPPDKPT NLTCIVNEGK NMLCQWDPGR ETYLETNYTL KSEWATEKFP DCQSKHGTSC
     MVSYMPTYYV NIEVWVEAEN ALGKVSSESI NFDPVDKVKP TPPYNLSVTN SEELSSILKL
     SWVSSGLGGL LDLKSDIQYR TKDASTWIQV PLEDTMSPRT SFTVQDLKPF TEYVFRIRSI
     KDSGKGYWSD WSEEASGTTY EDRPSRPPSF WYKTNPSHGQ EYRSVRLIWK ALPLSEANGK
     ILDYEVILTQ SKSVSQTYTV TGTELTVNLT NDRYVASLAA RNKVGKSAAA VLTIPSPHVT
     AAYSVVNLKA FPKDNLLWVE WTPPPKPVSK YILEWCVLSE NAPCVEDWQQ EDATVNRTHL
     RGRLLESKCY QITVTPVFAT GPGGSESLKA YLKQAAPARG PTVRTKKVGK NEAVLAWDQI
     PVDDQNGFIR NYSISYRTSV GKEMVVHVDS SHTEYTLSSL SSDTLYMVRM AAYTDEGGKD
     GPEFTFTTPK FAQGEIEAIV VPVCLAFLLT TLLGVLFCFN KRDLIKKHIW PNVPDPSKSH
     IAQWSPHTPP RHNFNSKDQM YSDGNFTDVS VVEIEANNKK PCPDDLKSVD LFKKEKVSTE
     GHSSGIGGSS CMSSSRPSIS SNEENESAQS TASTVEYSTV VHSGYRHQVP SVQVFSRSES
     TQPLLDSEER PEDLQLVDSV DGGDEILPRQ PYFKQNCSQP EACPEISHFE RSNQVLSGNE
     EDFVRLKQQQ VSDHISQPYG SEQRRLFQEG STADALGTGA DGQMERFESV GMETTIDEEI
     PKSYLPQTVR QGGYMPQ
//
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   EGFR_MOUSE              Reviewed;        1210 AA.
AC   Q01279;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   08-MAR-2011, entry version 127.
DE   RecName: Full=Epidermal growth factor receptor;
DE            EC=2.7.10.1;
DE   Flags: Precursor;
GN   Name=Egfr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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=93026370; PubMed=1408137;
RA   Avivi A., Skorecki K., Yayon A., Givol D.;
RT   "Promoter region of the murine fibroblast growth factor receptor 2
RT   (bek/KGFR) gene.";
RL   Oncogene 7:1957-1962(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c, and CD-1; TISSUE=Decidua, and Liver;
RX   MEDLINE=93126380; PubMed=7678348; DOI=10.1073/pnas.90.1.55;
RA   Paria B.C., Das S.K., Andrews G.K., Dey S.K.;
RT   "Expression of the epidermal growth factor receptor gene is regulated
RT   in mouse blastocysts during delayed implantation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:55-59(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Liver;
RA   Hibbs M.L.;
RL   Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=B6/C3; TISSUE=Liver;
RX   MEDLINE=94170986; PubMed=8125255;
RA   Luetteke N.C., Phillips H.K., Qiu T.H., Copeland N.G., Earp H.S.,
RA   Jenkins N.A., Lee D.C.;
RT   "The mouse waved-2 phenotype results from a point mutation in the EGF
RT   receptor tyrosine kinase.";
RL   Genes Dev. 8:399-413(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-714.
RC   TISSUE=Brain;
RX   MEDLINE=91232866; PubMed=2030916;
RA   Avivi A., Lax I., Ullrich A., Schlessinger J., Givol D., Morse B.;
RT   "Comparison of EGF receptor sequences as a guide to study the ligand
RT   binding site.";
RL   Oncogene 6:673-676(1991).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 969-1117.
RC   STRAIN=C3H;
RA   Eisinger D.P., Serrero G.;
RL   Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-352 AND ASN-444, 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   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-175, 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: The EGF receptor mediates the biological signal of EGF,
CC       and also of TGF-alpha, amphiregulin, heparin-binding EGF, GP30 and
CC       vaccinia virus growth factor (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBUNIT: Binds RIPK1. Interacts (via autophosphorylated C-terminal
CC       tail) with CBL. Part of a complex with ERBB2 and either PIK3C2A or
CC       PIK3C2B. Interacts (autophosphorylated form) with PIK3C2B; the
CC       interaction may be indirect. Interacts with PELP1. Binds MUC1.
CC       Interacts with AP2M1. Interacts with GAB2 (By similarity).
CC       Interacts with COPG, upon EGF treatment; interaction is essential
CC       for regulation of EGF-dependent nuclear transport of EGFR by
CC       retrograde trafficking from the Golgi to the ER (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein. Endoplasmic reticulum membrane; Single-pass type I
CC       membrane protein (By similarity). Golgi apparatus membrane;
CC       Single-pass type I membrane protein (By similarity). Nucleus
CC       membrane; Single-pass type I membrane protein (By similarity).
CC       Note=In response to EGF, translocated from the cell membrane to
CC       the nucleus via Golgi and ER (By similarity).
CC   -!- PTM: Monoubiquitinated and polyubiquitinated upon EGF stimulation;
CC       which does not affect tyrosine kinase activity or signaling
CC       capacity but may play a role in lysosomal targeting. Polyubiquitin
CC       linkage is mainly through 'Lys-63', but linkage through 'Lys-48',
CC       'Lys-11' and 'Lys-29' also occur (By similarity).
CC   -!- MISCELLANEOUS: Binding of EGF to the receptor leads to
CC       dimerization, internalization of the EGF-receptor complex,
CC       induction of the tyrosine kinase activity, stimulation of cell DNA
CC       synthesis, and cell proliferation.
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; X78987; CAA55587.1; -; mRNA.
DR   EMBL; U03425; AAA17899.1; -; mRNA.
DR   EMBL; X59698; CAA42219.1; -; mRNA.
DR   EMBL; L06864; AAA53029.1; -; mRNA.
DR   EMBL; Z12608; CAA78249.1; -; mRNA.
DR   IPI; IPI00121190; -.
DR   PIR; A53183; A53183.
DR   RefSeq; NP_997538.1; NM_207655.2.
DR   UniGene; Mm.420648; -.
DR   UniGene; Mm.439882; -.
DR   UniGene; Mm.8534; -.
DR   ProteinModelPortal; Q01279; -.
DR   SMR; Q01279; 26-636, 671-1020.
DR   DIP; DIP-5763N; -.
DR   MINT; MINT-143143; -.
DR   STRING; Q01279; -.
DR   PhosphoSite; Q01279; -.
DR   PRIDE; Q01279; -.
DR   Ensembl; ENSMUST00000020329; ENSMUSP00000020329; ENSMUSG00000020122.
DR   GeneID; 13649; -.
DR   KEGG; mmu:13649; -.
DR   UCSC; uc007ibo.1; mouse.
DR   CTD; 13649; -.
DR   MGI; MGI:95294; Egfr.
DR   eggNOG; roNOG15098; -.
DR   HOGENOM; HBG445128; -.
DR   HOVERGEN; HBG000490; -.
DR   InParanoid; Q01279; -.
DR   OMA; MRRRHIV; -.
DR   OrthoDB; EOG44MXR6; -.
DR   PhylomeDB; Q01279; -.
DR   BRENDA; 2.7.10.1; 244.
DR   NextBio; 284374; -.
DR   ArrayExpress; Q01279; -.
DR   Bgee; Q01279; -.
DR   CleanEx; MM_EGFR; -.
DR   Genevestigator; Q01279; -.
DR   GermOnline; ENSMUSG00000020122; Mus musculus.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0030139; C:endocytic vesicle; 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:0005006; F:epidermal growth factor receptor activity; IDA:MGI.
DR   GO; GO:0004716; F:receptor signaling protein tyrosine kinase activity; IEA:InterPro.
DR   GO; GO:0021795; P:cerebral cortex cell migration; IMP:MGI.
DR   GO; GO:0048546; P:digestive tract morphogenesis; IMP:MGI.
DR   GO; GO:0001892; P:embryonic placenta development; IMP:MGI.
DR   GO; GO:0001942; P:hair follicle development; IMP:MGI.
DR   GO; GO:0060571; P:morphogenesis of an epithelial fold; IMP:MGI.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR   GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
DR   GO; GO:0007435; P:salivary gland morphogenesis; IMP:MGI.
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; 4.
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   ATP-binding; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW   Golgi apparatus; Isopeptide bond; Kinase; Membrane;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Receptor; Repeat; Signal;
KW   Transferase; Transmembrane; Transmembrane helix;
KW   Tyrosine-protein kinase; Ubl conjugation.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25   1210       Epidermal growth factor receptor.
FT                                /FTId=PRO_0000016666.
FT   TOPO_DOM     25    647       Extracellular (Potential).
FT   TRANSMEM    648    670       Helical; (Potential).
FT   TOPO_DOM    671   1210       Cytoplasmic (Potential).
FT   REPEAT       75    300       Approximate.
FT   REPEAT      390    600       Approximate.
FT   DOMAIN      714    981       Protein kinase.
FT   NP_BIND     720    728       ATP (By similarity).
FT   COMPBIAS   1028   1071       Ser-rich.
FT   ACT_SITE    839    839       Proton acceptor (By similarity).
FT   BINDING     747    747       ATP (By similarity).
FT   SITE       1018   1018       Important for interaction with PIK3C2B
FT                                (By similarity).
FT   MOD_RES     680    680       Phosphothreonine; by PKC (By similarity).
FT   MOD_RES     695    695       Phosphothreonine (By similarity).
FT   MOD_RES     697    697       Phosphoserine (By similarity).
FT   MOD_RES     727    727       Phosphothreonine (By similarity).
FT   MOD_RES     871    871       Phosphotyrosine (By similarity).
FT   MOD_RES     980    980       Phosphotyrosine (By similarity).
FT   MOD_RES     993    993       Phosphoserine (By similarity).
FT   MOD_RES     995    995       Phosphothreonine (By similarity).
FT   MOD_RES     997    997       Phosphoserine (By similarity).
FT   MOD_RES    1000   1000       Phosphotyrosine (By similarity).
FT   MOD_RES    1018   1018       Phosphotyrosine (By similarity).
FT   MOD_RES    1028   1028       Phosphoserine (By similarity).
FT   MOD_RES    1039   1039       Phosphoserine (By similarity).
FT   MOD_RES    1041   1041       Phosphoserine (By similarity).
FT   MOD_RES    1043   1043       Phosphothreonine (By similarity).
FT   MOD_RES    1044   1044       Phosphoserine (By similarity).
FT   MOD_RES    1047   1047       Phosphoserine (By similarity).
FT   MOD_RES    1069   1069       Phosphotyrosine (By similarity).
FT   MOD_RES    1070   1070       Phosphoserine (By similarity).
FT   MOD_RES    1071   1071       Phosphoserine (By similarity).
FT   MOD_RES    1092   1092       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1110   1110       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1138   1138       Phosphotyrosine (By similarity).
FT   MOD_RES    1166   1166       Phosphoserine (By similarity).
FT   MOD_RES    1172   1172       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1197   1197       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   CARBOHYD    128    128       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    175    175       N-linked (GlcNAc...).
FT   CARBOHYD    196    196       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    352    352       N-linked (GlcNAc...).
FT   CARBOHYD    413    413       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    444    444       N-linked (GlcNAc...).
FT   CARBOHYD    528    528       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    568    568       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    603    603       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    623    623       N-linked (GlcNAc...) (Potential).
FT   DISULFID    190    199       By similarity.
FT   DISULFID    194    207       By similarity.
FT   DISULFID    215    223       By similarity.
FT   DISULFID    219    231       By similarity.
FT   DISULFID    232    240       By similarity.
FT   DISULFID    236    248       By similarity.
FT   DISULFID    251    260       By similarity.
FT   DISULFID    264    291       By similarity.
FT   DISULFID    295    307       By similarity.
FT   DISULFID    311    326       By similarity.
FT   DISULFID    329    333       By similarity.
FT   DISULFID    506    515       By similarity.
FT   DISULFID    510    523       By similarity.
FT   DISULFID    526    535       By similarity.
FT   DISULFID    539    555       By similarity.
FT   DISULFID    558    571       By similarity.
FT   DISULFID    562    579       By similarity.
FT   DISULFID    582    591       By similarity.
FT   DISULFID    595    617       By similarity.
FT   DISULFID    620    628       By similarity.
FT   DISULFID    624    636       By similarity.
FT   CROSSLNK    718    718       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK    739    739       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK    756    756       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK    869    869       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK    931    931       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK    972    972       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CONFLICT     19     19       C -> S (in Ref. 2).
FT   CONFLICT    539    539       C -> W (in Ref. 5; CAA42219).
FT   CONFLICT    991    991       L -> F (in Ref. 4; AAA17899).
FT   CONFLICT   1116   1117       HP -> DR (in Ref. 6).
SQ   SEQUENCE   1210 AA;  134853 MW;  690E20D46DF2D2F5 CRC64;
     MRPSGTARTT LLVLLTALCA AGGALEEKKV CQGTSNRLTQ LGTFEDHFLS LQRMYNNCEV
     VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP LENLQIIRGN ALYENTYALA
     ILSNYGTNRT GLRELPMRNL QEILIGAVRF SNNPILCNMD TIQWRDIVQN VFMSNMSMDL
     QSHPSSCPKC DPSCPNGSCW GGGEENCQKL TKIICAQQCS HRCRGRSPSD CCHNQCAAGC
     TGPRESDCLV CQKFQDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV
     VTDHGSCVRA CGPDYYEVEE DGIRKCKKCD GPCRKVCNGI GIGEFKDTLS INATNIKHFK
     YCTAISGDLH ILPVAFKGDS FTRTPPLDPR ELEILKTVKE ITGFLLIQAW PDNWTDLHAF
     ENLEIIRGRT KQHGQFSLAV VGLNITSLGL RSLKEISDGD VIISGNRNLC YANTINWKKL
     FGTPNQKTKI MNNRAEKDCK AVNHVCNPLC SSEGCWGPEP RDCVSCQNVS RGRECVEKCN
     ILEGEPREFV ENSECIQCHP ECLPQAMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGIM
     GENNTLVWKY ADANNVCHLC HANCTYGCAG PGLQGCEVWP SGPKIPSIAT GIVGGLLFIV
     VVALGIGLFM RRRHIVRKRT LRRLLQEREL VEPLTPSGEA PNQAHLRILK ETEFKKIKVL
     GSGAFGTVYK GLWIPEGEKV KIPVAIKELR EATSPKANKE ILDEAYVMAS VDNPHVCRLL
     GICLTSTVQL ITQLMPYGCL LDYVREHKDN IGSQYLLNWC VQIAKGMNYL EDRRLVHRDL
     AARNVLVKTP QHVKITDFGL AKLLGAEEKE YHAEGGKVPI KWMALESILH RIYTHQSDVW
     SYGVTVWELM TFGSKPYDGI PASDISSILE KGERLPQPPI CTIDVYMIMV KCWMIDADSR
     PKFRELILEF SKMARDPQRY LVIQGDERMH LPSPTDSNFY RALMDEEDME DVVDADEYLI
     PQQGFFNSPS TSRTPLLSSL SATSNNSTVA CINRNGSCRV KEDAFLQRYS SDPTGAVTED
     NIDDAFLPVP EYVNQSVPKR PAGSVQNPVY HNQPLHPAPG RDLHYQNPHS NAVGNPEYLN
     TAQPTCLSSG FNSPALWIQK GSHQMSLDNP DYQQDFFPKE TKPNGIFKGP TAENAEYLRV
     APPSSEFIGA
//
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;
CC   -----------------------------------------------------------------------
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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   S30BP_MOUSE             Reviewed;         308 AA.
AC   Q02614; Q8VDJ5;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=SAP30-binding protein;
DE   AltName: Full=Transcriptional regulator protein HCNGP;
GN   Name=Sap30bp; Synonyms=Hcngp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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   TISSUE=Spleen;
RX   MEDLINE=93093334; PubMed=1459361;
RX   DOI=10.1111/j.1432-0436.1992.tb00697.x;
RA   Palmer D.B., McVey J.H., Robinson P.J., Dyson P.J.;
RT   "The chromatin structure of the mouse beta-2-microglobulin locus.";
RL   Differentiation 51:201-207(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
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: Induces cell death. May act as a transcriptional
CC       corepressor of a gene related to cell survival (By similarity).
CC       May be involved in the regulation of beta-2-microglobulin genes.
CC   -!- SUBUNIT: Interacts with SAP30 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the HCNGP family.
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DR   EMBL; X68061; CAA48198.1; -; mRNA.
DR   EMBL; AK147869; BAE28192.1; -; mRNA.
DR   EMBL; BC021757; AAH21757.1; -; mRNA.
DR   IPI; IPI00331167; -.
DR   PIR; S26660; S26660.
DR   RefSeq; NP_065229.2; NM_020483.3.
DR   UniGene; Mm.267810; -.
DR   ProteinModelPortal; Q02614; -.
DR   PhosphoSite; Q02614; -.
DR   PRIDE; Q02614; -.
DR   Ensembl; ENSMUST00000140991; ENSMUSP00000114844; ENSMUSG00000020755.
DR   GeneID; 57230; -.
DR   KEGG; mmu:57230; -.
DR   UCSC; uc007mjd.1; mouse.
DR   CTD; 57230; -.
DR   MGI; MGI:1927479; Sap30bp.
DR   eggNOG; roNOG09027; -.
DR   GeneTree; ENSGT00390000007870; -.
DR   HOGENOM; HBG715178; -.
DR   HOVERGEN; HBG051891; -.
DR   InParanoid; Q02614; -.
DR   OMA; IRIPPEP; -.
DR   OrthoDB; EOG48D0W8; -.
DR   PhylomeDB; Q02614; -.
DR   NextBio; 313509; -.
DR   ArrayExpress; Q02614; -.
DR   Bgee; Q02614; -.
DR   CleanEx; MM_SAP30BP; -.
DR   Genevestigator; Q02614; -.
DR   GermOnline; ENSMUSG00000020755; Mus musculus.
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   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR012479; HCNGP.
DR   PANTHER; PTHR13464; HCNGP; 1.
DR   Pfam; PF07818; HCNGP; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Nucleus; Phosphoprotein; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    308       SAP30-binding protein.
FT                                /FTId=PRO_0000083924.
FT   COMPBIAS    225    294       Thr-rich.
FT   MOD_RES      10     10       Phosphoserine (By similarity).
FT   MOD_RES      18     18       Phosphoserine (By similarity).
FT   MOD_RES      22     22       Phosphoserine (By similarity).
FT   MOD_RES      43     43       Phosphoserine (By similarity).
FT   MOD_RES      52     52       Phosphoserine (By similarity).
FT   MOD_RES     113    113       Phosphoserine (By similarity).
FT   CONFLICT     34     34       A -> R (in Ref. 1; CAA48198).
FT   CONFLICT    298    298       A -> T (in Ref. 1; CAA48198).
SQ   SEQUENCE   308 AA;  33832 MW;  4E36A6A4B58098FB CRC64;
     MAGKKNVLSS LAIYAEYSDP ESDGETGVDA VGGATEEKGG LVSDAYGEDD FSRPGGDEDG
     YEEEEDENSK QSEDDDSETE KPEADDPKDN TEAEKRDPQE LVASFSERVR NMSPDEIKIP
     PEPPGRCSNH LQDKIQKLYE RKIKEGMDMN YIIQRKKEFR NPSIYEKLIQ FCAIDELGTN
     YPKDMFDPHG WSEDSYYEAL AKAQKIEMDK LEKAKKERTK IEFVTGTKKG TTTNATATST
     STASTAVADA QKRKSKWDSA IPVTTIAQPT ILTTTATLPA VVTVTTSASG SKTTVISAVG
     TIVKKAKQ
//
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.
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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   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.
CC   -----------------------------------------------------------------------
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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   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.
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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   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   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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   LG3BP_MOUSE             Reviewed;         577 AA.
AC   Q07797; O35649; Q3U631; Q3U8K4; Q3UDL5;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Galectin-3-binding protein;
DE   AltName: Full=Cyp-C-associated protein;
DE            Short=CyCAP;
DE   AltName: Full=Lectin galactoside-binding soluble 3-binding protein;
DE   AltName: Full=Protein MAMA;
DE   Flags: Precursor;
GN   Name=Lgals3bp; Synonyms=Cycap, Mama;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, INTERACTION WITH
RP   PPIC, GLYCOSYLATION, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Bone marrow;
RX   MEDLINE=93342080; PubMed=8341703; DOI=10.1073/pnas.90.14.6815;
RA   Friedman J.S., Trahey M., Weissman I.L.;
RT   "Cloning and characterization of cyclophilin C-associated protein: a
RT   candidate natural cellular ligand for cyclophilin C.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:6815-6819(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Bone marrow macrophage;
RX   MEDLINE=94164889; PubMed=8119883;
RA   Chicheportiche Y., Vassalli P.;
RT   "Cloning and expression of a mouse macrophage cDNA coding for a
RT   membrane glycoprotein of the scavenger receptor cysteine-rich domain
RT   family.";
RL   J. Biol. Chem. 269:5512-5517(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, C57BL/6J, and NOD;
RC   TISSUE=Aorta, Bone marrow, Thymus, 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].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting 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=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: Promotes intergrin-mediated cell adhesion. May stimulate
CC       host defense against viruses and tumor cells (By similarity).
CC   -!- SUBUNIT: Homodimers and homomultimers. The multimers form ring-
CC       like structures with a diameter of 30-40 nm. Binds LGALS1 and
CC       LGALS3. Binds ITGB1, COL4A1, COL5A1, COL6A1, FN1 and NID (By
CC       similarity). Interacts with PPIC (in vitro).
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity). Secreted,
CC       extracellular space, extracellular matrix.
CC   -!- TISSUE SPECIFICITY: Detected in embryo, liver, spleen, kidney,
CC       lung, heart, intestine, thymus and lymph node.
CC   -!- INDUCTION: Up-regulated by TNF and IFNG.
CC   -!- PTM: N-glycosylated.
CC   -!- SIMILARITY: Contains 1 BACK (BTB/Kelch associated) domain.
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC   -!- SIMILARITY: Contains 1 SRCR 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; L16894; AAA37499.1; -; mRNA.
DR   EMBL; X67809; CAA48010.1; -; mRNA.
DR   EMBL; AK079915; BAC37782.1; -; mRNA.
DR   EMBL; AK137836; BAE23505.1; -; mRNA.
DR   EMBL; AK150021; BAE29246.1; -; mRNA.
DR   EMBL; AK152182; BAE31013.1; -; mRNA.
DR   EMBL; AK153313; BAE31894.1; -; mRNA.
DR   EMBL; AK153396; BAE31958.1; -; mRNA.
DR   EMBL; AK155031; BAE33003.1; -; mRNA.
DR   EMBL; AL591404; CAM23110.1; -; Genomic_DNA.
DR   EMBL; CH466558; EDL34661.1; -; Genomic_DNA.
DR   EMBL; CH466558; EDL34662.1; -; Genomic_DNA.
DR   EMBL; BC090658; AAH90658.1; -; mRNA.
DR   IPI; IPI00119809; -.
DR   PIR; A53202; A53202.
DR   RefSeq; NP_035280.1; NM_011150.2.
DR   UniGene; Mm.3152; -.
DR   HSSP; Q08380; 1BY2.
DR   ProteinModelPortal; Q07797; -.
DR   SMR; Q07797; 21-389.
DR   STRING; Q07797; -.
DR   PRIDE; Q07797; -.
DR   Ensembl; ENSMUST00000043722; ENSMUSP00000035579; ENSMUSG00000033880.
DR   GeneID; 19039; -.
DR   KEGG; mmu:19039; -.
DR   UCSC; uc007moz.1; mouse.
DR   CTD; 19039; -.
DR   MGI; MGI:99554; Lgals3bp.
DR   eggNOG; roNOG11068; -.
DR   GeneTree; ENSGT00530000063814; -.
DR   HOGENOM; HBG446242; -.
DR   HOVERGEN; HBG052323; -.
DR   InParanoid; Q07797; -.
DR   OMA; LDLYAYA; -.
DR   OrthoDB; EOG4B8JCN; -.
DR   PhylomeDB; Q07797; -.
DR   NextBio; 295485; -.
DR   ArrayExpress; Q07797; -.
DR   Bgee; Q07797; -.
DR   Genevestigator; Q07797; -.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0005044; F:scavenger receptor activity; TAS:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   InterPro; IPR011705; BACK.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR001190; Srcr_rcpt.
DR   InterPro; IPR017448; Srcr_rcpt-rel.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF07707; BACK; 1.
DR   Pfam; PF00530; SRCR; 1.
DR   PRINTS; PR00258; SPERACTRCPTR.
DR   SMART; SM00875; BACK; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00202; SR; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   SUPFAM; SSF56487; Srcr_receptor; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00420; SRCR_1; 1.
DR   PROSITE; PS50287; SRCR_2; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion; Direct protein sequencing; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Secreted; Signal.
FT   SIGNAL        1     18       Potential.
FT   CHAIN        19    577       Galectin-3-binding protein.
FT                                /FTId=PRO_0000357035.
FT   DOMAIN       24    124       SRCR.
FT   DOMAIN      153    221       BTB.
FT   DOMAIN      260    360       BACK.
FT   CARBOHYD     69     69       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    125    125       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    362    362       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    398    398       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    543    543       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    572    572       N-linked (GlcNAc...) (Potential).
FT   DISULFID     49    113       By similarity.
FT   DISULFID     62    123       By similarity.
FT   DISULFID     93    103       By similarity.
FT   CONFLICT     25     25       R -> G (in Ref. 1; AAA37499).
FT   CONFLICT    228    228       H -> P (in Ref. 1; AAA37499).
FT   CONFLICT    347    347       R -> C (in Ref. 3; BAE29246).
FT   CONFLICT    370    370       Q -> K (in Ref. 3; BAE31894).
FT   CONFLICT    465    465       D -> E (in Ref. 3; BAE31013).
FT   CONFLICT    466    467       KQ -> NE (in Ref. 1; AAA37499).
FT   CONFLICT    573    577       STDMV -> LH (in Ref. 1; AAA37499).
SQ   SEQUENCE   577 AA;  64491 MW;  9D4181A7BEC2BD7C CRC64;
     MALLWLLSVF LLVPGTQGTE DGDMRLVNGA SANEGRVEIF YRGRWGTVCD NLWNLLDAHV
     VCRALGYENA TQALGRAAFG PGKGPIMLDE VECTGTESSL ASCRSLGWMV SRCGHEKDAG
     VVCSNDTTGL HILDLSGELS DALGQIFDSQ QGCDLFIQVT GQGYEDLSLC AHTLILRTNP
     EAQALWQVVG SSVIMRVDAE CMPVVRDFLR YFYSRRIEVS MSSVKCLHKL ASAYGATELQ
     DYCGRLFATL LPQDPTFHTP LDLYAYARAT GDSMLEDLCV QFLAWNFEPL TQSESWSAVP
     TTLIQALLPK SELAVSSELD LLKAVDQWST ETIASHEDIE RLVEQVRFPM MLPQELFELQ
     FNLSLYQDHQ ALFQRKTMQA LEFHTVPVEV LAKYKGLNLT EDTYKPRLYT SSTWSSLVMA
     STWRAQRYEY NRYNQLYTYG YGSVARYNSY QSFQTPQHPS FLFKDKQISW SATYLPTMQS
     CWNYGFSCTS NELPVLGLTT SSYSNPTIGY ENRVLILCGG YSVVDVTSFE GSKAPIPTAL
     DTNSSKTPSL FPCASGAFSS FRVVIRPFYL TNSTDMV
//
ID   Q08EC2_MOUSE            Unreviewed;       877 AA.
AC   Q08EC2;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAR-2011, entry version 29.
DE   SubName: Full=Hk3 protein;
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   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 hexokinase family.
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DR   EMBL; BC117861; AAI17862.1; -; mRNA.
DR   IPI; IPI00798510; -.
DR   UniGene; Mm.267479; -.
DR   ProteinModelPortal; Q08EC2; -.
DR   SMR; Q08EC2; 33-871.
DR   STRING; Q08EC2; -.
DR   PRIDE; Q08EC2; -.
DR   Ensembl; ENSMUST00000123097; ENSMUSP00000116717; ENSMUSG00000025877.
DR   UCSC; uc007qps.1; mouse.
DR   MGI; MGI:2670962; Hk3.
DR   GeneTree; ENSGT00390000017159; -.
DR   HOVERGEN; HBG005020; -.
DR   PhylomeDB; Q08EC2; -.
DR   Bgee; Q08EC2; -.
DR   Genevestigator; Q08EC2; -.
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:InterPro.
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; 1.
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   877 AA;  95346 MW;  0B6AD9A42A4DFF99 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 LVQCVCVAVC TRAAQLCAAA LAAVLSRLQH SREQQTLQVA
     VATGGRVFER HPRRILEETL APFQLTLEQL TVVQAQMREA MIRGLQGEAS SLRMLPTYVR
     ATPDGSERGD FLALDLGGTN FRVLLVRVAE GSVQIINQVY SIPECRAQGS GQKLFDHIVD
     CIVDFQKRQG LSGQSLPLGF TFSFPCKQLG LDQGILLNWT KGFNASGCEG QDVVYLLREA
     IRRRQAVELN VVAIVNDTVG TMMSCGYDDP RCEMGLIVGT GTNACYMEEL RNVASVPGDS
     GLMCINMEWG AFGDDGSLGT LSTRFDTSVD QASINPGKQR FEKMISGMYL GEIVRHILLH
     LTNLGVLFRG QKTQCLQARD IFKTKFLSEI ESDSLALRQV RAILEDLGLT LTSDDALMVL
     EVCQAVSRRA AQLCGAGVAA VVEKIRENRG LQELTVSVGV DGTLYKLHPH FSKLVSATVR
     KLAPQCTVTF LQSEDGSGKG AALVTAVACR LTQMAHV
//
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   Q0IJ77_MOUSE            Unreviewed;       893 AA.
AC   Q0IJ77;
DT   03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2006, sequence version 1.
DT   08-FEB-2011, entry version 39.
DE   SubName: Full=Npas3 protein;
DE   Flags: Fragment;
GN   Name=Npas3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; 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 PAC (PAS-associated C-terminal) domain.
CC   -!- SIMILARITY: Contains 1 basic helix-loop-helix (bHLH) domain.
CC   -!- SIMILARITY: Contains 2 PAS (PER-ARNT-SIM) domains.
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DR   EMBL; BC120885; AAI20886.1; -; mRNA.
DR   IPI; IPI00137835; -.
DR   UniGene; Mm.247044; -.
DR   UniGene; Mm.466545; -.
DR   PRIDE; Q0IJ77; -.
DR   Ensembl; ENSMUST00000021396; ENSMUSP00000021396; ENSMUSG00000021010.
DR   UCSC; uc007nnp.1; mouse.
DR   MGI; MGI:1351610; Npas3.
DR   eggNOG; roNOG05628; -.
DR   HOVERGEN; HBG052656; -.
DR   InParanoid; Q0IJ77; -.
DR   ArrayExpress; Q0IJ77; -.
DR   Bgee; Q0IJ77; -.
DR   Genevestigator; Q0IJ77; -.
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; PS50112; PAS; 2.
PE   2: Evidence at transcript level;
KW   DNA-binding; Nucleus; Repeat; Transcription; Transcription regulation.
FT   NON_TER     893    893
SQ   SEQUENCE   893 AA;  96660 MW;  42E85B37F40BD128 CRC64;
     MGRAGAAANG TPQNVQGITS YQQRLQALRK EKSRDAARSR RGKENFEFYE LAKLLPLPAA
     ITSQLDKASI IRLTISYLKM RDFANQGDPP WNLRMEGPPP NTSVKVIGAQ RRRSPSALAI
     EVFEAHLGSH ILQSLDGFVF ALNQEGKFLY ISETVSIYLG LSQVELTGSS VFDYVHPGDH
     VEMAEQLGMK LPPGRGLLSQ GTTEDAASSA SSSSQSETPE PVETTSPSLL TTDNTLERSF
     FIRMKSTLTK RGVHIKSSGY KVIHITGRLR LRVSLSHGRT VPSQIMGLVV VAHALPPPTI
     NEVRIDCHMF VTRVNMDLNI IYCENRISDY MDLTPVDIVG KRCYHFIHAE DVEGIRHSHL
     DLLNKGQCVT KYYRWMQKNG GYIWIQSSAT IAINAKNANE KNIIWVNYLL SNPEYKDTPM
     DIAQLPHLPE KASESSETSD SESDSKDTSE DNENSKSDEK GNQSENSEDP EPDRKKSGSA
     CDNDMNCNDD GHSSSNPDSR DSDDSFEHSD FEHPKAAEDG FGALGPMQIK VERYVESEAD
     LRLQPCESLT SDSAKDSDSA NEAGAQASSK HQKRKRRRKR QKGGSASRRR LSSASSPGLD
     AGLVEPPRLL SSPHSASVLK IKTEIAEPIN FDNDSSIWNY PPNREISRNE SPYSMTKPPT
     SEHFPSPQGQ GGSSGGGGAL HVAIPDSVLT PPGADGTAGR KTQFSGTAPV PSDPLSPPLS
     ASPRDKHPGG GAGSGGGGPG ASNSLLYTGD LEALQRLQAG NVVLPLVHRV TGTLAATSTA
     AQRVYTTGTI RYAPAEVTLA MQGNLLPNAH AVNFVDVNSP GFGLDPKTPM EMLYHHVHRL
     NMSGPFGGAV SAASLTQMPG GNVFTTAEGL FSTLPFPVYS NGIHAAQTLE RKE
//
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   MDGA1_MOUSE             Reviewed;         940 AA.
AC   Q0PMG2;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   RecName: Full=MAM domain-containing glycosylphosphatidylinositol anchor protein 1;
DE   Flags: Precursor;
GN   Name=Mdga1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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 DISRUPTION PHENOTYPE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=16641224; DOI=10.1523/JNEUROSCI.4935-05.2006;
RA   Takeuchi A., O'Leary D.D.M.;
RT   "Radial migration of superficial layer cortical neurons controlled by
RT   novel Ig cell adhesion molecule MDGA1.";
RL   J. Neurosci. 26:4460-4464(2006).
RN   [2]
RP   TISSUE SPECIFICITY.
RX   PubMed=16959869; DOI=10.1093/cercor/bhl064;
RA   Takeuchi A., Hamasaki T., Litwack E.D., O'leary D.D.;
RT   "Novel IgCAM, MDGA1, expressed in unique cortical area- and layer-
RT   specific patterns and transiently by distinct forebrain populations of
RT   Cajal-Retzius neurons.";
RL   Cereb. Cortex 17:1531-1541(2007).
CC   -!- FUNCTION: Required for radial migration of cortical neurons in the
CC       superficial layer of the neocortex.
CC   -!- SUBUNIT: Interacts heterophilically through its MAM domain with
CC       proteins in axon-rich regions and through its Ig-like domains with
CC       proteins in differentiating muscle (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor (By
CC       similarity). Note=Associated with lipid rafts (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed by neurons in layers 2 and 3 of the
CC       cortex during their migration and settling in the cortical plate.
CC       Also found in layers 4 and 6a. From E9.5-E13.5, detected in the
CC       marginal zone of the developing cortex. At E16.5, modest
CC       expression is found in the intermediate zone. At postnatal day 0,
CC       evident in the superficial cortical plate. By postnatal day 7,
CC       expression is limited to layers 2 and 3 throughout most of the
CC       cortex.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the developing embryo and soon
CC       after birth but not detected in adults.
CC   -!- DISRUPTION PHENOTYPE: Mice display impaired migration of
CC       superficial layer cortical neurons with neurons found deep in the
CC       cortical plate or beneath it.
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC   -!- SIMILARITY: Contains 6 Ig-like (immunoglobulin-like) domains.
CC   -!- SIMILARITY: Contains 1 MAM domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; DQ788983; ABG78614.1; -; mRNA.
DR   IPI; IPI00408001; -.
DR   UniGene; Mm.40901; -.
DR   ProteinModelPortal; Q0PMG2; -.
DR   SMR; Q0PMG2; 46-132, 146-632, 737-904.
DR   STRING; Q0PMG2; -.
DR   PRIDE; Q0PMG2; -.
DR   Ensembl; ENSMUST00000066388; ENSMUSP00000067509; ENSMUSG00000043557.
DR   UCSC; uc008bto.1; mouse.
DR   MGI; MGI:1922012; Mdga1.
DR   eggNOG; roNOG12935; -.
DR   GeneTree; ENSGT00570000078878; -.
DR   HOVERGEN; HBG052403; -.
DR   OrthoDB; EOG447FSK; -.
DR   ArrayExpress; Q0PMG2; -.
DR   Bgee; Q0PMG2; -.
DR   Genevestigator; Q0PMG2; -.
DR   GO; GO:0046658; C:anchored to plasma membrane; ISS:UniProtKB.
DR   GO; GO:0001764; P:neuron migration; IDA:UniProtKB.
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; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR000998; MAM_dom.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 7.
DR   Pfam; PF07679; I-set; 6.
DR   Pfam; PF00629; MAM; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 5.
DR   SMART; SM00137; MAM; 1.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   SUPFAM; SSF49265; FN_III-like; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50835; IG_LIKE; 6.
DR   PROSITE; PS00740; MAM_1; FALSE_NEG.
DR   PROSITE; PS50060; MAM_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Developmental protein; Differentiation; Disulfide bond;
KW   Glycoprotein; GPI-anchor; Immunoglobulin domain; Lipoprotein;
KW   Membrane; Neurogenesis; Repeat; Signal.
FT   SIGNAL        1     18       Potential.
FT   CHAIN        19    917       MAM domain-containing
FT                                glycosylphosphatidylinositol anchor
FT                                protein 1.
FT                                /FTId=PRO_0000292926.
FT   PROPEP      918    940       Removed in mature form.
FT                                /FTId=PRO_0000292927.
FT   DOMAIN       24    123       Ig-like 1.
FT   DOMAIN      132    230       Ig-like 2.
FT   DOMAIN      240    323       Ig-like 3.
FT   DOMAIN      338    432       Ig-like 4.
FT   DOMAIN      440    532       Ig-like 5.
FT   DOMAIN      539    634       Ig-like 6.
FT   DOMAIN      622    724       Fibronectin type-III.
FT   DOMAIN      736    903       MAM.
FT   LIPID       917    917       GPI-anchor amidated serine (Potential).
FT   CARBOHYD     42     42       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    235    235       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    247    247       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    257    257       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    307    307       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    432    432       N-linked (GlcNAc...) (Potential).
FT   DISULFID     60    108       By similarity.
FT   DISULFID    157    214       By similarity.
FT   DISULFID    262    308       By similarity.
FT   DISULFID    357    415       By similarity.
FT   DISULFID    463    514       By similarity.
FT   DISULFID    560    616       By similarity.
SQ   SEQUENCE   940 AA;  104190 MW;  CCCDB0B724BC1152 CRC64;
     MEVTCLLLLA LIPFHCRGQG VYTPAQAQIV HAGQACVVKE DNISERVYTI RESDTLVLQC
     LVTGHPRPQV RWTKTAGSAS DKFQETSVFN ETLRIERIAR TQGGRYYCKA ENGVGVPAIK
     SIRVDVQYLD EPVLTVHQTV SDVRGNFYQE KTVFLRCTVS SNPPARFIWK RGSDTLSHSQ
     DNGVDIYEPL YTQGETKVLK LKNLRPQDYA SYTCQVSVRN VCGIPDKAIT FQLTNTTAPP
     ALKLSVNETL VVNPGENVTV QCLLTGGDPL PQLHWSHGPG PLPLGALAQG GTLSIPSVQA
     RDSGYYNCTA TNNVGNPAKK TVNLLVRSLK NATFQITPDM IKESENIQLG QDLKLSCHVD
     AVPQEKVNYQ WFKNGKPART SKRLLVTRND PELPAVTSSL ELIDLHFSDY GTYLCMASFP
     GSPVPDLSIE VNISSETVPP TISVPKGRAV VTVREGSPAE LQCEVRGKPR PPVLWSRVDK
     EAALLPSGLA LEETPDGKLR LESVSRDMSG TYRCQTARYN GFNVRPREAQ VQLTVHFPPE
     VEPSSQDVRQ ALGRPVLLRC SLLRGSPQRI ASAVWRFKGQ LLPPPPVLPA AAVETPDHAE
     LRLDALTRDS SGNYECSVSN DVGSATCLFQ VSVSHKLSKN YSYVLQWTQR EPDAVDPVLN
     YRLSIRQLNQ HNAMVKAIPV RRVEKGQLLE YILTDLRVPH SYEIRLTPYT TFGAGDMASR
     IIHYTEPINL PSLSDNTCHF EDEKICGYTQ DLTDNFDWTR QNALTQNPKR SPNTGPPTDI
     SGTPEGYYMF IETSRPRELG DRARLVSPLY NASAKFYCVS FFYHMYGKHI GSLNLLVRSR
     NKGTLDTHAW SLSGNKGNVW QQAHVPINPS GPFQIIFEGV RGSGYLGDIA IDDVTLKKGE
     CPRRQMDPNK VVVMPGSGAP RLSSLQLWGS MAIFLLALQR
//
ID   CTP5A_MOUSE             Reviewed;        1304 AA.
AC   Q0V8T9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   08-MAR-2011, entry version 35.
DE   RecName: Full=Contactin-associated protein like 5-1;
DE   AltName: Full=Cell recognition molecule Caspr5-1;
DE   AltName: Full=Cell recognition molecule Caspr5a;
DE   AltName: Full=Contactin-associated protein-like 5a;
DE   Flags: Precursor;
GN   Name=Cntnap5a; Synonyms=Caspr5-1;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting 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, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=16845472; DOI=10.1007/s00335-005-0157-1;
RA   Traut W., Weichenhan D., Himmelbauer H., Winking H.;
RT   "New members of the neurexin superfamily: multiple rodent homologues
RT   of the human CASPR5 gene.";
RL   Mamm. Genome 17:723-731(2006).
CC   -!- FUNCTION: May play a role in the correct development and proper
CC       functioning of the peripheral and central nervous system and be
CC       involved in cell adhesion and intercellular communication.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- TISSUE SPECIFICITY: Expressed in brain.
CC   -!- DEVELOPMENTAL STAGE: Expressed from E6 in brain.
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; AC098737; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC110160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC122189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC122812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC124547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC124690; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC132403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BN000865; CAJ55745.1; -; mRNA.
DR   IPI; IPI00750221; -.
DR   RefSeq; NP_001070893.1; NM_001077425.1.
DR   UniGene; Mm.337385; -.
DR   ProteinModelPortal; Q0V8T9; -.
DR   SMR; Q0V8T9; 29-528, 547-598, 797-943, 962-996.
DR   Ensembl; ENSMUST00000094621; ENSMUSP00000092205; ENSMUSG00000070695.
DR   GeneID; 636808; -.
DR   KEGG; mmu:636808; -.
DR   UCSC; uc007cia.1; mouse.
DR   CTD; 636808; -.
DR   MGI; MGI:3643623; Cntnap5a.
DR   eggNOG; maNOG22164; -.
DR   HOVERGEN; HBG057718; -.
DR   NextBio; 423786; -.
DR   Bgee; Q0V8T9; -.
DR   CleanEx; MM_CNTNAP5A; -.
DR   Genevestigator; Q0V8T9; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005102; F:receptor binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; IPR001969; Peptidase_aspartic_AS.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 5.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF02210; Laminin_G_2; 4.
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; FALSE_NEG.
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   2: Evidence at transcript level;
KW   Cell adhesion; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Membrane; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25   1304       Contactin-associated protein like 5-1.
FT                                /FTId=PRO_0000317378.
FT   TOPO_DOM     25   1236       Extracellular (Potential).
FT   TRANSMEM   1237   1257       Helical; (Potential).
FT   TOPO_DOM   1258   1304       Cytoplasmic (Potential).
FT   DOMAIN       25    174       F5/8 type C.
FT   DOMAIN      180    360       Laminin G-like 1.
FT   DOMAIN      367    544       Laminin G-like 2.
FT   DOMAIN      546    583       EGF-like 1.
FT   DOMAIN      584    790       Fibrinogen C-terminal.
FT   DOMAIN      791    956       Laminin G-like 3.
FT   DOMAIN      957    995       EGF-like 2.
FT   DOMAIN     1020   1198       Laminin G-like 4.
FT   COMPBIAS     44     47       Poly-Ser.
FT   COMPBIAS     52     55       Poly-Ser.
FT   CARBOHYD    282    282       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    496    496       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    622    622       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1057   1057       N-linked (GlcNAc...) (Potential).
FT   DISULFID    329    360       By similarity.
FT   DISULFID    512    544       By similarity.
FT   DISULFID    550    561       By similarity.
FT   DISULFID    555    570       By similarity.
FT   DISULFID    572    582       By similarity.
FT   DISULFID    929    956       By similarity.
FT   DISULFID    960    973       By similarity.
FT   DISULFID    967    982       By similarity.
FT   DISULFID    984    994       By similarity.
FT   DISULFID   1163   1198       By similarity.
SQ   SEQUENCE   1304 AA;  145711 MW;  5875C8DF4A92F814 CRC64;
     MDSVPRLNSV LTLVLSGLWH LGLTATNYNC DDPLSNFLSL KAFSSSSDIT GSSSSAQLNW
     RMGTGGWSPA DSNAQQWLQI DLQNRVEITA VATQGRYGSS DWVTSYRLMF SDTGHNWQPY
     NQEDSIWTFV GNMNSDSVVH HKLLHSVRAR FVRFVPLEWN PNGKIGMRVE AYGCSYRSDV
     ADFDGRSSLL YRFNQKTMST LKDVISLKFK SMQGDGVLFH GEGQRGDHIT LELQKGRLAL
     YLNLDDSKAR LSSTVPLVIL GSLLDDQHWH SVLLERVGKQ ANFTVDMNTQ HFRTKGDTDS
     LDIDYELSFG GIPVPSKPGT FLKKNFHGCI ENLYYNGVNI IDLAKRRKHQ IYSGNVTFSC
     SEPQIVPITF INSRSSYLML PGTPQIDGLS VSFQFRTWNE DGLLLSTELS EGSGTLLLIL
     EGGTLRLLIK KVARHGTEIL TGSGLNDGLW HSVSINARRN RVTLTLDNDA ASPAPDTSRI
     QIYSGKSYYF GGCPDNLTDS QCLNPIKAFQ GCMRLIFIDN QPKDLISVQQ GSLGSFSDLH
     IDLCSIKDRC LPNYCEHGGH CDQTWTTFYC NCSGTGYTGA TCHDSIYEQS CEVYRHRGHT
     AGFFYVDSDG SGPLGPLQVY CNITEDKIWM TVQHNNTELT RVQGSSPENP YSMTLNYGGS
     MEQLEALIDG SEYCEQEVIY HCRRSRLLNT PDGAPFTWWI GRSTERHPYW GGAVPGVQQC
     GCGLEESCLD SRHFCNCDAD IDEWANDTGL FSFKDHLPVT QIIIMDTNRT NSEAAWRIGP
     LRCYGDRHFW NAVSFSTEAS YLHFPTFHTE FSADISFFFK TTALSGVFLE NLGIKDFFRL
     EMSSPSEVTF AIDVGNGPIE LLVQSPYPLN DNQWHYIRAE TNLKETSLQV DNLPQSMREA
     SEGGHFRLQL NSQLFVGGTS SRQKGFLGCI RSLLLNGHKV DLEERAKVTS GVRPGCPGHC
     SSYGSNCHNG GKCVEKHTGY SCDCTNSPYE GPFCRKEISA LFDSGTSVTY MFQEPYPVTK
     NTSLSSSAIY TDLAPFKETI MLSFMTTQAP TLLLYLNFSS QNFLAILLSR NGSLQVRYRL
     SKDESHVFNM DTENLANRRV HQVKISRDGP ELSIQMDQQL FSYSFSPEVE FRTLRSLVLG
     KVTETLDLDP EVARANTLGF VGCLSSVQYN HIAPLKAALR HASIAPVTVQ KTLTESSCGS
     MVDSDVNAVT TVHSLSDSFG KTDDHEPLQN AVRSDSAVIG GVIAVVTFIT FCVIGIMTRF
     LYQHKQSHRT NQMKKEYPEN LDNSFRNEID LQNTATECKR EYFI
//
ID   Q0VGU4_MOUSE            Unreviewed;       617 AA.
AC   Q0VGU4;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   SubName: Full=MCG18019;
DE   SubName: Full=VGF nerve growth factor inducible;
GN   Name=Vgf; ORFNames=mCG_18019;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; 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, 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.
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; BC085134; AAH85134.1; -; mRNA.
DR   EMBL; BC138553; AAI38554.1; -; mRNA.
DR   EMBL; BC138554; AAI38555.1; -; mRNA.
DR   EMBL; CH466529; EDL19290.1; -; Genomic_DNA.
DR   IPI; IPI00378764; -.
DR   RefSeq; NP_001034474.1; NM_001039385.1.
DR   UniGene; Mm.389697; -.
DR   ProteinModelPortal; Q0VGU4; -.
DR   STRING; Q0VGU4; -.
DR   PhosphoSite; Q0VGU4; -.
DR   PRIDE; Q0VGU4; -.
DR   Ensembl; ENSMUST00000041543; ENSMUSP00000048273; ENSMUSG00000037428.
DR   GeneID; 381677; -.
DR   KEGG; mmu:381677; -.
DR   UCSC; uc009abl.1; mouse.
DR   CTD; 381677; -.
DR   MGI; MGI:1343180; Vgf.
DR   eggNOG; maNOG18061; -.
DR   GeneTree; ENSGT00390000017745; -.
DR   HOGENOM; HBG126508; -.
DR   HOVERGEN; HBG006806; -.
DR   InParanoid; Q0VGU4; -.
DR   OMA; EDKRSQE; -.
DR   OrthoDB; EOG4ZPDVP; -.
DR   NextBio; 402411; -.
DR   ArrayExpress; Q0VGU4; -.
DR   Bgee; Q0VGU4; -.
DR   Genevestigator; Q0VGU4; -.
DR   GO; GO:0005184; F:neuropeptide hormone activity; IMP:MGI.
DR   GO; GO:0006091; P:generation of precursor metabolites and energy; IMP:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0030073; P:insulin secretion; IGI:MGI.
DR   GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
DR   GO; GO:0009409; P:response to cold; IDA:MGI.
DR   GO; GO:0002021; P:response to dietary excess; IDA:MGI.
DR   GO; GO:0032868; P:response to insulin stimulus; IMP:MGI.
DR   GO; GO:0019953; P:sexual reproduction; IMP:MGI.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   617 AA;  68232 MW;  97E3598E7932EDE5 CRC64;
     MKTFTLPASV LFCFLLLIQG LGAAPPGRPD VFPPPLSSEH NGQVAEDAVS RPKDDGVPEV
     RAARNPEPQD QGELFQGVDP RALASVLLQA LDRPASPPSV PGGSQQGTPE EAAEALLTES
     VRSQTHSLPA PEIQAPAVAP PRPQTQDRDP EEDDRSEELE ALASLLQELR DFSPSNAKRQ
     QETAAAETET RTHTLTRVNL ESPGPERVWR ASWGEFQARV PERAPLPPPV PSQFQARMSE
     SAPLPETHQF GEGVSSPKTH LGETLTPLSK AYQSLGGPFP KVRRLEGSFL GGSEAGERLL
     QQGLAQVEAG RRQAEATRQA AAQEERLADL ASDLLLQYLL QGGARQRDLG GRELQETQQE
     RENEREEEAE QERRGGGEDD VGEEDEEAAE AEAEAEEAER ARQNALLFAE EEDGEAGAED
     KRSQEEAPGH RRKDAEGAEE GGEEDDDDEE MDPQTIDSLI ELSTKLHLPA DDVVSIIEEV
     EEKRKRKKNA PPEPVPPPRA APAPTHVRSP QPPPPAPARD ELPDWNEVLP PWDREEDEVF
     PPGPYHPFPN YIRPRTLQPP ASSRRRHFHH ALPPARHHPD LEAQARRAQE EADAEERRLQ
     EQEELENYIE HVLLHRP
//
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;
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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   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   HDX_MOUSE               Reviewed;         692 AA.
AC   Q14B70; Q14B69;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=Highly divergent homeobox;
GN   Name=Hdx;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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 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   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q14B70-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q14B70-2; Sequence=VSP_027709;
CC   -!- SIMILARITY: Contains 2 homeobox DNA-binding domains.
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DR   EMBL; BX539333; CAM14853.1; -; Genomic_DNA.
DR   EMBL; BX539333; CAM14854.1; -; Genomic_DNA.
DR   EMBL; BC116300; AAI16301.1; -; mRNA.
DR   EMBL; BC116301; AAI16302.1; -; mRNA.
DR   IPI; IPI00776189; -.
DR   IPI; IPI00830519; -.
DR   RefSeq; NP_001074018.1; NM_001080549.2.
DR   UniGene; Mm.246623; -.
DR   ProteinModelPortal; Q14B70; -.
DR   SMR; Q14B70; 3-67, 437-509.
DR   STRING; Q14B70; -.
DR   PRIDE; Q14B70; -.
DR   Ensembl; ENSMUST00000038472; ENSMUSP00000043482; ENSMUSG00000034551.
DR   GeneID; 245596; -.
DR   KEGG; mmu:245596; -.
DR   NMPDR; fig|10090.3.peg.22049; -.
DR   CTD; 245596; -.
DR   MGI; MGI:2685226; Hdx.
DR   eggNOG; roNOG10290; -.
DR   GeneTree; ENSGT00390000008591; -.
DR   HOGENOM; HBG444238; -.
DR   HOVERGEN; HBG095615; -.
DR   InParanoid; Q14B70; -.
DR   OMA; RQGTTKH; -.
DR   OrthoDB; EOG434W5J; -.
DR   PhylomeDB; Q14B70; -.
DR   NextBio; 386835; -.
DR   ArrayExpress; Q14B70; -.
DR   Bgee; Q14B70; -.
DR   CleanEx; MM_HDX; -.
DR   Genevestigator; Q14B70; -.
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   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 2.
DR   Pfam; PF00046; Homeobox; 1.
DR   SMART; SM00389; HOX; 2.
DR   SUPFAM; SSF46689; Homeodomain_like; 2.
DR   PROSITE; PS00027; HOMEOBOX_1; FALSE_NEG.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; DNA-binding; Homeobox; Nucleus; Repeat.
FT   CHAIN         1    692       Highly divergent homeobox.
FT                                /FTId=PRO_0000299488.
FT   DNA_BIND      3     63       Homeobox 1.
FT   DNA_BIND    437    500       Homeobox 2.
FT   COMPBIAS    117    120       Poly-Ser.
FT   VAR_SEQ       1     58       Missing (in isoform 2).
FT                                /FTId=VSP_027709.
SQ   SEQUENCE   692 AA;  76861 MW;  66D15D3E4B0E69AA CRC64;
     MNLRSVFTVE QQRILQRYYE NGMTNQSKNC FQLILQCAQE TKLDFSVVRT WVGNKRRKMS
     SKSCESGAAG TVSGTSLAAP DITVRNVVNI ARPSSQQSSW TSANNDVIVT GIYSPVSSSS
     KQGTTKHTNT QITEAHKIPI QKAANKNDTE LQLHIPVQRQ VAHCKNASVL LGEKTIILSR
     QTSVLNAGNS VYNHTKKSYG SSPVQASEMT VPQKPSVCQR PCKIEPVGIQ RSYKPEHAGL
     ASHNLCGQKP TIRDPCCRTQ NLEIREVFSL AVSDYPQRIL GGNSTQKPAS AEGTCLSIAM
     ETGDAEDEYA REEELASMGA QITSYSRFYE SGNSLRAENQ STNLPGPGRN LPNSQMVNIR
     DLSDNVLYQT RDYHLTPRTS LHTASSTMYS NTNPSRSNFS PHFVSSNQLR LSQNQNNYQI
     SGNLSVPWIT GCSRKRALQD RTQFSDRDLA TLKKYWDNGM TSLGSVCREK IEAVAIELNV
     DCEIVRTWIG NRRRKYRLMG IEVPPPRGGP ADFSEQPESG SLSALTPGEE AGPEVGEDND
     RNDEVSICLS EASSQEESNE LIPNETRAHK DEEHQAVSAD NVKIEIIDDE ESDMISNSEV
     EQENSLLDYK NEEVRFIENE LEIQKQKYFK LQSFVRNLIL AMKADDKDQQ QALLSDLPPE
     LEEMDCSHAS PDPDDTSLSV SSLSEKNASD SL
//
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;
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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.
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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   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   Q27YN9_MOUSE            Unreviewed;      2265 AA.
AC   Q27YN9;
DT   04-APR-2006, integrated into UniProtKB/TrEMBL.
DT   04-APR-2006, sequence version 1.
DT   08-MAR-2011, entry version 38.
DE   SubName: Full=T-type calcium channel alpha 1G subunit;
GN   Name=Cacna1g;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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; TISSUE=Inner ear;
RA   Nie L., Gratton M.A., Dinglasan J.N., Rodriguez-Contreras A.,
RA   Tsang P.H.T., Garcia J., Yamoah E.N.;
RT   "Identification of Cav3.1 Channels in the Sensory Epithelia of Inner
RT   Ear.";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; DQ317412; ABC47034.1; -; mRNA.
DR   IPI; IPI00649776; -.
DR   RefSeq; NP_001106284.1; NM_001112813.2.
DR   RefSeq; NP_033913.2; NM_009783.3.
DR   UniGene; Mm.29585; -.
DR   ProteinModelPortal; Q27YN9; -.
DR   STRING; Q27YN9; -.
DR   Ensembl; ENSMUST00000021234; ENSMUSP00000021234; ENSMUSG00000020866.
DR   Ensembl; ENSMUST00000107790; ENSMUSP00000103419; ENSMUSG00000020866.
DR   GeneID; 12291; -.
DR   KEGG; mmu:12291; -.
DR   CTD; 12291; -.
DR   MGI; MGI:1201678; Cacna1g.
DR   eggNOG; roNOG11835; -.
DR   HOVERGEN; HBG050764; -.
DR   ArrayExpress; Q27YN9; -.
DR   Bgee; Q27YN9; -.
DR   Genevestigator; Q27YN9; -.
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   2265 AA;  250728 MW;  C28C813415A77BED 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 RAGLLSSPVV 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 LEKKRRNLML DDVIASGSSA
     SAASEAQCKP YYSDYSRFRL LVHHLCTSHY LDLFITGVIG LNVVTMAMEH YQQPQILDEA
     LKICNYIFTV IFVLESVFKL VAFGFRRFFQ DRWNQLDLAI VLLSIMGITL EEIEVNASLP
     INPTIIRIMR VLRIARVLKL LKMAVGMRAL LDTVMQALPQ VGNLGLLFML LFFIFAALGV
     ELFGDLECDE THPCEGLGRH ATFRNFGMAF LTLFRVSTGD NWNGIMKDTL RDCDQESTCY
     NTVISPIYFV SFVLTAQFVL VNVVIAVLMK HLEESNKEAK EEAELEAELE LEMKTLSPQP
     HSPLGSPFLW PGVEGVNSPD SPKPGAPHTT AHIGAASSGF SLEHPTMVPH TEEGPVPLGP
     DLLTVRKSGV SRTHSLPNDS YMCRNGSTAE RSLGHRGWGL PKAQSGSILS VHSQPADTSC
     ILQLPKDAHY LLQPHGAPTW GAIPKLPPPG RSPLAQRPLR RQAAIRTDSL DVQGLGSRED
     LLSEVSGPSC PLTRSSSFWG GSSIQVQQRS GSQSKVSKHI RLPAPCPGLE PSWAKDPQET
     RSSLELDTEL SWISGDLLPS SQEEPLSPRD LKKCYSVEAQ SCRRRPGSWL DEQRRHSIAV
     SCLDSGSQPR LCPSPSSLGG QPLGGPGSRP KKKLSPPSIS IDPPESQGPR PPCSPGVCLR
     RRAPASDSKD PSASSPLDST AASPSPKKDA LSLSGLSSDP TDLDP
//
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;
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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   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   FILA2_MOUSE             Reviewed;        2362 AA.
AC   Q2VIS4; Q8CB36;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   08-MAR-2011, entry version 44.
DE   RecName: Full=Filaggrin-2;
DE            Short=FLG-2;
DE   AltName: Full=Intermediate filament-associated protein;
GN   Name=Flg2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; 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   Listwan P., Rothnagel J.A.;
RT   "FLG-2, a novel repetitive protein that is abundantly expressed in
RT   mammalian epidermis and functionally related to filaggrin.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2047-2362.
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; THR-115; SER-168;
RP   SER-968; SER-974; SER-975; SER-1042; SER-1049; SER-1055; SER-1438;
RP   SER-1439; SER-1666; SER-1672; SER-1673; SER-1980; SER-1986; SER-1987;
RP   SER-1993; SER-2231 AND SER-2241, 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 S100-fused protein family.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the S-100
CC       family.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
CC   -!- SIMILARITY: Contains 12 filaggrin repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC29615.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; DQ118292; AAZ99028.1; -; Genomic_DNA.
DR   EMBL; AK036878; BAC29615.1; ALT_INIT; mRNA.
DR   IPI; IPI00406870; -.
DR   RefSeq; NP_001013826.1; NM_001013804.1.
DR   UniGene; Mm.10755; -.
DR   HSSP; P24480; 1NSH.
DR   ProteinModelPortal; Q2VIS4; -.
DR   SMR; Q2VIS4; 1-93.
DR   STRING; Q2VIS4; -.
DR   PhosphoSite; Q2VIS4; -.
DR   PRIDE; Q2VIS4; -.
DR   Ensembl; ENSMUST00000098884; ENSMUSP00000096482; ENSMUSG00000049133.
DR   GeneID; 229574; -.
DR   KEGG; mmu:229574; -.
DR   CTD; 229574; -.
DR   MGI; MGI:3645678; Flg2.
DR   eggNOG; maNOG16233; -.
DR   GeneTree; ENSGT00530000063634; -.
DR   InParanoid; Q2VIS4; -.
DR   OrthoDB; EOG4RJG10; -.
DR   ArrayExpress; Q2VIS4; -.
DR   Genevestigator; Q2VIS4; -.
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; IPR001751; S100/CaBP-9k_CS.
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; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS00303; S100_CABP; 1.
PE   1: Evidence at protein level;
KW   Calcium; Phosphoprotein; Repeat.
FT   CHAIN         1   2362       Filaggrin-2.
FT                                /FTId=PRO_0000331455.
FT   DOMAIN        8     43       EF-hand 1.
FT   DOMAIN       49     84       EF-hand 2.
FT   REPEAT      261    308       Filaggrin 1.
FT   REPEAT      373    414       Filaggrin 2.
FT   REPEAT      555    607       Filaggrin 3.
FT   REPEAT      672    723       Filaggrin 4.
FT   REPEAT      880    927       Filaggrin 5.
FT   REPEAT      984   1035       Filaggrin 6.
FT   REPEAT     1165   1210       Filaggrin 7.
FT   REPEAT     1280   1334       Filaggrin 8.
FT   REPEAT     1474   1522       Filaggrin 9.
FT   REPEAT     1723   1756       Filaggrin 10.
FT   REPEAT     2016   2070       Filaggrin 11.
FT   REPEAT     2218   2259       Filaggrin 12.
FT   CA_BIND      62     73       Potential.
FT   REGION        1     81       S-100-like (By similarity).
FT   COMPBIAS    110    120       Poly-Glu.
FT   COMPBIAS    265    911       Ser-rich.
FT   COMPBIAS    994   1970       Gln-rich.
FT   MOD_RES     113    113       Phosphoserine.
FT   MOD_RES     115    115       Phosphothreonine.
FT   MOD_RES     168    168       Phosphoserine.
FT   MOD_RES     968    968       Phosphoserine.
FT   MOD_RES     974    974       Phosphoserine.
FT   MOD_RES     975    975       Phosphoserine.
FT   MOD_RES    1042   1042       Phosphoserine.
FT   MOD_RES    1049   1049       Phosphoserine.
FT   MOD_RES    1055   1055       Phosphoserine.
FT   MOD_RES    1438   1438       Phosphoserine.
FT   MOD_RES    1439   1439       Phosphoserine.
FT   MOD_RES    1666   1666       Phosphoserine.
FT   MOD_RES    1672   1672       Phosphoserine.
FT   MOD_RES    1673   1673       Phosphoserine.
FT   MOD_RES    1980   1980       Phosphoserine.
FT   MOD_RES    1986   1986       Phosphoserine.
FT   MOD_RES    1987   1987       Phosphoserine.
FT   MOD_RES    1993   1993       Phosphoserine.
FT   MOD_RES    2231   2231       Phosphoserine.
FT   MOD_RES    2241   2241       Phosphoserine.
FT   CONFLICT   2118   2118       N -> H (in Ref. 1; AAZ99028).
SQ   SEQUENCE   2362 AA;  251372 MW;  F3FB473737052808 CRC64;
     MAYLLRSVVT IIDVFYKYTK QDEECGTLSK DELKELLEKE FRPILKNPDD PDTVDVIMHM
     LDRDHDRRLD FTEFILMIFK LALACNKVLG KEYCKASGSK KHRRGHQHQE EESETEEEEE
     TPRQKSGFRF SSWSEGEEHG HSSGGSRGPA KHRRGSNSKR LERQDELSSS EESRKKHHGS
     IFGHSWSSNK EKDGSRSEEL GEKGDKSYDS PSRESEEEYE SGYRLNHQGR EGHSGLSCGL
     EKNKYELNYI QLRKGGEQKL GYNTSSSGNS KIQSHVYGFS NSSGCCRPKN ASSSCQASRS
     QGQGNQSCRT QSNCQSGTSG GQGYGCVSEG QSSRCCQPKP RSCSQSSSQR GYGSKQCGQP
     QNCGRQQRMG SSHSSCCGPY GSGATQSSGC GQQRMSSCGH SSSSHQKGCS SNGFSKGDQR
     ASGSGHSSCC EQHGTNSSQS SGFKQHGHES GQSCCGQHGT ASSQSSGYSQ HRVGSGQSCH
     YGQHGSSSGQ SSSSGRHGSG SGQSSSSRHN RSGSSQSSGL EEHGSSSHQS HSSGHHGSGS
     RQSSGSEQHG AVSGQSSGSG KHETGPSQSS SSGHHGSGSQ QHGGGSGQST GFGEHESSSG
     HSSSSGQHRS GSRHSSGSGK HESGRSQSSG SGHHGSGSQQ HGGGSGNSTG FGEHGSSSHP
     LPSSGQNESS SGQSSRSERH GTGSGQSSGF GQHGSGSHQS SSSGHNEYGS GQTSSSWPHG
     KGSGQESGYG EQESGHGQSS SSWQHGTGPG QSSSSEEEES RPGQSSSSWQ HGKGSGQESG
     YGEQEAGHGQ SSSSWQHGTG AGNQSSGYGE HKSGPSHSSR SWHHGTGSGQ SLGFGQHGKG
     SHQSESSGHY ESVSEPSSSS WQHGNGSGES YGYGEHESGH GQSSSAWNHG NESGQSNGYG
     EHESGHGQSS SAWNHGNESG QSNGFGENES GRDQEGYQQR ESFHGQHRHP LSQHEQHSQF
     GYGRSPRSPV HPESSEGEEH SVVPRRYSGY GHGQGQAGHQ QRESGYGQRG RPQGPSQDSS
     RQPQAGHGQP SQSGYGRSPR RSQVHPEYSE GEAHSEVSQR HSGSSHCHCH CHGQARHQQR
     ESVHGQRGRP QGPSQDSSRH PQAGPGQPSQ SGSRRSPRSQ PVHPESSEGE EHSVVPQRHS
     GSGHGHGQGQ GQAGHQQRES VHGQQGRPQG PSQDSSRQPQ AGQGQPSQSG SGRSPRRSPV
     HPESSEGEEH SVVPQRHSGS GHGHGQGQGQ GQAGHQQRES VHGQRSRPQG PFQDSSRQPQ
     AGQGQPSQSG SGRSPRRSPV HPESSEGEEH SVVPQRHSGS GHGHGQGQGQ AGHQQRESVH
     GQPVRPEVPT QDSSRQPQAG QGQPSQSGSG RSPRRSPVHP ESSEGEEHSV VPQRNSESCH
     CHCHDQAGHQ QRESVHGQRG RPQGPSQDSS RHPQAGPGQP SQSGSRRSPR SSPVHPESSE
     GEEHSVVPQR HSGSGHGHGQ GQGQAGHQQR ESVHGQRGRP QGPTQDSSRQ PQAGQGQPSQ
     SGSGRSPRRS PVHPESSEGE EHSVVPQRHS GSGHGHGHGQ GQGQAGHQQR ESVHGQRGRP
     QGPSQDSSRQ PQAGQGQPSQ SGSGRSPRRS PVHPESSEGE EHSVVPQRYS GSGHGHGQGQ
     AGHQQRESVH GQRGRPQGPS QDSSRQPQAG QGQPSQSGSG RSPRRSPVHP ESSEGEEHSV
     IPQRHSGSGH SHGQGQVHAE HQQRESVHGQ RGRPQGPSQD SSRQPQAGQG QPSLSGSGRS
     PRRSPVHPES SEGEEHSVVP QRHSHSESGH GHGQGQGQAG HQQRESVHGQ RGRPQGPSQD
     SSRQPQAGQG QPSQSGSGRS PGRSPVHPES SEGEEHSVVP QRHSESGHGH GQGQGQAGHQ
     QRESVHGQRG RPQGPSQDSS RQPQAGQGQP SQSGSGRSPR RSPVHPESSE GEEHSVVPQR
     HSGSGHGHGQ GQGQAGHQQR ESVHGQPVRP QGPSQDSSSQ PQASQGQPSQ SGSGRSPRRS
     PVHPESSEGE EHSVVPQRHS GSGHGHGQGQ GQAGHQQRES LHGQRGRSQS PFHPSHSIHW
     QSKCTISKKS SRLSGHYGRN HFQSTISGNQ YDSSQSSRHG SYGPQDYDYG QSGYGPSGRL
     RSNSQSSIPF SSAHRATNME VLPCGQSFSP SDHVGTKANE QIGELVFKYR ESETGPDQSV
     DYYNLTESNS TTRGHECSHG HSVVVPEHSD DSDFNYGHSY NGKQQICQSQ PTVQSCFDDS
     QYILFQKHLE SPSFGNQSGF SPNERQLYTC NESIDSYHLS SDSNNRNQIY SSNNSFPNLY
     CIGTEQCIYL PSATILGEGT EGQEPGYTQP GTICKYNQFL DGRKSRTRGN HETGKMKSGS
     AYLDSNTPLY TYVQEQKSYY FE
//
ID   Q32P04_MOUSE            Unreviewed;       580 AA.
AC   Q32P04;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 2.
DT   08-MAR-2011, entry version 49.
DE   SubName: Full=Keratin 5;
GN   Name=Krt5; ORFNames=mCG_144997;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; 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.
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 intermediate filament family.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC108361; AAI08362.2; -; mRNA.
DR   EMBL; CH466550; EDL04029.1; -; Genomic_DNA.
DR   IPI; IPI00139301; -.
DR   RefSeq; NP_081287.1; NM_027011.2.
DR   UniGene; Mm.451847; -.
DR   ProteinModelPortal; Q32P04; -.
DR   SMR; Q32P04; 160-197, 205-311, 328-398, 419-473.
DR   STRING; Q32P04; -.
DR   PRIDE; Q32P04; -.
DR   Ensembl; ENSMUST00000023709; ENSMUSP00000023709; ENSMUSG00000061527.
DR   GeneID; 110308; -.
DR   KEGG; mmu:110308; -.
DR   CTD; 110308; -.
DR   MGI; MGI:96702; Krt5.
DR   eggNOG; roNOG05657; -.
DR   HOVERGEN; HBG013015; -.
DR   InParanoid; Q32P04; -.
DR   OMA; FGRVSLG; -.
DR   PhylomeDB; Q32P04; -.
DR   NextBio; 363739; -.
DR   ArrayExpress; Q32P04; -.
DR   Bgee; Q32P04; -.
DR   Genevestigator; Q32P04; -.
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   2: Evidence at transcript level;
KW   Coiled coil; Intermediate filament; Keratin.
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   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).
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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   Q3TDH2_MOUSE            Unreviewed;       847 AA.
AC   Q3TDH2;
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;
DE   SubName: Full=RIKEN cDNA 4931406P16, isoform CRA_b;
GN   Name=4931406P16Rik; ORFNames=mCG_17486;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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.
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.
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DR   EMBL; AK170198; BAE41629.1; -; mRNA.
DR   EMBL; CH466618; EDL03040.1; -; Genomic_DNA.
DR   IPI; IPI00467793; -.
DR   UniGene; Mm.479525; -.
DR   Ensembl; ENSMUST00000085592; ENSMUSP00000082730; ENSMUSG00000066571.
DR   Ensembl; ENSMUST00000108074; ENSMUSP00000103709; ENSMUSG00000066571.
DR   UCSC; uc009gja.1; mouse.
DR   MGI; MGI:1924311; 4931406P16Rik.
DR   eggNOG; roNOG10998; -.
DR   HOVERGEN; HBG057618; -.
DR   InParanoid; Q3TDH2; -.
DR   OrthoDB; EOG4BCDM8; -.
DR   ArrayExpress; Q3TDH2; -.
DR   Bgee; Q3TDH2; -.
DR   Genevestigator; Q3TDH2; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   847 AA;  92380 MW;  AA016E22FCB551A4 CRC64;
     MGHTPELEEA VRSWRGAAEA TSRLRERGCD GCLAGIEVQQ LFCSQSAAIP EHQLKELNIK
     IDSALQAYKI ALESLGHCEY AMKAGFHLNP KAIEASLQGC CSEAEAQQTG RRQTPPQPMQ
     CELPTVPVQI GSHFLKGVSF NESAADNLKL KTHTMLQLIK EAGCYNGITP RDDLPVTEVL
     NQVCPSMWRG ACKTAVQLLF GQAGLVVVDT AQIENKEAYA PQISLEGSRI VVQVPSTWCL
     KEDPATMSLL QRSLDPEKTL GLVDVLYTAV LDLNRWRTGR EQALPCIQIQ LQRDICDFGN
     QADLPSGNGS KSSGLQKTFS KLTSRFTKKV SCTNSGSTHY SKNIFTAGCS EEKAKMMGNN
     IDTRLQSILN IGNFPRTTDP SQSSQNSSNP MVNGFLLERR ENFLHGDDGK DEKGMNLPTD
     QEMQEVIDFL SGFNMGQSHQ GSPLVTRRNS TATAMVTEQK TGTMQPQQPS LPLAPPLRPP
     QAGAHTPLAA QQGLAPQQQS PKQQQPQVQY YQHLLQPIGS QQTPPQPRAP AKWVHGSSQH
     PSQPMAAGLS PLGQWPGISD LSSDLYSLGL VSSYMDNMMS EVLGQKPQGP RNNTWPNRDQ
     SDGVFGMLGE ILPFDPAVGS DPEFARYVAG VSQAMQQKRQ AQHGRRPGNP RGNWPPMEDA
     HRTWPLPEFF TEGDSLHSGW SGAQGDSASS SDETSSANGD SLFSMFSGPD LVAAVKQRRK
     HSSGEQETST LPSPPLLTTV EDVNQDNKTK TWPPKAPWQH PSPMPSTLPS PVAPLYAVAS
     PGSQWNDTMQ MLQSPVWAAA NDCNTTSFTY VQTPPQPPPP PAHKAAPKGF KAFPGKAERR
     PAYLPQY
//
ID   MPZL1_MOUSE             Reviewed;         270 AA.
AC   Q3TEW6; Q2VW02; Q6GQX5;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Myelin protein zero-like protein 1;
DE   AltName: Full=Protein zero-related;
DE   Flags: Precursor;
GN   Name=Mpzl1; Synonyms=Pzr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; 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=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 [MRNA] (ISOFORMS 1 AND 2).
RA   Roubelakis M.G., Martin-Rendon E., Tsaknakis G., Watt S.M.;
RT   "The murine ortholog of the SHP-2 binding molecule, PZR, is expressed
RT   during mesodermal commitment and accelerates cell migration on
RT   fibronectin.";
RL   Submitted (SEP-2004) 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   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: Cell surface receptor, which is involved in signal
CC       transduction processes. Recruits PTPN11/SHP-2 to the cell membrane
CC       and is a putative substrate of PTPN11/SHP-2. Is a major receptor
CC       for concanavalin-A (ConA) and is involved in cellular signaling
CC       induced by ConA, which probably includes Src family tyrosine-
CC       protein kinases. Isoform 2 seems to have a dominant negative role;
CC       it blocks tyrosine phosphorylation of MPZL1 induced by ConA.
CC       Isoform 1, but not isoform 2, may be involved in regulation of
CC       integrin-mediated cell motility (By similarity).
CC   -!- SUBUNIT: Interacts with phosphorylated PTPN11/SHP-2 (By
CC       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=Q3TEW6-1; Sequence=Displayed;
CC       Name=2; Synonyms=b;
CC         IsoId=Q3TEW6-2; Sequence=VSP_019345;
CC   -!- DOMAIN: Contains 2 copies of a cytoplasmic motif that is referred
CC       to as the immunoreceptor tyrosine-based inhibitor motif (ITIM).
CC       This motif is involved in modulation of cellular responses. The
CC       phosphorylated ITIM motif can bind the SH2 domain of several SH2-
CC       containing phosphatases.
CC   -!- PTM: Phosphorylated on tyrosine residues upon stimulation with
CC       pervanadate and concanavalin-A (ConA). Phosphorylation at Tyr-242
CC       and Tyr-264 is required for interaction with PTPN11/SHP-2.
CC       Dephosphorylated by PTPN11/SHP-2 (in vitro) (By similarity).
CC   -!- SIMILARITY: Belongs to the myelin P0 protein family.
CC   -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC       domain.
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DR   EMBL; AK169385; BAE41132.1; -; mRNA.
DR   EMBL; AY764247; AAX11678.1; -; mRNA.
DR   EMBL; AY764248; AAX11679.1; -; mRNA.
DR   EMBL; BC072563; AAH72563.1; -; mRNA.
DR   IPI; IPI00620858; -.
DR   IPI; IPI00761717; -.
DR   RefSeq; NP_001001880.1; NM_001001880.2.
DR   RefSeq; NP_001077366.1; NM_001083897.1.
DR   UniGene; Mm.46438; -.
DR   ProteinModelPortal; Q3TEW6; -.
DR   SMR; Q3TEW6; 38-204.
DR   STRING; Q3TEW6; -.
DR   PhosphoSite; Q3TEW6; -.
DR   PRIDE; Q3TEW6; -.
DR   Ensembl; ENSMUST00000068705; ENSMUSP00000070343; ENSMUSG00000026566.
DR   Ensembl; ENSMUST00000111435; ENSMUSP00000107062; ENSMUSG00000026566.
DR   GeneID; 68481; -.
DR   KEGG; mmu:68481; -.
DR   UCSC; uc007djh.1; mouse.
DR   UCSC; uc007dji.1; mouse.
DR   CTD; 68481; -.
DR   MGI; MGI:1915731; Mpzl1.
DR   eggNOG; roNOG16621; -.
DR   GeneTree; ENSGT00530000062830; -.
DR   HOGENOM; HBG443550; -.
DR   HOVERGEN; HBG104511; -.
DR   InParanoid; Q3TEW6; -.
DR   OMA; YTGCSTS; -.
DR   OrthoDB; EOG4HX51X; -.
DR   PhylomeDB; Q3TEW6; -.
DR   NextBio; 327262; -.
DR   ArrayExpress; Q3TEW6; -.
DR   Bgee; Q3TEW6; -.
DR   CleanEx; MM_MPZL1; -.
DR   Genevestigator; Q3TEW6; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
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   InterPro; IPR000920; Myelin_P0.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF07686; V-set; 1.
DR   PRINTS; PR00213; MYELINP0.
DR   SMART; SM00406; IGv; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Phosphoprotein; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     35       Potential.
FT   CHAIN        36    270       Myelin protein zero-like protein 1.
FT                                /FTId=PRO_0000240336.
FT   TOPO_DOM     36    162       Extracellular (Potential).
FT   TRANSMEM    163    183       Helical; (Potential).
FT   TOPO_DOM    184    270       Cytoplasmic (Potential).
FT   DOMAIN       36    151       Ig-like V-type.
FT   MOTIF       240    245       ITIM motif 1.
FT   MOTIF       262    267       ITIM motif 2.
FT   MOD_RES     204    204       Phosphoserine (By similarity).
FT   MOD_RES     210    210       Phosphoserine (By similarity).
FT   MOD_RES     221    221       Phosphoserine (By similarity).
FT   MOD_RES     242    242       Phosphotyrosine (By similarity).
FT   MOD_RES     261    261       Phosphoserine (By similarity).
FT   MOD_RES     264    264       Phosphotyrosine (By similarity).
FT   CARBOHYD     50     50       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    130    130       N-linked (GlcNAc...).
FT   DISULFID     58    135       By similarity.
FT   VAR_SEQ     203    270       CSTSERLSPVKQAPRKCPSDTEGLVKSPPSAGSHQGPVIYA
FT                                QLDHSGGHHSGKINKSESVVYADIRKD -> AQSFT (in
FT                                isoform 2).
FT                                /FTId=VSP_019345.
FT   CONFLICT    202    202       G -> GFIS (in Ref. 2; AAX11678).
SQ   SEQUENCE   270 AA;  29495 MW;  1E033F0F5F732C22 CRC64;
     MAEAVGAVAL IAAPARRRWL WSVLAAMLGL LTARISALEV HTPKEIFVVN GTQGKLTCTF
     DSPNTTGWLT TVSWSFQPDG TDSAVSFFHY SQGQVYIGDY PPFKDRVTWA GDLDKKDASI
     NIENIQAVHN GTYICDVKNP PDIVVRPGHI RLHVVEIDNL LVFLVWVVVG TVTAVVLGLT
     LLISLVLVVL YRRKHSKRDY TGCSTSERLS PVKQAPRKCP SDTEGLVKSP PSAGSHQGPV
     IYAQLDHSGG HHSGKINKSE SVVYADIRKD
//
ID   Q3THL7_MOUSE            Unreviewed;       283 AA.
AC   Q3THL7;
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=Vdac1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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; AK168225; BAE40179.1; -; mRNA.
DR   IPI; IPI00122549; -.
DR   UniGene; Mm.3555; -.
DR   UniGene; Mm.470023; -.
DR   STRING; Q3THL7; -.
DR   Ensembl; ENSMUST00000020673; ENSMUSP00000020673; ENSMUSG00000020402.
DR   Ensembl; ENSMUST00000102758; ENSMUSP00000099819; ENSMUSG00000020402.
DR   Ensembl; ENSMUST00000109065; ENSMUSP00000104693; ENSMUSG00000020402.
DR   MGI; MGI:106919; Vdac1.
DR   eggNOG; roNOG10550; -.
DR   HOVERGEN; HBG054036; -.
DR   InParanoid; Q3THL7; -.
DR   OrthoDB; EOG4T4CVZ; -.
DR   ArrayExpress; Q3THL7; -.
DR   Bgee; Q3THL7; -.
DR   Genevestigator; Q3THL7; -.
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   283 AA;  30756 MW;  D32B05B6A6D7593C CRC64;
     MAVPPTYADL GKSARDVFTK GYGFGLIKLD LKTKSENGLE FTSSGSANTE TTKVNGSLET
     KYRWTEYGLT FTEKWNTDNT LGTEITVEDQ LARGLKLTFD SSFSPNTGKK NAKIKTGYKR
     EHINLGCDVD FDIAGPSIRG ALVLGYEGWL AGYQMNFETS KSRVTQSNFA VGYKTDEFQL
     HTNVNDGTEF GGSIYQKVNK KLETAVNLAW TAGNSNTRFG IAAEYQVDPD ACFSAKVNNS
     SLIGLGYTQT LKPGIKLTLS ALLDGKNVNA GGHKLGLGLE FQA
//
ID   METK2_MOUSE             Reviewed;         395 AA.
AC   Q3THS6; Q3TL60; Q76LX3;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 2.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=S-adenosylmethionine synthase isoform type-2;
DE            Short=AdoMet synthase 2;
DE            EC=2.5.1.6;
DE   AltName: Full=Methionine adenosyltransferase 2;
DE            Short=MAT 2;
GN   Name=Mat2a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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; TISSUE=Kidney;
RA   Sakata S., Okumura S.;
RT   "cDNA for mouse kidney methionine adenosyltransferase II alpha.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and 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).
CC   -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from
CC       methionine and ATP (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate +
CC       diphosphate + S-adenosyl-L-methionine.
CC   -!- COFACTOR: Binds 2 divalent ions per subunit. Magnesium or cobalt
CC       (By similarity).
CC   -!- COFACTOR: Binds 1 potassium ion per subunit (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine
CC       biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
CC   -!- SUBUNIT: Heterotetramer composed of 2 catalytic alpha subunits
CC       (alpha and alpha') (MAT2A) and 1 copy of beta subunit (MAT2B) (By
CC       similarity).
CC   -!- PTM: The alpha' subunit is a post-translationally modified version
CC       of MAT2A (By similarity).
CC   -!- SIMILARITY: Belongs to the AdoMet synthase family.
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DR   EMBL; AB070266; BAD06937.1; -; mRNA.
DR   EMBL; AK166671; BAE38932.1; -; mRNA.
DR   EMBL; AK168155; BAE40120.1; -; mRNA.
DR   IPI; IPI00454016; -.
DR   RefSeq; NP_663544.1; NM_145569.4.
DR   UniGene; Mm.29815; -.
DR   UniGene; Mm.479898; -.
DR   ProteinModelPortal; Q3THS6; -.
DR   SMR; Q3THS6; 16-395.
DR   STRING; Q3THS6; -.
DR   PhosphoSite; Q3THS6; -.
DR   PRIDE; Q3THS6; -.
DR   Ensembl; ENSMUST00000059472; ENSMUSP00000087118; ENSMUSG00000053907.
DR   GeneID; 232087; -.
DR   KEGG; mmu:232087; -.
DR   UCSC; uc009cip.1; mouse.
DR   CTD; 232087; -.
DR   MGI; MGI:2443731; Mat2a.
DR   HOGENOM; HBG443662; -.
DR   HOVERGEN; HBG001562; -.
DR   InParanoid; Q3THS6; -.
DR   OMA; FHDAFIE; -.
DR   OrthoDB; EOG4QVCC3; -.
DR   PhylomeDB; Q3THS6; -.
DR   BRENDA; 2.5.1.6; 244.
DR   NextBio; 380942; -.
DR   ArrayExpress; Q3THS6; -.
DR   Bgee; Q3THS6; -.
DR   CleanEx; MM_MAT2A; -.
DR   Genevestigator; Q3THS6; -.
DR   GermOnline; ENSMUSG00000053907; 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:0004478; F:methionine adenosyltransferase activity; IDA:MGI.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IDA:MGI.
DR   InterPro; IPR022631; ADOMET_SYNTHASE_CS.
DR   InterPro; IPR022630; S-AdoMet_synt_C.
DR   InterPro; IPR022629; S-AdoMet_synt_central.
DR   InterPro; IPR022628; S-AdoMet_synt_N.
DR   InterPro; IPR002133; S-AdoMet_synthetase.
DR   InterPro; IPR022636; S-AdoMet_synthetase_sfam.
DR   PANTHER; PTHR11964; S-AdoMet_synt; 1.
DR   Pfam; PF02773; S-AdoMet_synt_C; 1.
DR   Pfam; PF02772; S-AdoMet_synt_M; 1.
DR   Pfam; PF00438; S-AdoMet_synt_N; 1.
DR   PIRSF; PIRSF000497; MAT; 1.
DR   SUPFAM; SSF55973; S-AdoMet_synt; 3.
DR   TIGRFAMs; TIGR01034; metK; 1.
DR   PROSITE; PS00376; ADOMET_SYNTHASE_1; 1.
DR   PROSITE; PS00377; ADOMET_SYNTHASE_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cobalt; Magnesium; Metal-binding;
KW   Nucleotide-binding; One-carbon metabolism; Phosphoprotein; Potassium;
KW   Transferase.
FT   CHAIN         1    395       S-adenosylmethionine synthase isoform
FT                                type-2.
FT                                /FTId=PRO_0000174437.
FT   NP_BIND     131    136       ATP (Potential).
FT   METAL        31     31       Magnesium (By similarity).
FT   METAL        57     57       Potassium (By similarity).
FT   METAL       283    283       Potassium (By similarity).
FT   METAL       291    291       Magnesium (By similarity).
FT   BINDING     159    159       ATP (Potential).
FT   MOD_RES      81     81       N6-acetyllysine (By similarity).
FT   MOD_RES     114    114       Phosphoserine (By similarity).
FT   CONFLICT     24     24       S -> T (in Ref. 2; BAE40120).
FT   CONFLICT    128    128       E -> G (in Ref. 1; BAD06937).
FT   CONFLICT    283    283       S -> L (in Ref. 2; BAE38932).
FT   CONFLICT    302    302       A -> S (in Ref. 2; BAE40120).
SQ   SEQUENCE   395 AA;  43689 MW;  BB977989B75CB8F9 CRC64;
     MNGQLNGFHE AFIEEGTFLF TSESVGEGHP DKICDQISDA VLDAHLQQDP DAKVACETVA
     KTGMILLAGE ITSRAAIDYQ KVVREAIKHI GYDDSSKGFD YKTCNVLVAL EQQSPDIAQG
     VHLDRNEEDI GAGDQGLMFG YATDETEECM PLTIVLAHKL NAKLAELRRN GTLPWLRPDS
     KTQVTVQYMQ DRGAVLPIRV HTIVISVQHD EEVCLDEMRD ALKEKVIKAV VPAKYLDEDT
     IYHLQPSGRF VIGGPQGDAG LTGRKIIVDT YGGWGAHGGG AFSGKDYTKV DRSAAYAARW
     VAKSLVKGGL CRRVLVQVSY AIGVSHPLSI SIFHYGTSQK SERELLEIVK KNFDLRPGVI
     VRDLDLKKPI YQRTAAYGHF GRDSFPWEVP KKLKY
//
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;
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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   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
CC   Distributed under the Creative Commons Attribution-NoDerivs License
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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   Q3TQC6_MOUSE            Unreviewed;       535 AA.
AC   Q3TQC6;
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;
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; 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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK163689; BAE37458.1; -; mRNA.
DR   IPI; IPI00918030; -.
DR   UniGene; Mm.311840; -.
DR   UniGene; Mm.367369; -.
DR   STRING; Q3TQC6; -.
DR   PRIDE; Q3TQC6; -.
DR   Ensembl; ENSMUST00000148486; ENSMUSP00000122337; ENSMUSG00000003279.
DR   UCSC; uc008dlj.1; mouse.
DR   MGI; MGI:1346065; Dlgap1.
DR   eggNOG; roNOG04801; -.
DR   HOVERGEN; HBG018957; -.
DR   ArrayExpress; Q3TQC6; -.
DR   Bgee; Q3TQC6; -.
DR   Genevestigator; Q3TQC6; -.
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   535 AA;  59240 MW;  242C8B52C963707B CRC64;
     MIDLFKAEWV SSVCVQVSRN GRTDQVWVPQ DEWSGYTPRG KDDEIACRRM RSGSYIKAMG
     DEDSGDSDTS PKPSPKVAAR RESYLKATQP SLTELTTLKI SNEHSPKLQI RSHSYLRAVS
     EVSINRSLDS LDPAGLLTSP KFRSRNESYM RAMSTISQVS EMEVNGQFES VCESVFSELE
     SQAVEALDLP LPGCFRMRSH SYVRAIEKGC SQDDECVSLR SSSPPRTTTT VRTIQSSTVS
     SCITTYKKTP PPVPPRTTTK PFISITAQSS TESAQDAYMD GQGQRGDMIS QSGLSNSTES
     LDSMKALTAA IEAANAQIHG PASQHMGSNA AAVTTTTTIA TVTTEDRKKD FKKNRCLSIG
     IQVDDAEEPE KMAESKTSNK FQSVGVQVEE EKCFRRFTRS NSVTTAVQAD LDFHDNLENS
     LESIEDNSCP GPKARQFSRD ASTSTVSIQG SGNHYHACAA DDDFDTDFDP SILPPPDPWI
     DSITEDPLEA VQRSVCHRDG HWFLKLLQAE RDRMEGWCKL MEREERENNL PEDSK
//
ID   Q3TSA8_MOUSE            Unreviewed;       286 AA.
AC   Q3TSA8;
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=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.
RC   STRAIN=C57BL/6J; TISSUE=In vitro fertilized eggs, and 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=In vitro fertilized eggs, and 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=In vitro fertilized eggs, and 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=In vitro fertilized eggs, and 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=In vitro fertilized eggs, and 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=In vitro fertilized eggs, and 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=In vitro fertilized eggs, and 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=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 (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK132867; BAE21397.1; -; mRNA.
DR   EMBL; AK162168; BAE36767.1; -; mRNA.
DR   IPI; IPI00928306; -.
DR   UniGene; Mm.201455; -.
DR   STRING; Q3TSA8; -.
DR   Ensembl; ENSMUST00000022197; ENSMUSP00000022197; ENSMUSG00000021687.
DR   Ensembl; ENSMUST00000152555; ENSMUSP00000123135; ENSMUSG00000021687.
DR   Ensembl; ENSMUST00000153558; ENSMUSP00000120053; ENSMUSG00000021687.
DR   UCSC; uc007rlr.1; mouse.
DR   MGI; MGI:1349480; Scamp1.
DR   HOVERGEN; HBG071938; -.
DR   InParanoid; Q3TSA8; -.
DR   ArrayExpress; Q3TSA8; -.
DR   Bgee; Q3TSA8; -.
DR   Genevestigator; Q3TSA8; -.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR   GO; GO:0042589; C:zymogen granule membrane; IDA:MGI.
DR   GO; GO:0006887; P:exocytosis; IMP:MGI.
DR   InterPro; IPR007273; SCAMP.
DR   PANTHER; PTHR10687; SCAMP; 1.
DR   Pfam; PF04144; SCAMP; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   286 AA;  32338 MW;  BB68AFB973B00C73 CRC64;
     MPNVPNTQPA IMKPTEEHPA YTQITKEHAL AQAELLKRQE ELERKAAELD RREREMQNLS
     QHGRKNNWPP LPSNFPVGPC FYQDFSVDIP VEFQKTVKLM YYLWMFHAVT LFLNIFGCLA
     WFCVDSSRAV DFGLSILWFL LFTPCSFVCW YRPLYGAFRS DSSFRFFVFF FVYICQFAVH
     VLQAAGFHNW GNCGWISSLT GLNKNIPVGI MMIIIAALFT ASAVISLVMF KKVHGLYRTT
     GASFEKAQQE FATGVMSNKT VQTAAANAAS TAATSAAQNA FKGNQM
//
ID   Q3TTN3_MOUSE            Unreviewed;       283 AA.
AC   Q3TTN3;
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=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.
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 (APR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK161283; BAE36292.1; -; mRNA.
DR   IPI; IPI00122548; -.
DR   UniGene; Mm.227704; -.
DR   STRING; Q3TTN3; -.
DR   Ensembl; ENSMUST00000009036; ENSMUSP00000009036; ENSMUSG00000008892.
DR   MGI; MGI:106922; Vdac3.
DR   eggNOG; roNOG07651; -.
DR   HOVERGEN; HBG054036; -.
DR   ArrayExpress; Q3TTN3; -.
DR   Bgee; Q3TTN3; -.
DR   Genevestigator; Q3TTN3; -.
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   283 AA;  30739 MW;  A95AFD62C3112789 CRC64;
     MCNTPTYCDL GKAAKDVFNK GYGFGMVKID LKTKSCSGVE FSTSGHAYTD TGKASGNLET
     KYKVCNYGLT FTQKWNTDNT LGTEISWENK LAEGLKLTLD TIFVPNTGKK SGKLKASYRR
     DCFSLGSNVD IDFSGPTIYG WAVLAFEGWL AGYQMSFDTA KSKLSQNNFA LGYKAADFQL
     HTHVNDGTEF GGSIYQKVNE RIETSINLAW TAGSNNTRFG IAANYKLDCR TSLSAKVNNA
     SLIGLGYTQT LRPGVKLTLS ALIDGKNFNA GGHKVGLGFE LEA
//
ID   K22E_MOUSE              Reviewed;         707 AA.
AC   Q3TTY5; Q0VBW1; Q61869;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Keratin, type II cytoskeletal 2 epidermal;
DE   AltName: Full=Cytokeratin-2e;
DE            Short=CK-2e;
DE   AltName: Full=Epithelial keratin-2e;
DE   AltName: Full=Keratin-2 epidermis;
DE   AltName: Full=Keratin-2e;
DE            Short=K2e;
DE   AltName: Full=Type-II keratin Kb2;
GN   Name=Krt2; Synonyms=K2e, Krt2-17, Krt2a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=NMRI; TISSUE=Foot sole tissue;
RX   PubMed=2448177; 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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=NMRI;
RX   MEDLINE=94149286; PubMed=7508961; DOI=10.1111/1523-1747.ep12371757;
RA   Herzog F., Winter H., Schweizer J.;
RT   "The large type II 70-kDa keratin of mouse epidermis is the ortholog
RT   of human keratin K2e.";
RL   J. Invest. Dermatol. 102:165-170(1994).
RN   [3]
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   [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 23-36; 210-216; 288-296 AND 483-491, 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 KRT10.
RX   PubMed=9378767;
RA   Reichelt J., Bauer C., Porter R., Lane E., Magin V.;
RT   "Out of balance: consequences of a partial keratin 10 knockout.";
RL   J. Cell Sci. 110:2175-2186(1997).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=15118396; DOI=10.1159/000077033;
RA   Mahler B., Gocken T., Brojan M., Childress S., Spandau D.F., Foley J.;
RT   "Keratin 2e: a marker for murine nipple epidermis.";
RL   Cells Tissues Organs 176:169-177(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388 AND SER-606, 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   VARIANT IBS PRO-500.
RX   PubMed=12533510; DOI=10.1101/gad.1023703;
RA   Fitch K.R., McGowan K.A., van Raamsdonk C.D., Fuchs H., Lee D.,
RA   Puech A., Herault Y., Threadgill D.W., Hrabe de Angelis M.,
RA   Barsh G.S.;
RT   "Genetics of dark skin in mice.";
RL   Genes Dev. 17:214-228(2003).
CC   -!- FUNCTION: Probably contributes to terminal cornification.
CC       Associated with keratinocyte activation, proliferation and
CC       keratinization (By similarity).
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC       Associates with KRT10.
CC   -!- TISSUE SPECIFICITY: Expressed mainly in the middle spinous and
CC       granular cells of the epidermis of adult tail, nipple and footsole
CC       skin. Also found in ear.
CC   -!- DEVELOPMENTAL STAGE: Induction occurs during the first 2 weeks
CC       after birth, being first observed in the epidermis of tail then
CC       the footpad and later in the ear.
CC   -!- DISEASE: Note=Defects in Krt2 are a cause of ichthyosis bullosa of
CC       siemens (IBS). IBS is a rare autosomal dominant disorder
CC       displaying a type of epidermolytic hyperkeratosis characterized by
CC       extensive blistering from birth. Hyperkeratoses and shedding of
CC       the outer layers of the epidermis (molting) are observed in later
CC       weeks.
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; X74784; CAA52788.1; -; mRNA.
DR   EMBL; AK132476; BAE21186.1; -; mRNA.
DR   EMBL; AK161078; BAE36187.1; -; mRNA.
DR   EMBL; AK161098; BAE36194.1; -; mRNA.
DR   EMBL; BC120485; AAI20486.1; -; mRNA.
DR   IPI; IPI00622240; -.
DR   RefSeq; NP_034798.2; NM_010668.2.
DR   UniGene; Mm.358616; -.
DR   ProteinModelPortal; Q3TTY5; -.
DR   SMR; Q3TTY5; 197-234, 241-347, 365-435, 456-510.
DR   STRING; Q3TTY5; -.
DR   PhosphoSite; Q3TTY5; -.
DR   PRIDE; Q3TTY5; -.
DR   Ensembl; ENSMUST00000023712; ENSMUSP00000023712; ENSMUSG00000064201.
DR   GeneID; 16681; -.
DR   KEGG; mmu:16681; -.
DR   UCSC; uc007xub.1; mouse.
DR   CTD; 16681; -.
DR   MGI; MGI:96699; Krt2.
DR   eggNOG; maNOG15734; -.
DR   GeneTree; ENSGT00550000074491; -.
DR   HOGENOM; HBG715391; -.
DR   HOVERGEN; HBG013015; -.
DR   InParanoid; Q3TTY5; -.
DR   OMA; EHAIKDA; -.
DR   OrthoDB; EOG44QT16; -.
DR   NextBio; 290429; -.
DR   ArrayExpress; Q3TTY5; -.
DR   Bgee; Q3TTY5; -.
DR   CleanEx; MM_KRT2; -.
DR   Genevestigator; Q3TTY5; -.
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   1: Evidence at protein level;
KW   Coiled coil; Direct protein sequencing; Disease mutation; Ichthyosis;
KW   Intermediate filament; Keratin; Phosphoprotein.
FT   CHAIN         1    707       Keratin, type II cytoskeletal 2
FT                                epidermal.
FT                                /FTId=PRO_0000283763.
FT   REGION        1    198       Head.
FT   REGION      199    508       Rod.
FT   REGION      199    234       Coil 1A.
FT   REGION      235    253       Linker 1.
FT   REGION      254    345       Coil 1B.
FT   REGION      346    369       Linker 12.
FT   REGION      370    508       Coil 2.
FT   REGION      509    707       Tail.
FT   COMPBIAS     12    701       Gly-rich.
FT   SITE        450    450       Stutter.
FT   MOD_RES      64     64       Phosphoserine (By similarity).
FT   MOD_RES     388    388       Phosphoserine.
FT   MOD_RES     606    606       Phosphoserine.
FT   VARIANT     500    500       T -> P (in IBS).
FT   CONFLICT    238    246       DVGSRTTNL -> ACRQPHHKP (in Ref. 2;
FT                                CAA52788).
FT   CONFLICT    361    361       N -> T (in Ref. 2; CAA52788).
FT   CONFLICT    439    439       K -> I (in Ref. 2; CAA52788).
FT   CONFLICT    451    451       R -> H (in Ref. 2; CAA52788).
FT   CONFLICT    533    533       V -> M (in Ref. 2; CAA52788).
FT   CONFLICT    562    562       Missing (in Ref. 4; AAI20486).
FT   CONFLICT    564    564       T -> S (in Ref. 2; CAA52788).
FT   CONFLICT    625    625       G -> GG (in Ref. 4; AAI20486).
FT   CONFLICT    641    641       V -> A (in Ref. 2; CAA52788).
SQ   SEQUENCE   707 AA;  70923 MW;  464D375DCBA90EF4 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 GGSTYGSGGR SSGSRGSGSG SGGGGYSSGG GSRGGSGGGY
     GSGGGSRGGS GGGYGSGGGS GSGGGYSSGG GSRGGSGGGG VSSGGGSRGG SSSGGGSRGG
     SSSGGGGYSS GGGSRGGSSS GGAGSSSEKG GSGSGEGCGS GVTFSFR
//
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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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   Q3TWS4_MOUSE            Unreviewed;       582 AA.
AC   Q3TWS4;
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=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.
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 ENTH (epsin N-terminal homology) domain.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK159570; BAE35192.1; -; mRNA.
DR   IPI; IPI00652215; -.
DR   UniGene; Mm.281651; -.
DR   UniGene; Mm.472993; -.
DR   ProteinModelPortal; Q3TWS4; -.
DR   SMR; Q3TWS4; 19-281.
DR   STRING; Q3TWS4; -.
DR   PRIDE; Q3TWS4; -.
DR   Ensembl; ENSMUST00000074501; ENSMUSP00000074095; ENSMUSG00000033419.
DR   UCSC; uc009qxw.1; mouse.
DR   MGI; MGI:109132; Snap91.
DR   eggNOG; roNOG10141; -.
DR   GeneTree; ENSGT00390000008805; -.
DR   HOVERGEN; HBG049391; -.
DR   OrthoDB; EOG4VHK72; -.
DR   ArrayExpress; Q3TWS4; -.
DR   Bgee; Q3TWS4; -.
DR   Genevestigator; Q3TWS4; -.
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   582 AA;  61425 MW;  A52F62E2ABC23F66 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
     SKSSPATTVT SPNSTPAKTI DTSPPVDIFA TASAAAPVSS AKPSSDLLDL QPDFSGAAAG
     AAAPVVPPSG GATAWGGFGG SFMAPSTTPV TPAQNNLLQP SFEAAFGTTP STSSSSSFDP
     SVFDGLGDLL MPTMAPSGQP APVSMVPPSP AMAASKGLGS DLDSSLASLV GNLGISGTTS
     KKGDLQWNAG EKKLTGGANW QPKVTPATWS AGVPPQGTVP PTSSVPPGAG APSVGQPGAG
     FGMPPSGTGM TMMSQQPVMF AQPMMRPPFG AAAVPGTQLQ FL
//
ID   Q3TXF9_MOUSE            Unreviewed;      1023 AA.
AC   Q3TXF9;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   SubName: Full=Putative uncharacterized protein;
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.
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 cation transport ATPase (P-type)
CC       family.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK159279; BAE34957.1; -; mRNA.
DR   IPI; IPI00311682; -.
DR   UniGene; Mm.280103; -.
DR   ProteinModelPortal; Q3TXF9; -.
DR   SMR; Q3TXF9; 26-1023.
DR   STRING; Q3TXF9; -.
DR   Ensembl; ENSMUST00000036493; ENSMUSP00000039657; ENSMUSG00000033161.
DR   MGI; MGI:88105; Atp1a1.
DR   eggNOG; roNOG12622; -.
DR   HOVERGEN; HBG004298; -.
DR   InParanoid; Q3TXF9; -.
DR   ArrayExpress; Q3TXF9; -.
DR   Bgee; Q3TXF9; -.
DR   Genevestigator; Q3TXF9; -.
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: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   2: Evidence at transcript level;
KW   ATP-binding; Hydrolase; Ion transport; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Transmembrane; Transmembrane helix; Transport.
SQ   SEQUENCE   1023 AA;  112983 MW;  F242E371DFC6B296 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 ASESALLECI 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   Q3TYL3_MOUSE            Unreviewed;       337 AA.
AC   Q3TYL3;
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=Opcml;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK158538; BAE34550.1; -; mRNA.
DR   IPI; IPI00463489; -.
DR   UniGene; Mm.379474; -.
DR   ProteinModelPortal; Q3TYL3; -.
DR   SMR; Q3TYL3; 31-304.
DR   STRING; Q3TYL3; -.
DR   Ensembl; ENSMUST00000115243; ENSMUSP00000110898; ENSMUSG00000062257.
DR   MGI; MGI:97397; Opcml.
DR   eggNOG; roNOG14812; -.
DR   HOVERGEN; HBG017341; -.
DR   OrthoDB; EOG4DZ1VM; -.
DR   ArrayExpress; Q3TYL3; -.
DR   Bgee; Q3TYL3; -.
DR   Genevestigator; Q3TYL3; -.
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;
SQ   SEQUENCE   337 AA;  37228 MW;  2971A8F82E60F4AB CRC64;
     MYHPAYWIVF SATTALLFIP GVPVRSGDAT FPKAMDNVTV RQGESATLRC TIDDRVTRVA
     WLNRSTILYA GNDKWSIDPR VIILVNTPTQ YSIMIQNVDV YDEGPYTCSV QTDNHPKTSR
     VHLIVQVPPQ IMNISSDITV NEGSSVTLLC LAIGRPEPTV TWRHLSVKGQ GFVSEDEYLE
     ISDIKRDQSG EYECSALNDV AAPDVRKVKI TVNYPPYISK AKNTGVSVGQ KGILSCEASA
     VPMAEFQWFK EDTRLATGLD GVRIENKGRI STLTFFNVSE KDYGNYTCVA TNKLGNTNAS
     ITLYEPGAVI DGVNSASRAL ACLWLSGTFF AHFFIKF
//
ID   Q3TZR9_MOUSE            Unreviewed;       483 AA.
AC   Q3TZR9;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   SubName: Full=Activating transcription factor 7, isoform CRA_a;
GN   Name=Atf7; ORFNames=mCG_17588;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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.
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.
CC   -!- SIMILARITY: Belongs to the bZIP family.
CC   -!- SIMILARITY: Contains 1 bZIP domain.
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CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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DR   EMBL; AK157628; BAE34138.1; -; mRNA.
DR   EMBL; CH466550; EDL03960.1; -; Genomic_DNA.
DR   IPI; IPI00623249; -.
DR   UniGene; Mm.208714; -.
DR   UniGene; Mm.475149; -.
DR   ProteinModelPortal; Q3TZR9; -.
DR   SMR; Q3TZR9; 1-38, 334-394.
DR   STRING; Q3TZR9; -.
DR   PhosphoSite; Q3TZR9; -.
DR   PRIDE; Q3TZR9; -.
DR   Ensembl; ENSMUST00000064254; ENSMUSP00000069887; ENSMUSG00000052414.
DR   UCSC; uc007xwm.1; mouse.
DR   MGI; MGI:2443472; Atf7.
DR   eggNOG; roNOG15325; -.
DR   GeneTree; ENSGT00390000020106; -.
DR   HOGENOM; HBG714930; -.
DR   HOVERGEN; HBG004300; -.
DR   InParanoid; Q3TZR9; -.
DR   OMA; EFKKASD; -.
DR   OrthoDB; EOG4QFWDQ; -.
DR   PhylomeDB; Q3TZR9; -.
DR   ArrayExpress; Q3TZR9; -.
DR   Bgee; Q3TZR9; -.
DR   Genevestigator; Q3TZR9; -.
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:0008270; F:zinc ion binding; IEA:InterPro.
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   483 AA;  51780 MW;  4DF10D373FE376C8 CRC64;
     MGDDRPFVCS APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RTDSVIIADQ TPTPTRFLKN
     CEEVGLFNEL ASSFEHEFKK ASDDDEKKGA AGPLDMSLPS TPDIKIKEEE PVEVDSSPPD
     SPASSPCSPP LKEKEVTTKP VVISTPTPTI VRPGSLPLHL GYDPLHPTLP SPTSVITQAP
     PSNRQIGSPT GSLPLVMHLA NGQTMPMLPG PPVQMPSVIS LARPVSMVPN IPGIPGPPVN
     NSGSISPSGH PMPSEAKMRL KATLTHQVSS INGGCGMVVG TASTMVTARP EQNQILIQHP
     DAPSPAQPQV SPAQPTPSTG GRRRRTVDED PDERRQRFLE RNRAAASRCR QKRKLWVSSL
     EKKAEELTSQ NIQLSNEVTL LRNEVAQLKQ LLLAHKDCPV TALQKKTQGY LESPKESSEP
     TGSPAPVIQH SSASAPSNGL SVRSAAEAVA TSVLTQMASQ RTELSMPIQS HVIMTPQSQS
     AGR
//
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   CC021_MOUSE             Reviewed;         392 AA.
AC   Q3U4G3; Q3TLX5; Q8K2I0;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   RecName: Full=Uncharacterized protein C3orf21 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=NOD; 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   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-14 is the initiator.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH31419.1; Type=Erroneous initiation;
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DR   EMBL; AK154256; BAE32468.1; -; mRNA.
DR   EMBL; AK166259; BAE38667.1; -; mRNA.
DR   EMBL; BC031419; AAH31419.1; ALT_INIT; mRNA.
DR   IPI; IPI00387551; -.
DR   UniGene; Mm.286693; -.
DR   ProteinModelPortal; Q3U4G3; -.
DR   CAZy; GT8; Glycosyltransferase Family 8.
DR   PRIDE; Q3U4G3; -.
DR   Ensembl; ENSMUST00000055389; ENSMUSP00000050246; ENSMUSG00000047434.
DR   UCSC; uc007yxa.1; mouse.
DR   MGI; MGI:2146443; AI480653.
DR   eggNOG; roNOG09127; -.
DR   GeneTree; ENSGT00390000008021; -.
DR   HOGENOM; HBG714669; -.
DR   HOVERGEN; HBG061240; -.
DR   InParanoid; Q3U4G3; -.
DR   OrthoDB; EOG4WM4TW; -.
DR   NextBio; 392552; -.
DR   ArrayExpress; Q3U4G3; -.
DR   Bgee; Q3U4G3; -.
DR   CleanEx; MM_AI480653; -.
DR   Genevestigator; Q3U4G3; -.
DR   GermOnline; ENSMUSG00000047434; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:InterPro.
DR   InterPro; IPR002495; Glyco_trans_8.
DR   Pfam; PF01501; Glyco_transf_8; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    392       Uncharacterized protein C3orf21 homolog.
FT                                /FTId=PRO_0000234428.
FT   TRANSMEM     20     42       Helical; (Potential).
FT   CONFLICT     46     47       ET -> LP (in Ref. 2; AAH31419).
FT   CONFLICT     80     81       GF -> AS (in Ref. 1; BAE38667).
FT   CONFLICT    100    100       L -> Q (in Ref. 1; BAE38667).
FT   CONFLICT    110    110       N -> D (in Ref. 1; BAE38667).
FT   CONFLICT    312    312       S -> A (in Ref. 1; BAE38667).
SQ   SEQUENCE   392 AA;  43885 MW;  01B670119A6A59F2 CRC64;
     MGLLRGGAAC ARAMARLGAL RSHYCALLLA AALAVCAFYY LGSGRETFSS ATKRLKEARA
     GAAAPTPPAP ELARGSAAPG FGAKAKSLEG GVVVPVDYHL LMMFTKAEHN APLQAKARVA
     LSSLLRLAKF EAHEVLNLHF VSEEASREVA KALLRELLPP AAGFKCKVIF HDVAVLTDKL
     FPVVEAMQKY FSAGSGTYYS DSIFFLSVAM HQIMPKEIPR IIQLDLDLKY KTNIRELFEE
     FDNFLPGAVI GIAREMQPVY RHTFWQFRHE NPKTRVGDPP PEGLPGFNSG VMLLNLEAMR
     QSPLYSHLLE PSWVQQLADK YHFRGHLGDQ DFFTMIGMEH PELFHVLDCT WNRQLCTWWR
     DHGYSDVFQA YFRCEGHVKI YHGNCNTPIP ED
//
ID   Q3U6K8_MOUSE            Unreviewed;       283 AA.
AC   Q3U6K8;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-FEB-2011, entry version 34.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Vdac1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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; AK153094; BAE31716.1; -; mRNA.
DR   IPI; IPI00122549; -.
DR   UniGene; Mm.3555; -.
DR   UniGene; Mm.470023; -.
DR   STRING; Q3U6K8; -.
DR   Ensembl; ENSMUST00000020673; ENSMUSP00000020673; ENSMUSG00000020402.
DR   Ensembl; ENSMUST00000102758; ENSMUSP00000099819; ENSMUSG00000020402.
DR   Ensembl; ENSMUST00000109065; ENSMUSP00000104693; ENSMUSG00000020402.
DR   MGI; MGI:106919; Vdac1.
DR   GeneTree; ENSGT00390000011336; -.
DR   HOVERGEN; HBG054036; -.
DR   InParanoid; Q3U6K8; -.
DR   ArrayExpress; Q3U6K8; -.
DR   Bgee; Q3U6K8; -.
DR   Genevestigator; Q3U6K8; -.
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   283 AA;  30725 MW;  2F8CCA901E18766A CRC64;
     MAVPPTYADL GKSARDVFTK GYGFGLIKLD LKTKSENGLE FTSSGSANTE TTKVNGSLET
     KYRWAEYGLT FTEKWNTDNT LGTEITVEDQ LARGLKLTFD SSFSPNTGKK NAKIKTGYKR
     EHINLGCDVD FDIAGPSIRG ALVLGYEGWL AGYQMNFETS KSRVTQSNFA VGYKTDEFQL
     HTNVNDGTEF GGSIYQKVNK KLETAVNLAW TAGNSNTRFG IAAKYQVDPD ACFSAKVNNS
     SLIGLGYTQT LKPGIKLTLS ALLDGKNVNA GGHKLGLGLE FQA
//
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.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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   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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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   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.
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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   WNK2_MOUSE              Reviewed;        2149 AA.
AC   Q3UH66; Q3V387; Q6PAN9; Q6ZPI6; Q7TNS1; Q811F2;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=Serine/threonine-protein kinase WNK2;
DE            EC=2.7.11.1;
DE   AltName: Full=Protein kinase lysine-deficient 2;
DE   AltName: Full=Protein kinase with no lysine 2;
GN   Name=Wnk2; Synonyms=Kiaa1760;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1506-2149 (ISOFORM 5).
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] OF 443-2149 (ISOFORM 6),
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 801-2149 (ISOFORM 3), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1513-2149 (ISOFORM 4).
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 761-2149 (ISOFORM 7).
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   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activation requires autophosphorylation of Ser-
CC       356. Phosphorylation of Ser-352 also promotes increased activity
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=1;
CC         IsoId=Q3UH66-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q3UH66-2; Sequence=VSP_023369;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q3UH66-3; Sequence=VSP_023370, VSP_023372;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q3UH66-4; Sequence=VSP_023370, VSP_023371;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q3UH66-5; Sequence=VSP_023370, VSP_023372, VSP_023373;
CC         Note=No experimental confirmation available;
CC       Name=6;
CC         IsoId=Q3UH66-6; Sequence=VSP_023366, VSP_023367, VSP_023370,
CC                                  VSP_023371;
CC         Note=No experimental confirmation available;
CC       Name=7;
CC         IsoId=Q3UH66-7; Sequence=VSP_023367, VSP_023368, VSP_023370,
CC                                  VSP_023372, VSP_023374;
CC         Note=No experimental confirmation available;
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-224 is present instead of the conserved Lys which is
CC       expected to be an active site residue. Lys-207 appears to fulfill
CC       the required catalytic function.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH46464.1; Type=Erroneous initiation;
CC       Sequence=AAH55795.1; Type=Erroneous initiation;
CC       Sequence=BAE20646.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; CAAA01187366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC140284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK044381; BAE20646.1; ALT_INIT; mRNA.
DR   EMBL; AK147550; BAE27991.1; -; mRNA.
DR   EMBL; BC046464; AAH46464.1; ALT_INIT; mRNA.
DR   EMBL; BC055795; AAH55795.1; ALT_INIT; mRNA.
DR   EMBL; BC060187; AAH60187.1; -; mRNA.
DR   EMBL; AK129439; BAC98249.1; -; mRNA.
DR   IPI; IPI00355244; -.
DR   IPI; IPI00408595; -.
DR   IPI; IPI00653345; -.
DR   IPI; IPI00828549; -.
DR   IPI; IPI00828654; -.
DR   IPI; IPI00828738; -.
DR   IPI; IPI00828980; -.
DR   RefSeq; NP_083637.2; NM_029361.3.
DR   UniGene; Mm.342723; -.
DR   ProteinModelPortal; Q3UH66; -.
DR   SMR; Q3UH66; 184-522.
DR   STRING; Q3UH66; -.
DR   PhosphoSite; Q3UH66; -.
DR   PRIDE; Q3UH66; -.
DR   Ensembl; ENSMUST00000035538; ENSMUSP00000047231; ENSMUSG00000037989.
DR   Ensembl; ENSMUST00000049265; ENSMUSP00000049327; ENSMUSG00000037989.
DR   Ensembl; ENSMUST00000091623; ENSMUSP00000089212; ENSMUSG00000037989.
DR   Ensembl; ENSMUST00000110096; ENSMUSP00000105723; ENSMUSG00000037989.
DR   Ensembl; ENSMUST00000110097; ENSMUSP00000105724; ENSMUSG00000037989.
DR   GeneID; 75607; -.
DR   KEGG; mmu:75607; -.
DR   UCSC; uc009val.1; mouse.
DR   CTD; 75607; -.
DR   MGI; MGI:1922857; Wnk2.
DR   eggNOG; roNOG06757; -.
DR   GeneTree; ENSGT00550000074385; -.
DR   HOVERGEN; HBG050345; -.
DR   OrthoDB; EOG4NP72M; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 343494; -.
DR   ArrayExpress; Q3UH66; -.
DR   Bgee; Q3UH66; -.
DR   CleanEx; MM_WNK2; -.
DR   Genevestigator; Q3UH66; -.
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   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1   2149       Serine/threonine-protein kinase WNK2.
FT                                /FTId=PRO_0000278774.
FT   DOMAIN      195    453       Protein kinase.
FT   NP_BIND     201    209       ATP (By similarity).
FT   COMPBIAS    172    177       Poly-Glu.
FT   COMPBIAS    645   1080       Pro-rich.
FT   COMPBIAS   1430   1496       Pro-rich.
FT   COMPBIAS   1594   1597       Poly-Ser.
FT   ACT_SITE    323    323       Proton acceptor (By similarity).
FT   BINDING     207    207       ATP (By similarity).
FT   MOD_RES      49     49       Phosphoserine (By similarity).
FT   MOD_RES     352    352       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     356    356       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1725   1725       Phosphoserine (By similarity).
FT   MOD_RES    1726   1726       Phosphoserine (By similarity).
FT   MOD_RES    1770   1770       Phosphoserine (By similarity).
FT   MOD_RES    1797   1797       Phosphoserine (By similarity).
FT   VAR_SEQ     731    742       Missing (in isoform 6).
FT                                /FTId=VSP_023366.
FT   VAR_SEQ     971   1068       Missing (in isoform 6 and isoform 7).
FT                                /FTId=VSP_023367.
FT   VAR_SEQ    1592   1593       AE -> E (in isoform 7).
FT                                /FTId=VSP_023368.
FT   VAR_SEQ    1921   2004       Missing (in isoform 2).
FT                                /FTId=VSP_023369.
FT   VAR_SEQ    1935   1935       R -> AHASTPP (in isoform 3, isoform 4,
FT                                isoform 5, isoform 6 and isoform 7).
FT                                /FTId=VSP_023370.
FT   VAR_SEQ    1971   2024       Missing (in isoform 4 and isoform 6).
FT                                /FTId=VSP_023371.
FT   VAR_SEQ    2019   2025       SLYDSPG -> R (in isoform 3, isoform 5 and
FT                                isoform 7).
FT                                /FTId=VSP_023372.
FT   VAR_SEQ    2142   2149       DPESEKPD -> GTVHSSLSGPPCTLPLCQYGGLLPDPVSW
FT                                GPWVASGNPEGSWGSQSPTQVPVFPVFLRPPVISTPGPRLH
FT                                IT (in isoform 5).
FT                                /FTId=VSP_023373.
FT   VAR_SEQ    2142   2149       DPESEKPD -> EACALPTPPCKFLSRPSSGQPTEGRSISG
FT                                GFHDTCPGGERGDENSLTPSG (in isoform 7).
FT                                /FTId=VSP_023374.
FT   CONFLICT    761    794       PYLAPTSQVVAPAQLKPLQMPQPPLQPLAQVPPQ -> RRY
FT                                LWPIFCSPQGWGTRPWTRPVHACLQGLLARE (in Ref.
FT                                4; BAC98249).
SQ   SEQUENCE   2149 AA;  227527 MW;  A4BBF1D391FE9BEC CRC64;
     MDGDGGRRDA PGALMEAGRG TGSAGMAEPR ARAARLGPQR FLRRSVVESD QEEPPGLEAA
     ETPSAQPPQP LQRRVLLLCK TRRLIAERAR GRPAAPAPAA PAAPPGSPSV PSDPGPERAG
     TQEPSPDPTT ASAAATQVPD 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 PLPMAQPPTL PQVLAPQPMG TVQPVPSHLP PYLAPTSQVV APAQLKPLQM
     PQPPLQPLAQ VPPQMPQMPV VPPITPLTGL DGLPQTLTDL PAANVAPVPP PQYFSPAVIL
     PSLTTPLPTS PALPMQAVKL PHPPGTPLAV PCQTIVPNAP AAIPLLAVAP QGVAALSIHP
     AVAQIPAQPV YPAAFPQMVP GDIPPSPHHT VQSLRATPPQ LASPVPPQPV QPSVIHLPEQ
     AAPTAASGTQ VLLGHPPSYT ADVAAPVSAV SLPPAVLSPP LPDTLLPTVP DLLPKVPSSL
     APTVVAASQS APAQTSSLLL PTNPPLPTGP AVAGPCPAVQ LMVEVAQEEQ VSQDKPPGPP
     QSSESFGGSD VTSGRDLSDS CEGTFGGGRL EGRTARKHHR RSTRARSRQE RASRPRLTIL
     NVCNTGDKMV ECQLETHNHK MVTFKFDLDG DAPDEIATYM VEHDFILPAE RETFIEQMKD
     VMDKAEDMLS EDTDADHGSD TGTSPPHLGT CGLATGEENR QSQANAPVYQ QNVLHTGKRW
     FIICPVAEHP ATDTSESSPP LPLSSLQPEA SQDPAPYPDQ LSLTDKPSFP AAQQLLSQAG
     SSNPPGGASA PLAPSSPPVT TVIPAAPATS TVPESAAGTA MQAGGPGTHQ GPASVHETLQ
     PLAETRSAQC TAQPLSTGQG PCTPALEASR CSTGLGEPIS TREVSTQGEP LPASVPEPSP
     PTGATQSVPG QPPPPLPITV GAISLAAPQL PSPPLGPTAP PPPPSALESD GEGPPPRVGF
     VDNTIKSLDE KLRTLLYQEH VPTSSASAGT PMEASDRDFT LEPLRGDLPS ALSDKTPSLT
     QQTQPSLEKS ETAPAGWALA QREQGASSPM TAESSSSNTL GCDSDAGQVA SDSSTAPSVP
     QDASGSSVPT HMDPKDQNSS VPREALAAPM QSGPGSFTVG SPAQLRGARD SGSPHKRPGQ
     QDNSSPAKTV GRFSVVSTQD EWTLASPHSL RYSAPPDVYL DEIPSSPEVK LAVRRVQTAS
     SIEVGVEEPA SSDSGDERPR RRSQVQKQSS LPGTGGVASD FVKKATAFLH RSSRAGSLGP
     ETPSRAGVKV PTISITSFHS QSSYISSDND SEFEDADIKK ELRSLREKHL KEISELQSQQ
     KQEIEALYRR LGKPLPPNVG FFHTAPPMGR RRKTSKSKLK AGKLLNPLVQ QLKVVASSTG
     HLSDSSRGPP TKDPRGTKAV QTQQPCSVRA SLSTDICSGL ASDGGGARGQ GWTVYHPTSE
     RGAYKSSSKP RARFLSGPVS VSIWSALKRL CLGKEHSSSL YDSPGSSTSS LAPGPEPGPQ
     PTLHVQAQVN NSNNKKGTFT DDLHKLVDEW TTKTVGAAQV KPTLNQLKQT QKLHDMEASG
     DARATSVPRA AVGASCLAPA PGPLSTTATP GATPALPVPI PDPESEKPD
//
ID   LIMC1_MOUSE             Reviewed;        1057 AA.
AC   Q3UH68; Q6DIC3; Q80TK1;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   11-JAN-2011, entry version 53.
DE   RecName: Full=LIM and calponin homology domains-containing protein 1;
GN   Name=Limch1; Synonyms=Kiaa1102;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; 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).
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 [LARGE SCALE MRNA] OF 273-1057 (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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-719 AND
RP   SER-973, 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-201; THR-215; SER-217;
RP   SER-231 AND SER-719, 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=Q3UH68-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UH68-2; Sequence=VSP_026551, VSP_026553;
CC       Name=3;
CC         IsoId=Q3UH68-3; Sequence=VSP_026552, VSP_026554;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the LIMCH1 family.
CC   -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC   -!- SIMILARITY: Contains 1 LIM zinc-binding domain.
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DR   EMBL; AK134095; BAE22010.1; -; mRNA.
DR   EMBL; AK147547; BAE27989.1; -; mRNA.
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   EMBL; BC075634; AAH75634.1; -; mRNA.
DR   EMBL; AK122443; BAC65725.1; -; mRNA.
DR   IPI; IPI00844691; -.
DR   IPI; IPI00853683; -.
DR   IPI; IPI00853814; -.
DR   RefSeq; NP_001001980.2; NM_001001980.2.
DR   UniGene; Mm.404233; -.
DR   ProteinModelPortal; Q3UH68; -.
DR   SMR; Q3UH68; 9-178, 982-1048.
DR   STRING; Q3UH68; -.
DR   PhosphoSite; Q3UH68; -.
DR   PRIDE; Q3UH68; -.
DR   Ensembl; ENSMUST00000101164; ENSMUSP00000098723; ENSMUSG00000037736.
DR   GeneID; 77569; -.
DR   KEGG; mmu:77569; -.
DR   UCSC; uc008xpj.1; mouse.
DR   CTD; 77569; -.
DR   MGI; MGI:1924819; Limch1.
DR   HOVERGEN; HBG108087; -.
DR   OMA; LLYGPYR; -.
DR   NextBio; 347118; -.
DR   ArrayExpress; Q3UH68; -.
DR   Bgee; Q3UH68; -.
DR   CleanEx; MM_LIMCH1; -.
DR   Genevestigator; Q3UH68; -.
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   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; LIM domain; Metal-binding;
KW   Phosphoprotein; Zinc.
FT   CHAIN         1   1057       LIM and calponin homology domains-
FT                                containing protein 1.
FT                                /FTId=PRO_0000293620.
FT   DOMAIN       21    125       CH.
FT   DOMAIN      985   1051       LIM zinc-binding.
FT   COILED      348    439       Potential.
FT   COMPBIAS    771    826       Glu-rich.
FT   MOD_RES     169    169       Phosphoserine.
FT   MOD_RES     192    192       Phosphoserine (By similarity).
FT   MOD_RES     201    201       Phosphoserine.
FT   MOD_RES     204    204       Phosphoserine (By similarity).
FT   MOD_RES     207    207       Phosphoserine (By similarity).
FT   MOD_RES     210    210       Phosphoserine (By similarity).
FT   MOD_RES     212    212       Phosphoserine (By similarity).
FT   MOD_RES     215    215       Phosphothreonine.
FT   MOD_RES     217    217       Phosphoserine.
FT   MOD_RES     225    225       Phosphoserine (By similarity).
FT   MOD_RES     231    231       Phosphoserine.
FT   MOD_RES     233    233       Phosphoserine (By similarity).
FT   MOD_RES     274    274       Phosphoserine (By similarity).
FT   MOD_RES     277    277       Phosphothreonine (By similarity).
FT   MOD_RES     377    377       Phosphoserine (By similarity).
FT   MOD_RES     471    471       Phosphoserine (By similarity).
FT   MOD_RES     493    493       Phosphoserine (By similarity).
FT   MOD_RES     523    523       Phosphoserine (By similarity).
FT   MOD_RES     529    529       Phosphothreonine (By similarity).
FT   MOD_RES     603    603       Phosphoserine (By similarity).
FT   MOD_RES     719    719       Phosphoserine.
FT   MOD_RES     973    973       Phosphoserine.
FT   VAR_SEQ       1    156       Missing (in isoform 2).
FT                                /FTId=VSP_026551.
FT   VAR_SEQ       1     13       MACPALGLEVLQP -> MHKTCTIRSFIRDFYRILFTCARP
FT                                SIMSDDAESTSMFDMRCEEEAAVLPHSRARQEQ (in
FT                                isoform 3).
FT                                /FTId=VSP_026552.
FT   VAR_SEQ     157    162       LAQMRK -> MDPERQ (in isoform 2).
FT                                /FTId=VSP_026553.
FT   VAR_SEQ     199    398       Missing (in isoform 3).
FT                                /FTId=VSP_026554.
FT   CONFLICT    682    682       S -> P (in Ref. 3; AAH75634).
SQ   SEQUENCE   1057 AA;  118196 MW;  3989AAF7718E320C 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 MESPGERRKS ISGKKLCSSC GLTLGKGAAM IIETLNLYFH IQCFRCGICK
     GQLGDAVSGT DVRIRNGLLN CTDCYMRSRS AGQPTTL
//
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   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   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   Q3UHK5_MOUSE            Unreviewed;      1020 AA.
AC   Q3UHK5;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   SubName: Full=MCG142115, isoform CRA_c;
GN   Name=Atp1a2; ORFNames=mCG_142115;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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, and C57BL/6J;
RC   TISSUE=Brain, Heart, Medulla oblongata, and Bone;
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, and C57BL/6J;
RC   TISSUE=Brain, Heart, Medulla oblongata, and Bone;
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, and C57BL/6J;
RC   TISSUE=Brain, Heart, Medulla oblongata, and Bone;
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, and C57BL/6J;
RC   TISSUE=Brain, Heart, Medulla oblongata, and Bone;
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, and C57BL/6J;
RC   TISSUE=Brain, Heart, Medulla oblongata, and Bone;
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, and C57BL/6J;
RC   TISSUE=Brain, Heart, Medulla oblongata, and Bone;
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, and C57BL/6J;
RC   TISSUE=Brain, Heart, Medulla oblongata, and Bone;
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, and C57BL/6J; TISSUE=Brain, and Bone;
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.
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Medulla oblongata;
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 cation transport ATPase (P-type)
CC       family.
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DR   EMBL; AK137602; BAE23426.1; -; mRNA.
DR   EMBL; AK147331; BAE27852.1; -; mRNA.
DR   EMBL; AK161840; BAE36600.1; -; mRNA.
DR   EMBL; AK164509; BAE37817.1; -; mRNA.
DR   EMBL; AK168703; BAE40545.1; -; mRNA.
DR   EMBL; CH466520; EDL39028.1; -; Genomic_DNA.
DR   IPI; IPI00420569; -.
DR   RefSeq; NP_848492.1; NM_178405.3.
DR   UniGene; Mm.207432; -.
DR   ProteinModelPortal; Q3UHK5; -.
DR   SMR; Q3UHK5; 25-1020.
DR   STRING; Q3UHK5; -.
DR   PRIDE; Q3UHK5; -.
DR   Ensembl; ENSMUST00000085913; ENSMUSP00000083077; ENSMUSG00000007097.
DR   GeneID; 98660; -.
DR   KEGG; mmu:98660; -.
DR   CTD; 98660; -.
DR   MGI; MGI:88106; Atp1a2.
DR   eggNOG; roNOG13230; -.
DR   HOVERGEN; HBG004298; -.
DR   InParanoid; Q3UHK5; -.
DR   OMA; KIQINAE; -.
DR   NextBio; 353565; -.
DR   ArrayExpress; Q3UHK5; -.
DR   Bgee; Q3UHK5; -.
DR   Genevestigator; Q3UHK5; -.
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:0005515; F:protein binding; IPI:MGI.
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   2: Evidence at transcript level;
KW   ATP-binding; Hydrolase; Ion transport; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Transmembrane; Transmembrane helix; Transport.
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   TNR6A_MOUSE             Reviewed;        1896 AA.
AC   Q3UHK8;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Trinucleotide repeat-containing gene 6A protein;
GN   Name=Tnrc6a; Synonyms=Kiaa1460;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-976, 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 both
CC       micro-RNAs (miRNAs) and short interfering RNAs (siRNAs). Required
CC       for miRNA-dependent repression of translation and for siRNA-
CC       dependent endonucleolytic cleavage of complementary mRNAs by
CC       argonaute 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   -!- SIMILARITY: Belongs to the GW182 family.
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; AK147327; BAE27849.1; -; mRNA.
DR   IPI; IPI00670741; -.
DR   RefSeq; NP_659174.3; NM_144925.3.
DR   UniGene; Mm.102305; -.
DR   ProteinModelPortal; Q3UHK8; -.
DR   SMR; Q3UHK8; 1169-1246, 1716-1786.
DR   STRING; Q3UHK8; -.
DR   PhosphoSite; Q3UHK8; -.
DR   Ensembl; ENSMUST00000094053; ENSMUSP00000091595; ENSMUSG00000052707.
DR   GeneID; 233833; -.
DR   KEGG; mmu:233833; -.
DR   UCSC; uc009jpc.1; mouse.
DR   CTD; 233833; -.
DR   MGI; MGI:2385292; Tnrc6a.
DR   HOGENOM; HBG446435; -.
DR   InParanoid; Q3UHK8; -.
DR   OrthoDB; EOG4DFPMT; -.
DR   NextBio; 381871; -.
DR   ArrayExpress; Q3UHK8; -.
DR   Bgee; Q3UHK8; -.
DR   Genevestigator; Q3UHK8; -.
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:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009267; P:cellular response to starvation; IDA:MGI.
DR   GO; GO:0035278; P:negative regulation of translation involved in gene silencing by miRNA; ISS:UniProtKB.
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   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF10427; Ago_hook; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF46934; UBA_like; 1.
DR   PROSITE; PS50102; RRM; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; RNA-binding; RNA-mediated gene silencing;
KW   Translation regulation.
FT   CHAIN         1   1896       Trinucleotide repeat-containing gene 6A
FT                                protein.
FT                                /FTId=PRO_0000373980.
FT   DOMAIN     1716   1788       RRM.
FT   REGION      239    488       Sufficient for interaction with EIF2C1,
FT                                EIF2C3 and EIF2C4 (By similarity).
FT   REGION      255    331       Sufficient for interaction with EIF2C2
FT                                (By similarity).
FT   REGION      303    384       Sufficient for interaction with EIF2C2
FT                                (By similarity).
FT   REGION      325    424       Sufficient for interaction with EIF2C2
FT                                (By similarity).
FT   REGION      394    480       Sufficient for interaction with EIF2C2
FT                                (By similarity).
FT   REGION      487    736       Sufficient for interaction with EIF2C2
FT                                (By similarity).
FT   REGION      551   1279       Sufficient for interaction with EIF2C1
FT                                and EIF2C4 (By similarity).
FT   REGION     1059   1129       Sufficient for interaction with EIF2C2
FT                                (By similarity).
FT   REGION     1605   1896       Sufficient for interaction with EIF2C2
FT                                (By similarity).
FT   COMPBIAS     31     54       Lys-rich.
FT   COMPBIAS     93    113       Gln-rich.
FT   COMPBIAS    334    337       Poly-Ser.
FT   COMPBIAS   1127   1130       Poly-Glu.
FT   COMPBIAS   1332   1415       Gln-rich.
FT   COMPBIAS   1592   1597       Poly-Ser.
FT   COMPBIAS   1890   1893       Poly-Gly.
FT   MOD_RES     976    976       Phosphoserine.
FT   MOD_RES    1406   1406       Phosphothreonine (By similarity).
FT   MOD_RES    1520   1520       Phosphoserine (By similarity).
SQ   SEQUENCE   1896 AA;  203222 MW;  D70578F1D6531608 CRC64;
     MRELEAKATK DVERNLSRDL VQEEEQLMEE KKKKKDDKKK KEAAQKKATE QKIKVPEQIK
     PSVSQPQPAN SDNGTSTATS TNNNAKRATA SNQQPPPPQQ QQPQQEQQQQ QPQALPRYPR
     EVPPRFRHQE HKQLLKRGQH FPVIAANLGS AVKVLNSQSE SSAVTNQQPQ NNGEVQNSKS
     QSDINHNTSG SHYENCQRGP VSSTSDCSTS CKNAVNDLLE KEAWPSAPGS DPELAPECID
     ADSASNSESE RNITVMASGN TGGEKDGLRN STGLGSQSKF VVGSSSNNVG HGSSTGPWGF
     PHGALISTCQ VSVDAPESKP ESSNNRMNAW GTVSSSSNGG LNPSTLNSAS NHGAWPVLEN
     NGLALKGPVG SGSSGINIQC STIGQMPNNQ NINSKVSGSS THGTWGSLQE TCEPEVSGTQ
     KVSFSGQPQN ITTETTGPNN TTNFMTSSLP NSGSVQNNEL PTSNPGAWRV STMNHPQIQA
     PSVMNGTSLS HLSNGESKTG GSYGTTWGAY GSNYSGDKCA GPNGQANGDT VNATLMQPGI
     NGPMGTNFQV NTNKGGGVWE PGTVNSQSSP WGSGNGANSG GSRRGWESPA QNTGTGLSSV
     EWNKLPSNQH SNDSANGNGK KLTNGWKSTE EDDQGSATSQ TNEQNSVWAK AGGTVESDGS
     AESTGRLEEK VTGESQSRDR RKIDQHTLLQ SIVNRTDLDP RVLSNSGWGQ TPIKQNTAWD
     TETSPRGERK TDNGTEAWGS SATQTFNSGA CTDKTSPNSN DTSSVSGWGD PKPTLRWGDS
     KGSNCQGGWE DDSAATGMIK SNQWGGCKED KSTWNDSQKS KQGWGDGQKS SQGWSISAGD
     NWGESSRSNH WGEANKKSSS GGSDSDRSIS GWNELGKTSS FTWGNNINPN NSSGWDESSK
     PNSSQGWGDP PKCNQSLGWG DSSKPVSSPD WNKQQDIVGS WGIPPATSKP PGTGWLGGPI
     PAPAKEEEPT GWEEPSPESI RRKMEIDDGT SAWGDPSKYN YKNVNMWNKN IPEASGRSDQ
     QAQMHRLLPA ASAVSSKETS SGSGWGEPWA EPSTPATTVD NGTSAWGKPI DSGPSWGEPI
     TAASNASTWG SSSVGPQSLS KSGPKSMQDG WCGDDMPLPG SRPTGWEEEE DVEIGMWNSN
     SSQELNSSLN WPPYTKKMSS KGLSGKKRRR ERGMMKGGNK QEDAWINPFV KQFSNISFSR
     DSPEENVQSN KMDLSGGMLQ DKRMEIDKHS LNIGDYNRTV GKGPGSRPQI SKESSMERNP
     YFDKNGNPNM FGVGNTAAQP RGMQQPPAQP LSSSQPNLRA QVPPPLLSPQ VPVSLLKYAP
     NNGGLNPLFG PQQVAMLNQL SQLNQLSQIS QLQRLLAQQQ RAQSQRSAPS ANRQQQDQQG
     RPLSVQQQMM QQSRQLDPSL LVKQQTPPSQ QPLHQPAMKS FLDNVMPHTT PELQKGPSPV
     NAFSNFPIGL NSNLNVNMDM NSIKEPQSRL RKWTTVDSMS VNTSLDQNSS KHGAISSGFR
     LEESPFVPYD FMNSSTSPAS PPGSIGDGWP RAKSPNGSSS VNWPPEFRPG EPWKGYPNID
     PETDPYVTPG SVINSLSINT VREVDHLRDR NSGSSSSLNT TLPSTSAWSS IRASNYNVPL
     SSTAQSTSAR NSDSKLTWSP GSVTNTSLAH ELWKVPLPPK NITAPSRPPP GLTGQKPPLS
     TWDNSPLRVG GGWGNSDARY TPGSSWGESS SGRITNWLVL KNLTPQIDGS TLRTLCMQHG
     PLITFHLNLP HGNALVRYSS KEEVVKAQKS LHMCVLGNTT ILAEFASEEE ISRFFAQSQS
     LTPSPGWQSL GSSQSRLGSL DCSHSFSSRT DVNHWNGAGL SGANCGDLHG TSLWGTPHYS
     TSLWGPPSSD PRGISSPSPI NAFLSVDHLG GGGESM
//
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   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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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   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   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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CC   -----------------------------------------------------------------------
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   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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   Q3UUL5_MOUSE            Unreviewed;      1009 AA.
AC   Q3UUL5;
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=Glutamate receptor, ionotropic, delta 1;
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Grid1; ORFNames=RP23-120M21.1-001, mCG_6345;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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   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.
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RA   Glithero R.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE.
RA   Corby N.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK138279; BAE23610.1; -; mRNA.
DR   EMBL; CT009532; CAX15538.1; -; Genomic_DNA.
DR   EMBL; AC114572; CAX15538.1; JOINED; Genomic_DNA.
DR   EMBL; AC154388; CAX15538.1; JOINED; Genomic_DNA.
DR   EMBL; AC154730; CAX15538.1; JOINED; Genomic_DNA.
DR   EMBL; AC163280; CAX15538.1; JOINED; Genomic_DNA.
DR   EMBL; AC169510; CAX15538.1; JOINED; Genomic_DNA.
DR   EMBL; CT030647; CAX15538.1; JOINED; Genomic_DNA.
DR   EMBL; CT030647; CAX15982.1; -; Genomic_DNA.
DR   EMBL; AC114572; CAX15982.1; JOINED; Genomic_DNA.
DR   EMBL; AC154388; CAX15982.1; JOINED; Genomic_DNA.
DR   EMBL; AC154730; CAX15982.1; JOINED; Genomic_DNA.
DR   EMBL; AC163280; CAX15982.1; JOINED; Genomic_DNA.
DR   EMBL; AC169510; CAX15982.1; JOINED; Genomic_DNA.
DR   EMBL; CT009532; CAX15982.1; JOINED; Genomic_DNA.
DR   EMBL; CH466573; EDL24889.1; -; Genomic_DNA.
DR   IPI; IPI00856177; -.
DR   RefSeq; NP_032192.2; NM_008166.2.
DR   UniGene; Mm.121569; -.
DR   UniGene; Mm.413604; -.
DR   UniGene; Mm.477417; -.
DR   ProteinModelPortal; Q3UUL5; -.
DR   SMR; Q3UUL5; 436-547.
DR   STRING; Q3UUL5; -.
DR   PRIDE; Q3UUL5; -.
DR   Ensembl; ENSMUST00000043349; ENSMUSP00000044009; ENSMUSG00000041078.
DR   GeneID; 14803; -.
DR   KEGG; mmu:14803; -.
DR   NMPDR; fig|10090.3.peg.28854; -.
DR   UCSC; uc007tbj.1; mouse.
DR   CTD; 14803; -.
DR   MGI; MGI:95812; Grid1.
DR   eggNOG; roNOG09195; -.
DR   HOVERGEN; HBG051840; -.
DR   InParanoid; Q3UUL5; -.
DR   OMA; LPWICQC; -.
DR   PhylomeDB; Q3UUL5; -.
DR   NextBio; 286969; -.
DR   ArrayExpress; Q3UUL5; -.
DR   Bgee; Q3UUL5; -.
DR   Genevestigator; Q3UUL5; -.
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-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   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   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   1009 AA;  112210 MW;  143243A1E3EBD660 CRC64;
     MEALTLWLLP WICQCVTVRA DSIIHIGAIF EENAAKDDRV FQLAVSDLSL NDDILQSEKI
     TYSIKVIEAN NPFQAVQEAC DLMTQGILAL VTSTGCASAN ALQSLTDAMH IPHLFVQRNP
     GGSPRTACHL NPSPDGEAYT LASRPPVRLN DVMLRLVTEL RWQKFVMFYD SEYDIRGLQS
     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   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   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   LRC55_MOUSE             Reviewed;         311 AA.
AC   Q3UY51;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Leucine-rich repeat-containing protein 55;
DE   Flags: Precursor;
GN   Name=Lrrc55; Synonyms=Gm351;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; 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).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Contains 6 LRR (leucine-rich) repeats.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-14 is the initiator.
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DR   EMBL; AK134968; BAE22362.1; -; mRNA.
DR   IPI; IPI00352775; -.
DR   RefSeq; NP_001028518.1; NM_001033346.2.
DR   UniGene; Mm.291095; -.
DR   UniGene; Mm.476412; -.
DR   ProteinModelPortal; Q3UY51; -.
DR   SMR; Q3UY51; 48-261.
DR   PRIDE; Q3UY51; -.
DR   Ensembl; ENSMUST00000099930; ENSMUSP00000097514; ENSMUSG00000075224.
DR   Ensembl; ENSMUST00000111601; ENSMUSP00000107228; ENSMUSG00000075224.
DR   GeneID; 241528; -.
DR   KEGG; mmu:241528; -.
DR   NMPDR; fig|10090.3.peg.6276; -.
DR   UCSC; uc008kkc.1; mouse.
DR   CTD; 241528; -.
DR   MGI; MGI:2685197; Lrrc55.
DR   eggNOG; roNOG06946; -.
DR   GeneTree; ENSGT00560000076985; -.
DR   HOGENOM; HBG716091; -.
DR   HOVERGEN; HBG081932; -.
DR   InParanoid; Q3UY51; -.
DR   OMA; ITANCCH; -.
DR   OrthoDB; EOG4NS3BS; -.
DR   NextBio; 385045; -.
DR   Bgee; Q3UY51; -.
DR   CleanEx; MM_LRRC55; -.
DR   Genevestigator; Q3UY51; -.
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   InterPro; IPR000372; LRR-contain_N.
DR   Pfam; PF00560; LRR_1; 2.
DR   Pfam; PF01462; LRRNT; 1.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00013; LRRNT; 1.
DR   PROSITE; PS51450; LRR; 5.
PE   2: Evidence at transcript level;
KW   Leucine-rich repeat; Membrane; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     47       By similarity.
FT   CHAIN        48    311       Leucine-rich repeat-containing protein
FT                                55.
FT                                /FTId=PRO_0000232914.
FT   TRANSMEM    272    292       Helical; (Potential).
FT   REPEAT       50     76       LRR 1.
FT   REPEAT       77    100       LRR 2.
FT   REPEAT      101    124       LRR 3.
FT   REPEAT      126    148       LRR 4.
FT   REPEAT      150    173       LRR 5.
FT   REPEAT      174    197       LRR 6.
FT   COMPBIAS    307    310       Poly-Glu.
SQ   SEQUENCE   311 AA;  34460 MW;  9F19777359807820 CRC64;
     MGSLQHCCCQ LPKMGDTWAQ LPWPGPPHSA LLLVFFLLAA GVMHSDAGTS CPVLCTCRNQ
     VVDCSNQRLF SVPPDLPMDT RNLSLAHNRI AAVPPGYLTC YMELRVLDLR NNSLMELPPG
     LFLHAKRLAH LDLSYNNLSH VPADMFREAH GLVHIDLSHN PWLRRVHPQA FQGLVHLRDL
     DLSYGGLAFL SLEALEGLPG LVTLQIGGNP WVCGCTMEPL LKWLRNRIQR CTADSQLAEC
     RGPPEVEGAP LFSLTEESFK ACHLTLTLDD YLFIAFVGFV VSIASVATNF LLGITANCCH
     RWSKANEEEE I
//
ID   TBCD9_MOUSE             Reviewed;        1264 AA.
AC   Q3UYK3; Q69ZW8; Q8BIJ5; Q8BVP3; Q9CUB3;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=TBC1 domain family member 9;
GN   Name=Tbc1d9; Synonyms=Kiaa0882;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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 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 36-1264 (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: May act as a GTPase-activating protein for Rab family
CC       protein(s).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UYK3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UYK3-2; Sequence=VSP_025698;
CC         Note=No experimental confirmation available;
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; AK017015; BAB30550.1; -; mRNA.
DR   EMBL; AK049049; BAC33525.1; -; mRNA.
DR   EMBL; AK077081; BAC36601.1; -; mRNA.
DR   EMBL; AK134614; BAE22209.1; -; mRNA.
DR   EMBL; AK173050; BAD32328.1; -; mRNA.
DR   IPI; IPI00222145; -.
DR   IPI; IPI00464309; -.
DR   RefSeq; NP_001104774.1; NM_001111304.1.
DR   RefSeq; NP_082034.1; NM_027758.4.
DR   UniGene; Mm.24031; -.
DR   ProteinModelPortal; Q3UYK3; -.
DR   SMR; Q3UYK3; 488-936.
DR   PhosphoSite; Q3UYK3; -.
DR   PRIDE; Q3UYK3; -.
DR   Ensembl; ENSMUST00000034145; ENSMUSP00000034145; ENSMUSG00000031709.
DR   Ensembl; ENSMUST00000093393; ENSMUSP00000091093; ENSMUSG00000031709.
DR   GeneID; 71310; -.
DR   KEGG; mmu:71310; -.
DR   CTD; 71310; -.
DR   MGI; MGI:1918560; Tbc1d9.
DR   eggNOG; roNOG13875; -.
DR   GeneTree; ENSGT00580000081243; -.
DR   HOGENOM; HBG447190; -.
DR   HOVERGEN; HBG054142; -.
DR   InParanoid; Q3UYK3; -.
DR   OMA; QALMTMY; -.
DR   OrthoDB; EOG48D0TH; -.
DR   PhylomeDB; Q3UYK3; -.
DR   NextBio; 333519; -.
DR   ArrayExpress; Q3UYK3; -.
DR   Bgee; Q3UYK3; -.
DR   CleanEx; MM_TBC1D9; -.
DR   Genevestigator; Q3UYK3; -.
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; Phosphoprotein; Repeat.
FT   CHAIN         1   1264       TBC1 domain family member 9.
FT                                /FTId=PRO_0000288500.
FT   DOMAIN      146    213       GRAM 1.
FT   DOMAIN      293    361       GRAM 2.
FT   DOMAIN      515    702       Rab-GAP TBC.
FT   DOMAIN      886    921       EF-hand.
FT   COMPBIAS     31     41       Poly-Gly.
FT   MOD_RES     997    997       Phosphoserine (By similarity).
FT   VAR_SEQ     121    353       Missing (in isoform 2).
FT                                /FTId=VSP_025698.
FT   CONFLICT    376    376       N -> S (in Ref. 1; BAE22209).
FT   CONFLICT    465    465       T -> N (in Ref. 1; BAE22209).
FT   CONFLICT    544    544       G -> D (in Ref. 2; BAD32328).
FT   CONFLICT   1261   1261       A -> R (in Ref. 1; BAC36601).
SQ   SEQUENCE   1264 AA;  143024 MW;  CBCB4203FD6C48D3 CRC64;
     MWVNPEEVLL ANALWITERA NPYFILQRRK GHGGDGGGGG GLAGLLVGTL DVVLDSSARV
     APYRILYQTP DSLVYWTIAC GGSRKEVTEH WEWLEQNLLQ TLSIFENEND VTTFVRGKIQ
     GIIAEYNKIN DVKEDEDTEK FKEAIVKFHR LFGMPEEEKL VNYYSCSYWK GRVPRQGWMY
     LSINHLCFSS FLMGREAKLV IRWVDITQLE KNATLLLPDM IKVSTRSSEH FFSVFLNINE
     TFKLMEQLAN IAMRQLLDNE GFEQDRSLPK LKKKSPKKVS ALKRDLDARA KSERYRALFR
     LPKDEKLDGH TDCTLWTPFN KMHILGQMFV STNYICFTSK EENLCSLIIP LREVTIVEKA
     DSCSVLPSPL SISTRNRMTF LFANLKDRDF LVQRISDFLQ QTTSRIYSDK EFSGSCNSSD
     DEVYSRPSSL VSSSPQRSTS SDADGERPFN LNGNSVPTAT QTLMTMYRRR SPEEFNPKLA
     KEFLKEQAWK IHFAEYGQGI CMYRTEKTRE LVLKGIPESM RGELWLLLSG AINEKATHPG
     YYEGLVEKSM GKYNLATEEI ERDLHRSLPE HPAFQNEMGI AALRRVLTAY AFRNPNIGYC
     QAMNIVTSVL LLYAKEEEAF WLLVALCERM LPDYYNTRVV GALVDQGVFE ELARDYVPQL
     YDCMQDLGVI STISLSWFLT LFLSVMPFES AVVVVDCFFY EGIKVIFQLA LAVLDANVDK
     LLNCKDDGEA MTVLGRYLDS VTNKDSTLPP IPHLHSLLSD DVGPYPAVDI FRLIGTSYEK
     FGTIRADLIE QMRFKQRLKV IQTLEDTTKR NVVRTIVTET SFTIDELEEL YALFKAEHLT
     SCYWGGSSNA LDRHDPSLPY LEQYRIDFEQ FKGMFVLLFP WACGTHSDVL ASRLFQLLDE
     NGDSLINFRE FVSGLSAACH GDLTEKLKLL YKMHVLPEPS CDQDEPDSAF EATQYFFEDI
     TPECTHVVGL DSRGKQSADD GFVTVSLKQD RGKRANSQEN RNYLKLWTAE NKSKSKTAKD
     LPKLNQGQFI ELCKTMYNMF SEDPNEQELY HATAAVTSLL LEIGEVGKFF ITQPAKEDAV
     PGPPCGQAIP GMLFPKKGSS QSYVVESTEP LTASLAVDSE EHSLGGQMED IKLEDSSPRD
     NGACSSMLIS DDDTKDDSSM SSYSVLSAGS HEEDKLHCED IGEDTVLVRS SQGRATLPRS
     SSLDRDWAIT FEQFLASLLT EPALVRYFDK PVCMMARVTS AKNIRMMGKP LTSASDYEIS
     ALSG
//
ID   ARMX5_MOUSE             Reviewed;         606 AA.
AC   Q3UZB0; A2AGB5;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 44.
DE   RecName: Full=Armadillo repeat-containing X-linked protein 5;
GN   Name=Armcx5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; 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).
CC   -!- SIMILARITY: Contains 3 ARM repeats.
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DR   EMBL; AK133950; BAE21947.1; -; mRNA.
DR   EMBL; AL683822; CAM27374.1; -; Genomic_DNA.
DR   IPI; IPI00377388; -.
DR   RefSeq; NP_001009575.2; NM_001009575.4.
DR   UniGene; Mm.271980; -.
DR   ProteinModelPortal; Q3UZB0; -.
DR   PRIDE; Q3UZB0; -.
DR   Ensembl; ENSMUST00000096321; ENSMUSP00000094045; ENSMUSG00000072969.
DR   GeneID; 494468; -.
DR   KEGG; mmu:494468; -.
DR   UCSC; uc009uhk.1; mouse.
DR   CTD; 494468; -.
DR   MGI; MGI:2148026; Armcx5.
DR   HOGENOM; HBG127441; -.
DR   HOVERGEN; HBG080263; -.
DR   InParanoid; Q3UZB0; -.
DR   OMA; PSVGSWF; -.
DR   OrthoDB; EOG4FR0RK; -.
DR   NextBio; 411755; -.
DR   ArrayExpress; Q3UZB0; -.
DR   Bgee; Q3UZB0; -.
DR   Genevestigator; Q3UZB0; -.
DR   GermOnline; ENSMUSG00000072969; Mus musculus.
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.
DR   PROSITE; PS50176; ARM_REPEAT; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Repeat.
FT   CHAIN         1    606       Armadillo repeat-containing X-linked
FT                                protein 5.
FT                                /FTId=PRO_0000191373.
FT   REPEAT      349    388       ARM 1.
FT   REPEAT      470    509       ARM 2.
FT   REPEAT      511    551       ARM 3.
SQ   SEQUENCE   606 AA;  67895 MW;  4E48CBF48402219C CRC64;
     MIGSKTKRKA REESGASSKP GTNSPANAKG KAKNQTTKAV KAEPKEEWGN QAEARDEAVA
     RTQPAISTEP KTVTWKVKKK KDKTNARVMA QAKTELPAGP ALVPHTKSDA LPTSVVITVT
     KSEVKIDTGI EASLKGAAKA TDKRSIKQKP EIKKEVCVKS RAGDKAKEVC VKSSAGDKAK
     EVCVKSRAGD KAKEVCVKSR AGDKASIVIN TTDEDEDYVC SWFWTGEEPS VGSWFWPKEE
     NPLQVYQPPP KVEEEPEPPD TFDYALKKKA AAWLRGRFIV LVPIEEPQPS LPPDGNWTLV
     ATLIETPLGI RPLTKIPPYG GPYFQTLADL KNQIREKEKY GPNPNTCRCK SRTFSLEPVD
     FDKLVALLKL TRDPFIHEIA TMIMGISPAY PFTQDIVHDV GITVMIENFV NNPNAKKYPR
     TLNINANPDA PEEVKETEAH VNKVCRDILC CPLNCSVQVE ELKLLVSLSV KFDYHHVVIY
     YVRYFISLLN KGSVKIKFQI LRVLLCLSKN QANTRELISA EVMSSLVALF HKNESKANIL
     HIIEIFENIN FQFKKRAKLF TKEMFTKSEL ISIFREAKEF DQKLQDLTDH SDPDVRDKVI
     RLILKL
//
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.
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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   ITA1_MOUSE              Reviewed;        1179 AA.
AC   Q3V3R4;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Integrin alpha-1;
DE   AltName: Full=CD49 antigen-like family member A;
DE   AltName: Full=Laminin and collagen receptor;
DE   AltName: Full=VLA-1;
DE   AltName: CD_antigen=CD49a;
DE   Flags: Precursor;
GN   Name=Itga1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; 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: Integrin alpha-1/beta-1 is a receptor for laminin and
CC       collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-
CC       E-R in collagen (By similarity).
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-1
CC       associates with beta-1 (By similarity). Interacts with RAB21 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins
CC       with I-domains do not undergo protease cleavage.
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC   -!- SIMILARITY: Contains 7 FG-GAP repeats.
CC   -!- SIMILARITY: Contains 1 VWFA domain.
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DR   EMBL; AK035870; BAE20498.1; -; mRNA.
DR   IPI; IPI00466371; -.
DR   RefSeq; NP_001028400.2; NM_001033228.3.
DR   UniGene; Mm.317280; -.
DR   HSSP; P18614; 2B2X.
DR   ProteinModelPortal; Q3V3R4; -.
DR   SMR; Q3V3R4; 169-362, 378-665, 1136-1173.
DR   STRING; Q3V3R4; -.
DR   PhosphoSite; Q3V3R4; -.
DR   PRIDE; Q3V3R4; -.
DR   Ensembl; ENSMUST00000061673; ENSMUSP00000077132; ENSMUSG00000042284.
DR   GeneID; 109700; -.
DR   KEGG; mmu:109700; -.
DR   UCSC; uc007rxx.1; mouse.
DR   CTD; 109700; -.
DR   MGI; MGI:96599; Itga1.
DR   HOGENOM; HBG443663; -.
DR   HOVERGEN; HBG006185; -.
DR   InParanoid; Q3V3R4; -.
DR   OrthoDB; EOG4THVS7; -.
DR   NextBio; 362605; -.
DR   ArrayExpress; Q3V3R4; -.
DR   Bgee; Q3V3R4; -.
DR   CleanEx; MM_ITGA1; -.
DR   Genevestigator; Q3V3R4; -.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IMP:MGI.
DR   GO; GO:0045123; P:cellular extravasation; IMP:MGI.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0030593; P:neutrophil chemotaxis; 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   InterPro; IPR002035; VWF_A.
DR   Pfam; PF01839; FG-GAP; 1.
DR   Pfam; PF08441; Integrin_alpha2; 1.
DR   Pfam; PF00092; VWA; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   SMART; SM00191; Int_alpha; 5.
DR   SMART; SM00327; VWA; 1.
DR   PROSITE; PS51470; FG_GAP; 7.
DR   PROSITE; PS00242; INTEGRIN_ALPHA; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Disulfide bond; Glycoprotein; Integrin;
KW   Magnesium; Membrane; Receptor; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     28       By similarity.
FT   CHAIN        29   1179       Integrin alpha-1 (By similarity).
FT                                /FTId=PRO_0000273722.
FT   TOPO_DOM     29   1141       Extracellular (Potential).
FT   TRANSMEM   1142   1164       Helical; (Potential).
FT   TOPO_DOM   1165   1179       Cytoplasmic (Potential).
FT   REPEAT       30     91       FG-GAP 1.
FT   REPEAT      101    160       FG-GAP 2.
FT   DOMAIN      175    364       VWFA.
FT   REPEAT      365    417       FG-GAP 3.
FT   REPEAT      422    474       FG-GAP 4.
FT   REPEAT      475    537       FG-GAP 5.
FT   REPEAT      556    614       FG-GAP 6.
FT   REPEAT      618    678       FG-GAP 7.
FT   CA_BIND     497    505       Potential.
FT   CA_BIND     579    587       Potential.
FT   CA_BIND     641    649       Potential.
FT   MOTIF      1167   1171       GFFKR motif.
FT   CARBOHYD    100    100       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    105    105       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    112    112       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    217    217       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    317    317       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    341    341       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    402    402       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    418    418       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    459    459       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    531    531       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    698    698       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    747    747       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    779    779       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    839    839       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    882    882       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    907    907       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    938    938       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    965    965       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    973    973       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1007   1007       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1083   1083       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1102   1102       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1113   1113       N-linked (GlcNAc...) (Potential).
FT   DISULFID     82     92       By similarity.
FT   DISULFID    687    696       By similarity.
FT   DISULFID    702    755       By similarity.
FT   DISULFID    807    813       By similarity.
FT   DISULFID    877    885       By similarity.
FT   DISULFID   1029   1062       By similarity.
FT   DISULFID   1065   1072       By similarity.
SQ   SEQUENCE   1179 AA;  130809 MW;  EE919113E1E390B0 CRC64;
     MVPRRPASLE VTVACIWLLT VILGVCISFN VDVKNSMSFS GPVEDMFGYT VQQYENEEGK
     WVLIGSPLVG QPKARTGDVY KCPVGRERSM PCVKLDLPVN TSIPNVTEIK ENMTFGSTLV
     TNPKGGFLAC GPLYAYRCGH LHYTTGICSD VSPTFQVVNS FAPVQECSTQ LDIVIVLDGS
     NSIYPWESVT AFLNDLLKRM DIGPKQTQVG IVQYGANVTH EFNLNKYSST EEVLVAANKI
     GRRGGLQTMT ALGIDTARKE AFTEARGARR GVKKVMVIVT DGESHDNYRL KQVIQDCEDE
     NIQRFSIAIL GHYNRGNLST EKFVEEIKSI ASEPTEKHFF NVSDELALVT IVKALGERIF
     ALEATADQSA ASFEMEMSQT GFSAHYSQDW VMLGAVGAYD WNGTVVMQKA NQIVIPHNTT
     FQTEPTKMNE PLASYLGYTV NSATIPGDVL YIAGQPRYNH TGQVVIYKME DGDVNILQTL
     SGEQIGSYFG SVLTTIDIDK DSYTDLLLVG APMYMGTEKE EQGKVYVYAV NQTRFEYQMS
     LEPIKQTCCS SLKDNSCTKE NKNEPCGARF GTAVAAVKDL NVDGFNDVVI GAPLEDDHAG
     AVYIYHGSGK TIRKEYAQRI PSGGDGKTLK FFGQSIHGEM DLNGDGLTDV TIGGLGGAAL
     FWARDVAVVK VTMNFEPNKV NIQKKNCRVE GKETVCINAT MCFHVKLKSK EDSVYEADLQ
     YRVTLDSLRQ ISRSFFSGTQ ERRIQRNLTV RESECIRHSF YMLDKHDFQD SVRVTLDFNL
     TNPENGPVLD DALPNSVHGH IPFAKDCGNK ERCVSDLTLD VSTTEKNLLI VRSQNDKFNV
     SLTVKNKGDS AYNTRTVVQY SPNLIFSGIE EIQKDSCESN QNITCRVGYP FLRTGDVVNF
     KIIFQFNTSH LSENAIIHLS ATSDSEEPLE SLYDNEVNIS IPVKYEVGLQ FYSSASEHHI
     SVAANETVPE LINSTKDIGD EINVFYTIRK RGHFPMPELR LAISFPNLTS DGYPVLYPTG
     WSSSDNVNCR PRSLEDPLGI NSGKKMTISK SEVLKRGTIQ DCSTCKIATI TCHLLPSDVS
     QVNVSLILWK PTFIKAHFSS LNLTIRGELQ SENSSLTLSS SNRKRELAIQ ISKDGLPGRV
     PLWVILLSAF AGLLLLMLLI LALWKIGFFK RPLKKKMEK
//
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   FAM5C_MOUSE             Reviewed;         766 AA.
AC   Q499E0; Q8K0R9;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 2.
DT   08-MAR-2011, entry version 44.
DE   RecName: Full=Protein FAM5C;
DE   Flags: Precursor;
GN   Name=Fam5c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CD-1; TISSUE=Eye, 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   -!- SUBCELLULAR LOCATION: Secreted (Potential).
CC   -!- SIMILARITY: Belongs to the FAM5 family.
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DR   EMBL; BC030498; AAH30498.1; -; mRNA.
DR   EMBL; BC099956; AAH99956.1; -; mRNA.
DR   IPI; IPI00169621; -.
DR   RefSeq; NP_001139279.1; NM_001145807.1.
DR   RefSeq; NP_705767.3; NM_153539.3.
DR   UniGene; Mm.441817; -.
DR   ProteinModelPortal; Q499E0; -.
DR   SMR; Q499E0; 98-159.
DR   PRIDE; Q499E0; -.
DR   Ensembl; ENSMUST00000074622; ENSMUSP00000074201; ENSMUSG00000035131.
DR   GeneID; 215378; -.
DR   KEGG; mmu:215378; -.
DR   UCSC; uc007cxo.1; mouse.
DR   CTD; 215378; -.
DR   MGI; MGI:2443035; Fam5c.
DR   eggNOG; maNOG13335; -.
DR   GeneTree; ENSGT00390000008571; -.
DR   HOGENOM; HBG445938; -.
DR   HOVERGEN; HBG081412; -.
DR   InParanoid; Q499E0; -.
DR   OMA; PRQRTST; -.
DR   OrthoDB; EOG4TB49M; -.
DR   PhylomeDB; Q499E0; -.
DR   NextBio; 374682; -.
DR   ArrayExpress; Q499E0; -.
DR   Bgee; Q499E0; -.
DR   CleanEx; MM_B830045N13RIK; -.
DR   Genevestigator; Q499E0; -.
DR   GermOnline; ENSMUSG00000035131; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR020864; MACPF.
DR   Pfam; PF01823; MACPF; 1.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00457; MACPF; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Secreted; Signal.
FT   SIGNAL        1     33       Potential.
FT   CHAIN        34    766       Protein FAM5C.
FT                                /FTId=PRO_0000045775.
FT   CARBOHYD    168    168       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    337    337       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    456    456       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    562    562       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    609    609       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    641    641       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    599    599       T -> A (in Ref. 1; AAH99956).
SQ   SEQUENCE   766 AA;  88483 MW;  15BC4F2DAF813B71 CRC64;
     MIWRRRAGAE LSSLMALWEW IVLSLHCWVL AVAAVSDQHA TSPFDWLLSD KGPFHRSQEY
     TDFVDRSRQG FSTRYKIYRE FGRWKVNNLA VERRNFLGSP LPLAPEFFRN IRLLGRRPTL
     QQITENLIKK YGTHFLLSAT LGGEESLTIF VDKRKLSKRS EGSETSTNSS SVTLETLHQL
     AASYFIDRDS TLRRLHHIQI ASTAIKVTET RTGPLGCSNY DNLDSVSSVL VQSPENKIQL
     QGLQVLLPDY LQERFVQAAL SYIACNSEGE FICKDNDCWC HCGPKFPECN CPSMDIQAME
     ENLLRITETW KAYNSDFEDS DEFKFFMKRL PMNYFLNTST IMHLWTMDSN FQRRYEQLEN
     SMKQLFLKAH RIVHKLFSLS KRCHKQPLIS LPRQRTSTYW LTRIQSFLYC NENGLLGSFS
     EETHSCTCPN DQVVCTAFLP CTVGDASACL TCAPDNRTRC GTCNTGYMLS QGLCKPEVAE
     STDHYIGFET DLQDLEMKYL LQKTDRRIEV HAIFISNDMR LNSWFDPSWR KRMLLTLKSN
     KYKSSLVHMI LGLSLQICLT KNSTLEPVLA VYVNPFGGSH SESWFMPVSE SSFPDWERTK
     LDLPLQCYNW TLTLGNKWKT FFETVHIYLR SRIKANGPNS NESIYYEPLE FIDPSRNLGY
     MKINNIQVFG YSMHFDPEAI RDLILQLDYP YTQGSQDSAL LQLLEIRDRV NKLSPPGQRR
     LDLFSCLLRH RLKLSTSEVV RIQSALQAFN AKLPNTVDYD TTKLCS
//
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;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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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   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.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   Q4FJL2_MOUSE            Unreviewed;       780 AA.
AC   Q4FJL2;
DT   30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2005, sequence version 1.
DT   11-JAN-2011, entry version 49.
DE   SubName: Full=Putative uncharacterized protein;
DE   SubName: Full=Reticulon 1;
DE   SubName: Full=Reticulon 1, isoform CRA_a;
DE   SubName: Full=Rtn1 protein;
GN   Name=Rtn1; ORFNames=RP23-450G14.1-001, mCG_121605;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; 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   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   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Clark S.;
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
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   [7]
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   [8]
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   [9]
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   [10]
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   [11]
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   [12]
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; AK132364; BAE21127.1; -; mRNA.
DR   EMBL; CT010392; CAJ18599.1; -; mRNA.
DR   EMBL; CT010476; CAM46128.1; -; Genomic_DNA.
DR   EMBL; AC103353; CAM46128.1; JOINED; Genomic_DNA.
DR   EMBL; CH466526; EDL36535.1; -; Genomic_DNA.
DR   IPI; IPI00395193; -.
DR   RefSeq; NP_703187.2; NM_153457.6.
DR   UniGene; Mm.221275; -.
DR   ProteinModelPortal; Q4FJL2; -.
DR   SMR; Q4FJL2; 643-702.
DR   STRING; Q4FJL2; -.
DR   PRIDE; Q4FJL2; -.
DR   Ensembl; ENSMUST00000078505; ENSMUSP00000077594; ENSMUSG00000021087.
DR   GeneID; 104001; -.
DR   KEGG; mmu:104001; -.
DR   CTD; 104001; -.
DR   MGI; MGI:1933947; Rtn1.
DR   HOVERGEN; HBG008971; -.
DR   InParanoid; Q4FJL2; -.
DR   OMA; DSPLMKP; -.
DR   NextBio; 356325; -.
DR   ArrayExpress; Q4FJL2; -.
DR   Bgee; Q4FJL2; -.
DR   Genevestigator; Q4FJL2; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   InterPro; IPR003388; Reticulon.
DR   PANTHER; PTHR10994; Reticulon; 1.
DR   Pfam; PF02453; Reticulon; 1.
DR   PROSITE; PS50845; RETICULON; 1.
PE   2: Evidence at transcript level;
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   UBN1_MOUSE              Reviewed;        1135 AA.
AC   Q4G0F8; Q3UUZ4; Q6P9K7; Q8BNC3; Q9CRM4; Q9CS40;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Ubinuclein-1;
DE   AltName: Full=Ubiquitously expressed nuclear protein;
GN   Name=Ubn1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; 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 1-197 (ISOFORM 1/2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 557-1135 (ISOFORM 3).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryo, Placenta, Spinal ganglion, Vagina, 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].
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 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 70-1135 (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   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=18823282; DOI=10.1042/BC20080072;
RA   Aho S., Lupo J., Coly P.-A., Sabine A., Castellazzi M., Morand P.,
RA   Sergeant A., Manet E., Boyer V., Gruffat H.;
RT   "Characterization of the ubinuclein protein as a new member of the
RT   nuclear and adhesion complex components (NACos).";
RL   Biol. Cell 101:319-334(2009).
CC   -!- FUNCTION: Acts as a novel regulator of senescence. Involved in the
CC       formation of senescence-associated heterochromatin foci (SAHF),
CC       which represses expression of proliferation-promoting genes. Binds
CC       to proliferation-promoting genes. May be required for replication-
CC       independent chromatin assembly (By similarity).
CC   -!- SUBUNIT: Component of a complex that includes at least ASF1A,
CC       CABIN1, HIRA, histone H3.3 and UBN1. Interacts with HIRA (via WD
CC       repeat domain); the interaction is direct. Interacts with ASF1A,
CC       CEBPA, TJP1, TJP2 and TJP3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm (By similarity).
CC       Nucleus, PML body (By similarity). Cell junction, tight junction.
CC       Note=Localized as a nuclear speckled-like pattern in proliferating
CC       primary fibroblasts. Colocalizes with HIRA, PML and SP100 in PML
CC       bodies of senescent cells. Colocalizes with CLDN1. Detected along
CC       the upper granular cell layer of epidermis. When overexpressed,
CC       accumulates in the nucleus in cells showing defective cytokinesis
CC       (By similarity). Colocalizes with TJP1.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q4G0F8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q4G0F8-2; Sequence=VSP_036972;
CC       Name=3;
CC         IsoId=Q4G0F8-3; Sequence=VSP_036973;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in bile canaliculi in liver, in
CC       bronchiolar epithelium in lung and in tubular structures of gland
CC       ducts inside the olfactory epithelium and tongue epithelium.
CC   -!- SIMILARITY: Belongs to the ubinuclein family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDK97277.1; Type=Erroneous gene model prediction;
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DR   EMBL; AK019173; BAB31587.1; -; mRNA.
DR   EMBL; AK020146; BAB32010.1; -; mRNA.
DR   EMBL; AK084046; BAC39106.1; -; mRNA.
DR   EMBL; AK137727; BAE23479.1; -; mRNA.
DR   EMBL; AK147571; BAE28001.1; -; mRNA.
DR   EMBL; CH466521; EDK97277.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC060723; AAH60723.1; -; mRNA.
DR   EMBL; BC098372; AAH98372.1; -; mRNA.
DR   IPI; IPI00352675; -.
DR   IPI; IPI00625369; -.
DR   IPI; IPI00929767; -.
DR   RefSeq; NP_080942.1; NM_026666.3.
DR   UniGene; Mm.66356; -.
DR   ProteinModelPortal; Q4G0F8; -.
DR   STRING; Q4G0F8; -.
DR   PhosphoSite; Q4G0F8; -.
DR   PRIDE; Q4G0F8; -.
DR   Ensembl; ENSMUST00000052449; ENSMUSP00000061843; ENSMUSG00000039473.
DR   GeneID; 170644; -.
DR   KEGG; mmu:170644; -.
DR   UCSC; uc007ybq.1; mouse.
DR   CTD; 170644; -.
DR   MGI; MGI:1891307; Ubn1.
DR   eggNOG; roNOG06944; -.
DR   GeneTree; ENSGT00530000063595; -.
DR   HOGENOM; HBG278124; -.
DR   InParanoid; Q4G0F8; -.
DR   OMA; FSKAGFT; -.
DR   NextBio; 370145; -.
DR   ArrayExpress; Q4G0F8; -.
DR   Bgee; Q4G0F8; -.
DR   Genevestigator; Q4G0F8; -.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0030216; P:keratinocyte differentiation; TAS:MGI.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Cell junction; Chromatin regulator;
KW   Coiled coil; DNA-binding; Nucleus; Phosphoprotein; Tight junction.
FT   CHAIN         1   1135       Ubinuclein-1.
FT                                /FTId=PRO_0000370691.
FT   COILED      476    539       Potential.
FT   COMPBIAS    181    261       Lys-rich.
FT   COMPBIAS    861   1032       Ser-rich.
FT   MOD_RES     173    173       Phosphoserine (By similarity).
FT   MOD_RES     175    175       Phosphoserine (By similarity).
FT   MOD_RES     222    222       N6-acetyllysine (By similarity).
FT   MOD_RES     336    336       Phosphoserine (By similarity).
FT   MOD_RES     493    493       Phosphoserine (By similarity).
FT   MOD_RES     660    660       Phosphoserine (By similarity).
FT   MOD_RES     677    677       Phosphoserine (By similarity).
FT   MOD_RES    1028   1028       Phosphoserine (By similarity).
FT   VAR_SEQ    1090   1120       SLLAGLHSSPPHTAPLPHAAVSTHVPQSLPD -> N (in
FT                                isoform 2).
FT                                /FTId=VSP_036972.
FT   VAR_SEQ    1091   1135       LLAGLHSSPPHTAPLPHAAVSTHVPQSLPDASQLHGKGPVV
FT                                PRKL -> KFLSPASVPMLCAMLGPVCVWCNHGNIPHLWKL
FT                                HSTRDSCFVPDWSAGCLGL (in isoform 3).
FT                                /FTId=VSP_036973.
FT   CONFLICT    184    184       K -> N (in Ref. 1; BAB31587).
FT   CONFLICT    681    681       A -> G (in Ref. 1; BAC39106).
FT   CONFLICT    801    801       G -> A (in Ref. 1; BAC39106).
FT   CONFLICT    969    969       A -> P (in Ref. 1; BAC39106).
SQ   SEQUENCE   1135 AA;  122336 MW;  8B5994B86F97E0F7 CRC64;
     MSEPHRVQFT SVPGSLNPAF LKKSRKEEVG GTEQHQDCEP AAAAVRITLT LFEPDHKRCP
     EFFYPELVKN IRGKVKGLHP GDKKKDVLDP FNDEEKERHK VEALARKFEE KYGGKKRRKD
     RIQDLIDMGY GYDESDSFID NSEAYDELVP ASLTTKYGGF YINSGTLQFR QASESEDDFI
     KEKKKKSPKK RKLKEGGEKI KKKKKDDTYD KEKKSKKSKF SKAGFTALNA SKEKKKKKYS
     GSLSVREMLK KFQKEKEAQK KREEEHKPVA VSSIEAQGLR ELEGTSDPLL SLFGSTSDND
     LLQAATAMDS LTDLDLEQLL SESPEGSPFR DMDDGSDSLG VGLDQEFRQP SSFPEGLPIP
     LEKRVKELAQ AARAAEGESK QKFFTQDING ILLDIEVQTR ELTSQIRSGV FAYLASFLPC
     SKDALVKRAR KLHLYEQGGR LKEPLQKLKD AIGRAMPEQV AKYQDECQAH TQAKVAKMLE
     EEKDKEQRER ICSDEEEDEE KGGRRIMGPR KKFQWNDEIR ELLCQVVKIK LESRDLERNS
     KAQAWEDCVK AFLDAEVKPL WPKGWMQART LFKESRRGHG HLTSLLAKKK VIAPSKIKMK
     ESSVKLDKKV SVPSGQHGGP TTLLSEHQGG GLNTGANSRE HPSQATCGLT DSVSVTLEDS
     LDEDLVRNPA SSVDAVSKEL ATLNSRAANS SEFTLPTPSK APTEKVGGVL CTEEKRNFAK
     PSSSAPPPTN ALQSPLNFLA EQALALGQSS QEKKPEGSGF KELSCQGPLS KGVPELHPSK
     AKHHNLPRTS HGPQAAAPVP GPQVKVFHAG TQQQKSFTPP SPFVNKLQGP KATSPQCHRS
     LLQLVKTAAK GQAFHATMPA SSGSSPASSS SAHKTTASNS TTISHPAKLH PTSSVGPSYK
     NNPFAGSVSK HGASSSSPSP GGGAQVQSSV SGASLPGVQS PSAGQSASRA APSSAVKKTP
     VTQKLTLVAP PGGPNGDSGG GTQGVAKLLT SSLKPAAVSS VTSSTSLPKG TGGAVLLSNT
     SSLSLLSSSY KSNNPKLPGA MNSNSLGIIT QFPLHVLSFN ADSSAKAGVS KDAIVTGPAP
     GTFHHGLSHS LLAGLHSSPP HTAPLPHAAV STHVPQSLPD ASQLHGKGPV VPRKL
//
ID   ABL2_MOUSE              Reviewed;        1182 AA.
AC   Q4JIM5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Tyrosine-protein kinase ABL2;
DE            EC=2.7.10.2;
DE   AltName: Full=Abelson murine leukemia viral oncogene homolog 2;
DE   AltName: Full=Abelson-related gene protein;
DE   AltName: Full=Tyrosine-protein kinase ARG;
GN   Name=Abl2; Synonyms=Arg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=129/SvJ;
RX   MEDLINE=21625084; PubMed=11752434; DOI=10.1073/pnas.251249298;
RA   Wang Y., Miller A.L., Mooseker M.S., Koleske A.J.;
RT   "The Abl-related gene (Arg) nonreceptor tyrosine kinase uses two F-
RT   actin-binding domains to bundle F-actin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:14865-14870(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], CAP DOMAIN, FUNCTION, ENZYME REGULATION,
RP   INTERACTION WITH CRK, AUTOPHOSPHORYLATION AT TYR-272; TYR-439; TYR-568
RP   AND TYR-684, AND MUTAGENESIS OF TYR-272; LYS-317; TYR-439; TYR-568 AND
RP   TYR-684.
RC   STRAIN=129/SvJ;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-439, 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-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-632, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., 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-621, 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: Regulates cytoskeleton remodeling during cell
CC       differentiation, cell division and cell adhesion. Localizes to
CC       dynamic actin structures, and phosphorylates CRK and CRKL, DOK1,
CC       and other proteins controlling cytoskeleton dynamics.
CC       Phosphorylates PSMA7 that leads to an inhibition of proteasomal
CC       activity and cell cycle transition blocks (By similarity).
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). Interacts with
CC       PSMA7 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
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; DQ084361; AAY86039.1; -; mRNA.
DR   IPI; IPI00117039; -.
DR   UniGene; Mm.329515; -.
DR   HSSP; P00519; 2G2F.
DR   ProteinModelPortal; Q4JIM5; -.
DR   SMR; Q4JIM5; 110-558, 1081-1182.
DR   STRING; Q4JIM5; -.
DR   PRIDE; Q4JIM5; -.
DR   Ensembl; ENSMUST00000027888; ENSMUSP00000027888; ENSMUSG00000026596.
DR   UCSC; uc007dcl.1; mouse.
DR   MGI; MGI:87860; Abl2.
DR   eggNOG; roNOG09900; -.
DR   HOGENOM; HBG446901; -.
DR   HOVERGEN; HBG004162; -.
DR   InParanoid; Q4JIM5; -.
DR   OrthoDB; EOG4NS39R; -.
DR   BRENDA; 2.7.10.2; 244.
DR   ArrayExpress; Q4JIM5; -.
DR   Bgee; Q4JIM5; -.
DR   Genevestigator; Q4JIM5; -.
DR   GermOnline; ENSMUSG00000026596; Mus musculus.
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: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:0051017; P:actin filament bundle assembly; IDA:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   ATP-binding; Cell adhesion; Cytoplasm; Cytoskeleton; Kinase;
KW   Lipoprotein; Magnesium; Manganese; Metal-binding; Myristate;
KW   Nucleotide-binding; Phosphoprotein; SH2 domain; SH3 domain;
KW   Transferase; Tyrosine-protein kinase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1182       Tyrosine-protein kinase ABL2.
FT                                /FTId=PRO_0000258019.
FT   DOMAIN      107    167       SH3.
FT   DOMAIN      173    263       SH2.
FT   DOMAIN      288    539       Protein kinase.
FT   NP_BIND     294    302       ATP (By similarity).
FT   NP_BIND     362    368       ATP (By similarity).
FT   REGION        2    106       CAP.
FT   MOTIF       427    451       Kinase activation loop (By similarity).
FT   MOTIF       659    661       Nuclear localization signal (Potential).
FT   ACT_SITE    409    409       Proton acceptor (By similarity).
FT   BINDING     317    317       ATP.
FT   MOD_RES      71     71       Phosphoserine (By similarity).
FT   MOD_RES      96     96       Phosphoserine (By similarity).
FT   MOD_RES     116    116       Phosphotyrosine (By similarity).
FT   MOD_RES     203    203       Phosphoserine (By similarity).
FT   MOD_RES     231    231       Phosphotyrosine (By similarity).
FT   MOD_RES     272    272       Phosphotyrosine; by autocatalysis.
FT   MOD_RES     275    275       Phosphoserine (By similarity).
FT   MOD_RES     299    299       Phosphotyrosine (By similarity).
FT   MOD_RES     303    303       Phosphotyrosine (By similarity).
FT   MOD_RES     310    310       Phosphotyrosine (By similarity).
FT   MOD_RES     439    439       Phosphotyrosine; by autocatalysis and
FT                                SRC-type Tyr-kinases.
FT   MOD_RES     440    440       Phosphothreonine (By similarity).
FT   MOD_RES     492    492       Phosphoserine (By similarity).
FT   MOD_RES     515    515       Phosphotyrosine (By similarity).
FT   MOD_RES     568    568       Phosphotyrosine; by autocatalysis.
FT   MOD_RES     621    621       Phosphoserine.
FT   MOD_RES     632    632       Phosphoserine.
FT   MOD_RES     634    634       Phosphoserine (By similarity).
FT   MOD_RES     656    656       Phosphoserine (By similarity).
FT   MOD_RES     672    672       Phosphoserine (By similarity).
FT   MOD_RES     684    684       Phosphotyrosine; by autocatalysis.
FT   MOD_RES     719    719       Phosphotyrosine (By similarity).
FT   MOD_RES     783    783       Phosphoserine (By similarity).
FT   MOD_RES     785    785       Phosphoserine (By similarity).
FT   MOD_RES     786    786       Phosphothreonine (By similarity).
FT   MOD_RES     817    817       Phosphothreonine (By similarity).
FT   MOD_RES     819    819       Phosphoserine (By similarity).
FT   MOD_RES     820    820       Phosphothreonine (By similarity).
FT   MOD_RES     821    821       Phosphoserine (By similarity).
FT   MOD_RES     822    822       Phosphoserine (By similarity).
FT   MOD_RES     915    915       Phosphoserine (By similarity).
FT   MOD_RES     936    936       Phosphoserine (By similarity).
FT   MOD_RES     938    938       Phosphothreonine (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
FT   MUTAGEN     272    272       Y->F: Minimal reduction in ability to
FT                                autophosphorylate.
FT   MUTAGEN     317    317       K->M: Loss of kinase activity.
FT   MUTAGEN     439    439       Y->F: Partial reduction in ability to
FT                                autophosphorylate.
FT   MUTAGEN     568    568       Y->F: No reduction in ability to
FT                                autophosphorylate.
FT   MUTAGEN     684    684       Y->F: Minimal reduction in ability to
FT                                autophosphorylate.
SQ   SEQUENCE   1182 AA;  128196 MW;  08507298A9081228 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 SLTVAVKTFK 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 HKKYELTGNF SPVASLQNAD GFSVAPSQQE PNLVPAKCYG
     GSFAQRNLCA DDDSGGGGGS GTAGGGWSGI TGFFTPRLIK KTLGLRAGKP TASDDTSKPF
     PRSNSTSSMS SGLPEQDRMA MTLPRNCQRS KLQLERTVST SSQPEENVDR ANDMLPKKSE
     EGAAPARERP KAKLLPRGAT ALPLRAPDPA ITESDSPGVG VAGVAAAPKG KERNGGTRLG
     VAGVPEDGEQ LGWSSPAKAV AVLPTTHNHK VPVLISPTLK HTPADVQLIG TDSQGNKFKL
     LSEHQVTSSG DKDRPRRVKP KCAPPPPPVM RLLQHPSTCS DPEEEPTAPP AGQHTPETQE
     GGKKAAPGPV PSSGKPGRPV MPPPQVPLPT SSISPAKMAN GTAGTKVALR KTKQAAEKIS
     ADKISKEALL ECADLLSSAI TEPVPNSQLV DTGHQLLDYC SGYVDSIPQT RNKFAFREAV
     SKLELSLQEL QVSSTAAGVP GTNPVLNNLL SCVQEISDVV QR
//
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;
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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   Q4VBF3_MOUSE            Unreviewed;       824 AA.
AC   Q4VBF3;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   08-MAR-2011, entry version 32.
DE   SubName: Full=Sipa1l3 protein;
DE   Flags: Fragment;
GN   Name=Sipa1l3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; 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).
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
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DR   EMBL; BC095969; AAH95969.1; -; mRNA.
DR   IPI; IPI00221567; -.
DR   UniGene; Mm.375176; -.
DR   UniGene; Mm.447042; -.
DR   PhosphoSite; Q4VBF3; -.
DR   Ensembl; ENSMUST00000085809; ENSMUSP00000082965; ENSMUSG00000030583.
DR   UCSC; uc009gbr.1; mouse.
DR   MGI; MGI:1921456; Sipa1l3.
DR   HOGENOM; HBG445166; -.
DR   HOVERGEN; HBG056135; -.
DR   InParanoid; Q4VBF3; -.
DR   ArrayExpress; Q4VBF3; -.
DR   Bgee; Q4VBF3; -.
DR   Genevestigator; Q4VBF3; -.
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   824 AA;  89772 MW;  F17AB26E360E9BEB CRC64;
     MTNGWETVDM TLRRNGLGQL GFHVKYDGTV AEVEDYGFAW QAGLRQGSRL VEICKVAVVT
     LSHDQMIDLL RTSVTVKVVI IPPFEDGTPR RGWPETYDMN ASEPKTESET TTPGGRPPYR
     SNAPWQWSGP ASHNSLPATK WTTPATPGHA QSLSRLPKQT PVVPFRESQP LHSKRPVSFP
     ETPFAASPAG ADRVPPYRQP SGSFSTPGSA TYARYKPSPE RYAAAPHPLL SFDPHFMHDG
     MSSGDSSSGG LTSQESTMER PKPEPLWHVP AQARLSAMTG SIGSKHPSRQ DAAGKDSPNR
     HSKGEPQYSS HSSSNTLSSN ASSSHSDDRW FDPLDPLEPE QDPFSKGGSS DSGIDTTLYT
     SSPSCMSLAK APRPTKPHKP PGNIGLCGGG RESAGRPHPV DRRREVSPAP VVAGQNKGYR
     PKLYSSGSCT PPGLVGGSRD PPRQPSDMGS RAGYPTQVYK TASAETPRPS QLSQCSPFQL
     STSVPKSFFS KQPAHNKHST GWKRTDEPPP RPLPFTDSKK QVDTNAKNVF GQPRLRASLR
     DLRSPRKNYK STIEDDLKKL IVMDNLGPEQ ERDTGSPQKS LQRTLSDESL CSGRREPSFA
     SPASLEPGLP SDVLFTSTCT FPSSTLPARR QHQHAHPPSG APSTTPATGN GFPEKKSAIS
     ASELSLADGR DRPLRRLDPG MMPLPDTAAG LEWSSLVNAA KAYEVQRAVS LFSLNDPALS
     PEIPPAHSPV HSHLSLERGP QTPRATPTMS EESPLDLTGK VYQLEVMLKQ LHTDLQKEKQ
     DKVVLQSEVA SLRQNNQRLQ EESQAASEQL RKFAELFSRE KKEL
//
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   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.
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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   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   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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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   Q571B1_MOUSE            Unreviewed;       512 AA.
AC   Q571B1;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   08-MAR-2011, entry version 30.
DE   SubName: Full=MKIAA4035 protein;
DE   Flags: Fragment;
GN   Name=Gltscr1; Synonyms=mKIAA4035;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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; AK220278; BAD90203.1; -; mRNA.
DR   IPI; IPI00340401; -.
DR   UniGene; Mm.440249; -.
DR   ProteinModelPortal; Q571B1; -.
DR   STRING; Q571B1; -.
DR   PhosphoSite; Q571B1; -.
DR   Ensembl; ENSMUST00000094821; ENSMUSP00000092416; ENSMUSG00000070808.
DR   MGI; MGI:2154263; Gltscr1.
DR   eggNOG; roNOG04287; -.
DR   GeneTree; ENSGT00530000063935; -.
DR   HOGENOM; HBG506023; -.
DR   InParanoid; Q571B1; -.
DR   OrthoDB; EOG451DS5; -.
DR   ArrayExpress; Q571B1; -.
DR   Bgee; Q571B1; -.
DR   Genevestigator; Q571B1; -.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   512 AA;  54889 MW;  EFE1094B46CF729F CRC64;
     PFLLPQYDSK LCSLKKQPLL QPSKEACFLE HLHKHQGSVL HPDYKTAFPS FEDALHRLLP
     YHVYQGALPS PNDYHKVDEE FETVSTQLLK RTQAMLNKYR LLLLEESRRV SPSAEMVMID
     RMFIQEEKTT LALDKQLAKE KPDEYVSSSR SLGFPVPVSS EGHRLPSHGQ SSSSSTSGTS
     AQPPPHLPTK LVIRHGGAGG SPSVTWARAS SSLSSTSSSS SSSSAASSLD ADEDGPMPTR
     NRPPIKTYEA RSRIGLKLKI KQEAGLSKVV HNTALDPVHQ PLPAPTPAKG AEPPPHPAPP
     PLPPATQAQM NGTLDHPPPA VRKPTVPASC PRLPLRKTYR ENMGNPGAAE GAQGRPRGAG
     SPTPLPTKVD EATSGLIREL AAVEDELYQR VLKGGPPPPE TPASATSQGP TEPSWEAPVL
     PPAKRRKSES PDVDQASFSS DSPQDDTLTE HLQSAIDSIL NLQQAPGRTP AGPYPHTGPT
     PGTPTSPAPL HRPDAFPPSS HNGGLGARTL NR
//
ID   Q571B7_MOUSE            Unreviewed;      1806 AA.
AC   Q571B7;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   08-FEB-2011, entry version 31.
DE   SubName: Full=MKIAA1884 protein;
DE   Flags: Fragment;
GN   Name=Csmd2; Synonyms=mKIAA1884;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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; AK220272; BAD90197.1; -; mRNA.
DR   IPI; IPI00754326; -.
DR   UniGene; Mm.392376; -.
DR   UniGene; Mm.421342; -.
DR   UniGene; Mm.482037; -.
DR   PRIDE; Q571B7; -.
DR   Ensembl; ENSMUST00000074081; ENSMUSP00000073724; ENSMUSG00000028804.
DR   UCSC; uc008uvb.1; mouse.
DR   MGI; MGI:2386401; Csmd2.
DR   GeneTree; ENSGT00600000084158; -.
DR   HOVERGEN; HBG051134; -.
DR   ArrayExpress; Q571B7; -.
DR   Bgee; Q571B7; -.
DR   Genevestigator; Q571B7; -.
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; 13.
DR   Gene3D; G3DSA:2.60.120.290; CUB; 8.
DR   Pfam; PF00431; CUB; 8.
DR   Pfam; PF00084; Sushi; 13.
DR   SMART; SM00032; CCP; 13.
DR   SMART; SM00042; CUB; 8.
DR   SUPFAM; SSF57535; Complement_control_module; 13.
DR   SUPFAM; SSF49854; CUB; 8.
DR   PROSITE; PS01180; CUB; 8.
DR   PROSITE; PS50923; SUSHI; 13.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   1806 AA;  196651 MW;  D32089B680FDB48D CRC64;
     PFPASPGTVW RARPASRAWG ADGACGARLC QAECGNSVTG TQGTLLSPNF PVNYNNNHEC
     IYSIQTQPGK GIQLKAKAFE LAEGDLLKVY DGTNNSARLL GVFSRSEMLG VTLNSTSSSL
     WLDFITDAEN TSKGFELQFS SFELIRCEDP GTPQFGYKVH DGGHFAGSSV TFSCDPGYSL
     RGSEELMCLS GERRTWDRPL PTCVAECGGT VRGEVSGQVL SPGYPAPYEH NLNCIWTIEA
     DAGCTIGLHF LVFDTEEVHD VLRIWDGPVE SGVLLKELSG PMLPKDLHST FNSVVLQFST
     DFFTSKQGFA IQFSVSTATS CNDPGVPQNG SRSGDSWEAG DSTVFQCDPG YALQGSAEIS
     CVKIQNRFFW QPSPPTCIAP CGGDLTGPSG VILSPNYPEP YPPGKECDWK VTVSPDYVIA
     LVFNTFNLEP GYDFLHIYDG RDSLSPLIGS FYGSQLPSRI ESSSNSLFLA FRSDASVSNA
     GFVIDYTENP RESCFDPGSI KNGTRVGSDL KLGSSVTYYC HGGYEVEGAS TLSCILGPDG
     KPMWNNPRPV CTAPCGGQYV GSDGVVLSPN YPQNYTSGQT CLYFVTVPKD YVVFGQFAFF
     HTALNDIVEV HDGYSQHSRL LSSLSGSHTG ESLPLATSNQ VLIKFSAKGQ VSARGFHFVY
     QAVPRTSATQ CSSVPEPRYG KRLGSDFSVG AIIRFECNSG YALQGSPEIE CLPVPGALAQ
     WNVSAPTCVV PCGGNLTERR GTILSPGFPE PYLNSLNCVW KIMVPEGAGI QIQVISFVTE
     QNWDSLEVFD GADNTVTMLG SFSGTTVPAL LNSTSNQLYL HFYSDISVSA AGFHLEYKTV
     GLSSCPEPAV PSNGVKTGER YLVNDVVSFQ CEPGYALQGH AHISCMPGTV RRWNYPPPLC
     IAQCGGAVEE MEGVILSPGF PGNYPSNMDC SWKISLPVGF GAHIQFLNFS TEPNHDFLEI
     RSGPSETSRM MGRFSGSELP GSLLSTSHDS IVYFHSDHSQ NRPGFKLEYQ AYELQECPDP
     EPFANGIVRG AGYNVGQSVT FECLPGYQLT GQPVLTCQHG TNRNWDHPLP RCEVPCGGNI
     TSFNGTVYSP GYPSPYSSSQ DCVWQITVPI GHGVHLNLSL LQIEPFGDYI TVWDGPQQTS
     LQLGVFTRSL SKKIAHSSSN QVLLKFHRDT ATGGIFAIAF SAYPLTKCPP PTILPNAEVV
     TENEEFNIGD IVRYRCLPGF TLVGSEILTC KLGTYLQFEG PPPICEVHCP TNELLTDSTG
     VILSQSYPGS YPQFQTCSWL VRVEPEYNIS ITVEYFLSEK QYDEFEIFDG PSGQSPLLKA
     LSGNYSAPLI VTSSSNSVYL RWSSDHAYNR KGFKIRYSAP YCSLPKAPLH GFILGQTTTQ
     PGGSIHFGCN TGYRLVGHSM AICTRHPQGY HLWSEAIPLC QALSCGLPDA PKNGIVFGKE
     YTVGTKAVYS CNEGYHLQAG AEATAECLDT GLWSNSNVPP QCVPVTCPDI SSISVEHGRW
     RLIFETQYQF QAQLMLICDP GYYYTGQRVI RCQANGRWSL GESMPTCQII SCGELPTPPS
     GHRIGTMSVY GATAIFSCNS GYTLVGSRVR ECMANGLWSG SEVRCLAGHC GTPEPIVNGH
     INGENFNYRG SVVYQCRAGF RLIGMSVRIC QQDHHWSGKT PFCVPITCGH PGNPVNGLTQ
     GSQFNLNDVV KFICNPGYIA EGAARSQCLA SGQWSDTLPT CRIINCTDPG HQENSVRQVH
     TSGPHRLSPS PTIPVSTTSI PRGKKKSKTK TKKKSFVQRY IFIIQSLYST KKRQEKKVYI
     FFHYCR
//
ID   LIN54_MOUSE             Reviewed;         749 AA.
AC   Q571G4; A0JLY2; Q3KQN0; Q3UYW5; Q8BMU8; Q8C107;
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=Protein lin-54 homolog;
GN   Name=Lin54; Synonyms=Kiaa2037;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; 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=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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
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] OF 66-749 (ISOFORM 1).
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: Component of the DREAM complex, a multiprotein complex
CC       that can both act as a transcription activator or repressor
CC       depending on the context. In G0 phase, the complex binds to more
CC       than 800 promoters and is required for repression of E2F target
CC       genes. In S phase, the complex selectively binds to the promoters
CC       of G2/M genes whose products are required for mitosis and
CC       participates in their cell cycle dependent activation. In the
CC       complex, acts as a DNA-binding protein that binds the promoter of
CC       CDK1 in a sequence-specific manner (By similarity).
CC   -!- SUBUNIT: Component of the DREAM complex (also named LINC complex)
CC       at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1,
CC       MYBL2, RBL1, RBL2, RBBP4, RBL2, TFDP1 and TFDP2. The complex
CC       exists in quiescent cells where it represses cell cycle-dependent
CC       genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54
CC       form a subcomplex that binds to MYBL2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q571G4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q571G4-2; Sequence=VSP_034277;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q571G4-3; Sequence=VSP_034278, VSP_034279;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The CXC domains mediate DNA-binding (By similarity).
CC   -!- SIMILARITY: Belongs to the lin-54 family.
CC   -!- SIMILARITY: Contains 2 CXC domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI06127.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=BAD90150.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK220225; BAD90150.1; ALT_INIT; mRNA.
DR   EMBL; AK028016; BAC25700.1; -; mRNA.
DR   EMBL; AK029288; BAC26373.1; -; mRNA.
DR   EMBL; AK134320; BAE22096.1; -; mRNA.
DR   EMBL; BC106126; AAI06127.1; ALT_SEQ; mRNA.
DR   EMBL; BC125580; AAI25581.1; -; mRNA.
DR   IPI; IPI00223922; -.
DR   IPI; IPI00895977; -.
DR   IPI; IPI00955725; -.
DR   RefSeq; NP_001108482.1; NM_001115010.1.
DR   RefSeq; NP_766302.2; NM_172714.4.
DR   UniGene; Mm.212568; -.
DR   ProteinModelPortal; Q571G4; -.
DR   STRING; Q571G4; -.
DR   PhosphoSite; Q571G4; -.
DR   PRIDE; Q571G4; -.
DR   Ensembl; ENSMUST00000046154; ENSMUSP00000041374; ENSMUSG00000035310.
DR   Ensembl; ENSMUST00000094577; ENSMUSP00000092156; ENSMUSG00000035310.
DR   GeneID; 231506; -.
DR   KEGG; mmu:231506; -.
DR   CTD; 231506; -.
DR   MGI; MGI:2140902; Lin54.
DR   eggNOG; roNOG09183; -.
DR   GeneTree; ENSGT00390000013974; -.
DR   HOGENOM; HBG715537; -.
DR   HOVERGEN; HBG108088; -.
DR   InParanoid; Q571G4; -.
DR   OMA; FGRCLMR; -.
DR   NextBio; 380584; -.
DR   ArrayExpress; Q571G4; -.
DR   Bgee; Q571G4; -.
DR   Genevestigator; Q571G4; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; IPR005172; CXC.
DR   Pfam; PF03638; CXC; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; Activator; Alternative splicing; Cell cycle; DNA-binding;
KW   Nucleus; Phosphoprotein; Repeat; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    749       Protein lin-54 homolog.
FT                                /FTId=PRO_0000341390.
FT   DOMAIN      520    560       CXC 1.
FT   DOMAIN      594    635       CXC 2.
FT   MOD_RES     244    244       N6-acetyllysine (By similarity).
FT   MOD_RES     249    249       N6-acetyllysine (By similarity).
FT   MOD_RES     282    282       Phosphoserine (By similarity).
FT   MOD_RES     310    310       Phosphoserine (By similarity).
FT   MOD_RES     314    314       Phosphoserine (By similarity).
FT   MOD_RES     357    357       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1    330       Missing (in isoform 2).
FT                                /FTId=VSP_034277.
FT   VAR_SEQ     229    237       IAKKPRTPT -> VKTKKGHIT (in isoform 3).
FT                                /FTId=VSP_034278.
FT   VAR_SEQ     238    749       Missing (in isoform 3).
FT                                /FTId=VSP_034279.
SQ   SEQUENCE   749 AA;  79566 MW;  9A547A07B7216394 CRC64;
     MEVVPAEVNS LLPDDIMDTA ITLVDEDSIE AVIVSSPIPM ETELEEIVNI NSTGDSTATP
     ISTEPITVYS NHTNQVAVNT TVSKADSNTT VKPAFPSGLQ KLGAQTPVTI SANQIILNKV
     SQTSDLKLGN QTLKPDGQKL ILTTLGKSGS PIVLALPHSQ LPQAQKVTAQ AQPGDAKLPP
     QQIKVVTIGG RPEVKPVIGV SALTPGSQLI NTTTQPSVLQ TQQLKTVQIA KKPRTPTSGP
     VITKLIFAKP INSKAVTGQT TQASPPVVTG RVLSQSTPGT PSKTITISES GVIGSTLNST
     TQTPNKIAIS PLKSPNKTVK SAVQTITVGG MSTSQFKTII PLATAPNVQQ IQVPGSKFHY
     VRLVTATTAS SSAQPVSQSP SVNTQPLQQA KPVVVNTTPV RMSVPFVQAQ AVKQVVPKPI
     NSTSQIVTTS QPQQRLIMPA TPLPQIQPNL TNLPPGTVLA PAPGTGNVGY AVLPAQYVTQ
     LQQSSYVSIA SNSNFTGTSG IQTQARLPFN GIIPSESTSR PRKPCNCTKS LCLKLYCDCF
     ANGEFCNNCN CTNCYNNLEH ENERQKAIKA CLDRNPEAFK PKIGKGKEGE SDRRHSKGCN
     CKRSGCLKNY CECYEAKIMC SSICKCIGCK NFEESPERKT LMHLADAAEV RVQQQTAAKT
     KLSSQISDLL TRPTPALNSA GGKLPFTFVT KEVAEATCNC LLAQAEQADK KGKSKAAAER
     MILEEFGRCL MSVINSAGKA KSDPCAMHC
//
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;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   Q59IW6_MOUSE            Unreviewed;      1179 AA.
AC   Q59IW6;
DT   26-APR-2005, integrated into UniProtKB/TrEMBL.
DT   26-APR-2005, sequence version 1.
DT   11-JAN-2011, entry version 44.
DE   SubName: Full=Target of Nesh-SH3 variant 5;
GN   Name=Abi3bp; Synonyms=TARSH;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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=15752759; DOI=10.1016/j.bbrc.2005.02.068;
RA   Uekawa N., Terauchi K., Nishikimi A., Shimada J., Maruyama M.;
RT   "Expression of TARSH gene in MEFs senescence and its potential
RT   implication in human lung cancer.";
RL   Biochem. Biophys. Res. Commun. 329:1031-1038(2005).
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DR   EMBL; AB190342; BAD91391.1; -; mRNA.
DR   IPI; IPI00556762; -.
DR   RefSeq; NP_001014423.1; NM_001014423.2.
DR   UniGene; Mm.209236; -.
DR   ProteinModelPortal; Q59IW6; -.
DR   SMR; Q59IW6; 109-212, 939-1036.
DR   STRING; Q59IW6; -.
DR   PRIDE; Q59IW6; -.
DR   Ensembl; ENSMUST00000048471; ENSMUSP00000036257; ENSMUSG00000035258.
DR   GeneID; 320712; -.
DR   KEGG; mmu:320712; -.
DR   UCSC; uc007zmq.1; mouse.
DR   CTD; 320712; -.
DR   MGI; MGI:2444583; Abi3bp.
DR   HOGENOM; HBG283943; -.
DR   HOVERGEN; HBG056157; -.
DR   InParanoid; Q59IW6; -.
DR   OMA; SLKVHIN; -.
DR   NextBio; 397269; -.
DR   Bgee; Q59IW6; -.
DR   Genevestigator; Q59IW6; -.
DR   GO; GO:0005614; C:interstitial matrix; IDA:MGI.
DR   GO; GO:0005518; F:collagen 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:0010811; P:positive regulation of cell-substrate adhesion; 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;
SQ   SEQUENCE   1179 AA;  129538 MW;  B1FD0D9E761408AE CRC64;
     MLSSLGCLLL CGSIALALGN AQKLPKGKKP SLKVHINTTS DSILLKFLRP NANVKLEGFL
     LGYGSNVSPN QYFPLPTEGK FTEAVVDAEP KYLIVVRPAP PPSQKKSCSG KSRPRKPLQL
     VVGTLTPSSV FLSWGFLINP HHDWTLPSHC PSDRFYTIRY REKDKEKKWI FQLCPATETI
     VENLKPNTVY EFGVKDNIEG GIWSKIFNHK TIVGSKNKVN GKIQSTYDQV HSVPVPRKLI
     PLTIIKQVIQ NVTHRASTKS PDKTPFGGTI LVHLIIPGLN ESTVKLPTSI MLEISDALKA
     QLAKNETLAL PAESKTPEVE KLAGQPVTVT PESVSRSTKP TLSSALDTAE TALVLSEKTS
     ETARSVLIPE FELPLSTLAP KRFPEFPEAK TAFPLEKPRG SWASSEEPWV VPGAKTSEDS
     RVVQPQTATY DVISSSTTSD ETEIEIHTAT RDPILDSVPP KTSRTAEQPR ATLAPIEALF
     ESRNVEIFTS PEVRPTTAAP QQTTSIPSTP KRQSTPKPPR VKPAPEPETR PSAQTTKAPR
     KTKKPGHHRL RRPKTTRSPE VPKSKPALEP ATVTPEILVP KIVPKPPQKP KATRRPEVPQ
     VKPAPRQTTS MPPKLKTPHS RMPAKEPVPK EPLHTTSKPK MPPSPEVADT TSVPKDERLS
     LKPDPEVTHS ETAPLETRGI PLIPVISPRP SQEELQTAME ETDQSTQELF TTKIPRTTEL
     AKTTQAPHRL HTAPVRPRIP GRPHGRPALN KTTTRPDKTK PRGTSHKNGV GTGTKQAPKP
     PSPGRNASVD SHATRKPGSV SGTRRPPIPH RHSSTRPVSP ERRPLPPNNV TGKPGRAGIV
     SSSRVTSPPL KATLHPIGTA TARPGAEQKE PTAPASEEEF GTTTDFSSSP TKETDPLGKP
     RFIGPHVRYI PKPENKPCSI TDSVRRFPTE EATEGNATSP PQNPPTNLTV VTVEGCPSFV
     ILDWEKPLND TVTEYEVISR ENGSFSGKNK SIQITNQTFS TVENLKPDTS YEFQVKPKNP
     LGEGPASNTV AFSTESADPR VSEPISAGRD AIWTERPFNS DSYSECKGKQ YVKRTWYKKF
     VGVQLCNSLR YKIYLSDSLT GKFYNIGDQR GHGEDHCQFV DSFLDGRTGQ QLTSEQLPTK
     EGYFRAVRQE PVQFGEIGGH TQINYVQWYE CGTTIPGKW
//
ID   Q5BJ28_MOUSE            Unreviewed;      1068 AA.
AC   Q5BJ28;
DT   12-APR-2005, integrated into UniProtKB/TrEMBL.
DT   12-APR-2005, sequence version 1.
DT   08-MAR-2011, entry version 35.
DE   SubName: Full=Ankhd1 protein;
DE   Flags: Fragment;
GN   Name=Ankhd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; 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 1 KH domain.
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DR   EMBL; BC091647; AAH91647.1; -; mRNA.
DR   IPI; IPI00462476; -.
DR   RefSeq; NP_780584.2; NM_175375.3.
DR   UniGene; Mm.24790; -.
DR   ProteinModelPortal; Q5BJ28; -.
DR   STRING; Q5BJ28; -.
DR   PhosphoSite; Q5BJ28; -.
DR   Ensembl; ENSMUST00000155329; ENSMUSP00000123270; ENSMUSG00000024483.
DR   GeneID; 108857; -.
DR   KEGG; mmu:108857; -.
DR   UCSC; uc008env.1; mouse.
DR   CTD; 108857; -.
DR   HOGENOM; HBG403061; -.
DR   InParanoid; Q5BJ28; -.
DR   OrthoDB; EOG4K9BB8; -.
DR   ArrayExpress; Q5BJ28; -.
DR   Bgee; Q5BJ28; -.
DR   Genevestigator; Q5BJ28; -.
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; 1.
DR   SMART; SM00322; KH; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   1068 AA;  112411 MW;  D735F13C18E408F0 CRC64;
     PKENSEQPEG EDEENDEDVE QEIPIEPPSA TTTTTIGISA TSTTFTNVFG KKRANVVTTP
     STNRKNKKNK TKESPPTAHL ILPEPHISLA QQKADKNKIN GEPRGGGAGG NSDSDNIDST
     DCNSESSSGG KSQEFSFPVD VNPASDKRCS TVVSSQEEKA VTTTSKTQTR LDGEVNSMST
     SYKSLPLSSP TMKLNLTSPK RGQKREEGWK EVVRRSKKLS VPASVVSRIM GRGGCNITAI
     QDVTGAHIDV DKQKDKNGER MITIRGGTES TRYAVQLINA LIQDPAKELE DLIPKNHIRT
     PASTKSIHTN FSSGVGTTAT SSKNAFPLGA PALVTSQATT LSTFQPTNKL SKNVPTNVRS
     PFPVSLPLAY PHPHFALLAA QTMQQIRHPR LPMAQFGGTF SPSPNTWGPF PVRPVNPGNT
     SSSPKHNNTA RLPNQNGPVL PSESPGLATT GCPITVSSVV AASQQLCMTN SRTPSSVRKQ
     LFACVPKTSP PATVISSVTS TSSSLPSVSS TSITSGHVTT TFMPAPTQVP LSSQKVESFS
     VIPPPKEKVS TQDQPLTNLC TPSPAATSCN SSASNTSGAP EAHPSSTPPP PPGNTQEEGQ
     PSKASDLSPV SMPFASNSET APLTLASPRL VAADNRDTGS LPQLTVPAPR VSHRMQPRGS
     FYSVVPNATM HQDPQSIFVT NPVPLTPPQG PPAAVQLSSA VNIMNGSQVH INPANKSLQP
     TFGPATLFNH FSSLFDSGQV PANQGWGDGP LPSRVAADAS FTVQSAFLSN SVLGHLENVH
     PDNSKAPGFR PPSQRVSTSP VGLPSIDPSG NSPSAAAPLT SFSGIPGTRV FLQGPAPVGT
     PSFNRQHFSP HPWTSASNTC DSPIPSVSSG SSSPLSATSA PPTLGQQPKG NSASQDRKIP
     PPIGTERLAR IRQGGSVAQA PVGTSFVAPV GHGGIWSFGV NAMSEGLSGW SQSVIGNHPM
     HQQLSDPSTF SQHQPMERDD SGMVAPTNIF HQPMGLPISM YGGTIIPSHP QLADVPGGPL
     FNGLHNPDPA WNPMIKVIQN SAECTEAQQI WPGTWAPHIG NMHLKYVN
//
ID   MYO16_MOUSE             Reviewed;        1919 AA.
AC   Q5DU14; B2RX94; Q6GQW7; Q8BUV4;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 44.
DE   RecName: Full=Myosin-XVI;
DE   AltName: Full=Unconventional myosin-16;
GN   Name=Myo16; Synonyms=Kiaa0865;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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 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 [LARGE SCALE MRNA] OF 1-992 (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] OF 736-1919.
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 TYR-1441, 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.
CC       May be involved in targeting of the catalytic subunit of protein
CC       phosphatase 1 during brain development (By similarity).
CC   -!- SUBUNIT: Binds PPP1CA and/or PPP1CC. Binds F-actin in an ATP-
CC       sensitive manner (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Found in puncta in soma and
CC       processes of astrocytes and dissociated cerebellar cells with the
CC       morphology of migrating granule cells (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5DU14-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5DU14-2; Sequence=VSP_052446;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 8 ANK repeats.
CC   -!- SIMILARITY: Contains 1 IQ domain.
CC   -!- SIMILARITY: Contains 2 myosin head-like domains.
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DR   EMBL; BC072580; AAH72580.1; -; mRNA.
DR   EMBL; BC151049; AAI51050.1; -; mRNA.
DR   EMBL; BC151051; AAI51052.1; -; mRNA.
DR   EMBL; BC157966; AAI57967.1; -; mRNA.
DR   EMBL; BC172122; AAI72122.1; -; mRNA.
DR   EMBL; AK082350; BAC38475.1; -; mRNA.
DR   EMBL; AK220356; BAD90419.1; -; Transcribed_RNA.
DR   IPI; IPI00381066; -.
DR   IPI; IPI00757256; -.
DR   UniGene; Mm.422761; -.
DR   HSSP; P08799; 1MND.
DR   ProteinModelPortal; Q5DU14; -.
DR   SMR; Q5DU14; 16-309, 388-1170.
DR   PhosphoSite; Q5DU14; -.
DR   PRIDE; Q5DU14; -.
DR   Ensembl; ENSMUST00000042103; ENSMUSP00000049345; ENSMUSG00000039057.
DR   Ensembl; ENSMUST00000110958; ENSMUSP00000106583; ENSMUSG00000039057.
DR   MGI; MGI:2685951; Myo16.
DR   eggNOG; roNOG08502; -.
DR   GeneTree; ENSGT00600000084376; -.
DR   HOGENOM; HBG715017; -.
DR   HOVERGEN; HBG108163; -.
DR   InParanoid; Q5DU14; -.
DR   OrthoDB; EOG4RFKRQ; -.
DR   ArrayExpress; Q5DU14; -.
DR   Bgee; Q5DU14; -.
DR   CleanEx; MM_MYO16; -.
DR   Genevestigator; Q5DU14; -.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0005654; C:nucleoplasm; ISS:HGNC.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC.
DR   GO; GO:0005886; C:plasma membrane; ISS:HGNC.
DR   GO; GO:0051015; F:actin filament binding; ISS:HGNC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW.
DR   GO; GO:0021549; P:cerebellum development; ISS:HGNC.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; ISS:HGNC.
DR   GO; GO:0045749; P:negative regulation of S phase of mitotic cell cycle; ISS:HGNC.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 3.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00248; ANK; 5.
DR   SMART; SM00015; IQ; 1.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
DR   PROSITE; PS50096; IQ; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; ANK repeat; ATP-binding;
KW   Cytoplasm; Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW   Repeat.
FT   CHAIN         1   1919       Myosin-XVI.
FT                                /FTId=PRO_0000289137.
FT   REPEAT       59     88       ANK 1.
FT   REPEAT       92    121       ANK 2.
FT   REPEAT      125    154       ANK 3.
FT   REPEAT      158    189       ANK 4.
FT   REPEAT      191    217       ANK 5.
FT   REPEAT      221    250       ANK 6.
FT   REPEAT      254    283       ANK 7.
FT   REPEAT      287    316       ANK 8.
FT   DOMAIN      402    801       Myosin head-like 1.
FT   DOMAIN      843   1131       Myosin head-like 2.
FT   MOD_RES    1441   1441       Phosphotyrosine.
FT   VAR_SEQ     620    629       YVSQGMREDV -> NMSSRCGQTP (in isoform 2).
FT                                /FTId=VSP_052446.
FT   CONFLICT    736    737       RD -> VN (in Ref. 3; BAD90419).
FT   CONFLICT    920    920       Missing (in Ref. 3; BAD90419).
SQ   SEQUENCE   1919 AA;  211383 MW;  9F3899BB2035BD48 CRC64;
     MEIDQCLLES LPLGQRQRLV KRMRCEQIKA YYEREKVFQK QEGPLKRSKP GKRQKVRFGL
     ADMIQDAVIH HHDKEVLQLL KEGADPHTLV SSGGSLLHLC ARYDNVFIAE VLIDRGVNVN
     HQDEDFWTPM HIACACDNPD IVLLLILAGA NVFLQDVNGN IPLDYAVEGT ESSAILLAYL
     DEKGVDLSSL RQIKLQRPLS MLTDVRHFLS SGGDVNEKND DGVTLLHMAC ASGYKEVVLL
     LLEHGGDLNG TDDRYWTPLH LAAKYGQTTL VKLLLAHQAN PHLVNCNGEK PSDIAASESI
     EEMLLKAEIA WEEKMKESPS APSLAQEELY EILHDLPDLS SKLSPLVLPI AKQDSLLEKD
     IMFKDTTKGL CKQESQDGPP ETSMTSNCGK PEQVQVMPPA PSDDLATLSE LNDSSLLYEI
     QKRFGNDQIH TFIGDIFLLV NPFKELPIYS TMVSQMYLSP TGQRSPSLPP HLFSCAERAF
     HRLFQERKPQ NIILSGERGS GKTQASKQIM KYLTSRASSS CTMFDSRLRH AIYIVEAFGH
     AKTTLNNVSS CLIQYWELQC CQRRKHITGA RISTYMLEKS RVVAQPPGQG TFLIFSWLMD
     GLSSEEKCGL HLNNFCAHRY VSQGMREDVS TAEHSLNKER LAALKHALNV IGFSTLEVEN
     LFVILSAILH IGDIQFTALT EADSAFVSDL QLLEQVAGML QVSTDELASA LTTDIQYFKG
     DVIIRRHTIQ MAAFYRDLLA KSLYSRLFGF LINTVNCCLQ NQDEYKSLQT LDIGILDIFG
     FEEFQKNEFE QLCVNLTNEK MHHYIQEVLF LQEQTECVQE GVAMETACSP GNQAGVLDFF
     FQKPSGFFSL LDEESQVIWS GEPNLPRKLQ GLLESSNTNA VYSPVKDGNG NVAFKGQGAA
     FTVMHYAGRV MYEMGGAVER NKDSLSQNLL FVMKTSENVV ISHLFQSKLS QTGSLISSYP
     SFKFGGHKST LLSKRTASSM VGVNKNYLEL SKLLKKKGTS TFLQRLERGE PATAASQLTK
     SLADITAKLQ RGSPHFILCI KPNTSQLPGV FDHFYVSAQL QYLGVLGLVR LFRSGYPVRP
     SFEDFLSRYE PLASVLLGET KGQAAEERCR LVLQRCKLQG WQIGVHKVFL KYWHVDQLSD
     LWLQLQRKIV TCQKVIRGFL ARQHLLQRMS IKQQEVTSIK SFLQSTEDMA LKTYDALVIQ
     NASDIAREHD RLRKEVHTAY HRNRQEEGTK RAEDQGGCRH VHSNSVPVPM VVDSLAQALT
     GPSTRPPSLH SVFSMDDSTG LPSPRKQPPP KPKRDPNTRL SASYEAVSAC LSAAKDAAGE
     ALTRPRPHSD DYSTMKKIPP RKPKRSPHTK LSGSYEEIWG PPRPSGTMGQ GGRHQAPGTL
     SVQWARPDSV PQCTPQLPLH LPLPQGDYDD DAEPVYIEMV GNAARAGGSE TDSPDQGESV
     YEEMKYILPE EGCGLGMLTF LPASPPLFLE TRKAIILEAA EGNCQPSKDT CDIPPPFPNL
     LPHRPPLLVF PPTPVTRSPA SDESPLTPLE VKKLPVLETN LKYPVQSEGS SPLSPQYSKA
     QKGDNDQLAS PGFPVFNGPS RISPPATPPP PPGPPPAPCG PPPAPCGPPP APCGPPPAPC
     GPPPAPCGPP PAPCGAASAS CGVAPAPCRP PTHFAFPPES VLVTAAKALT NSDLPRTQPK
     PSSAPVPGPC SSFVKAPYSP GKTARADLRK TSSTFSPPSP YSPPNSRPLS SPLDELASLF
     NSGRSVLRRS AVGRRIREAE GFETNMNLSS RDEPSSSEMA SETQDRNANN HGTQLSSSLS
     SDVTAENGNP VTNGLAEDDG CSRLCLSGMG TSSFQRNRES HTTQVIHQLR LSENESVALQ
     ELLDWRRKLC EAREGWQEAL QHPEPRAPPP PPCKKPTLLK KPEGGSCTRL PSQLWDSSM
//
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   Q5DU62_MOUSE            Unreviewed;       992 AA.
AC   Q5DU62;
DT   29-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   29-MAR-2005, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   SubName: Full=MFLJ00139 protein;
DE   Flags: Fragment;
GN   Name=Micall2; Synonyms=mFLJ00139;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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 1 LIM zinc-binding domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK220308; BAD90386.1; -; mRNA.
DR   IPI; IPI00280103; -.
DR   UniGene; Mm.240510; -.
DR   ProteinModelPortal; Q5DU62; -.
DR   STRING; Q5DU62; -.
DR   Ensembl; ENSMUST00000044642; ENSMUSP00000039707; ENSMUSG00000036718.
DR   MGI; MGI:2444818; Micall2.
DR   HOVERGEN; HBG052476; -.
DR   InParanoid; Q5DU62; -.
DR   ArrayExpress; Q5DU62; -.
DR   Bgee; Q5DU62; -.
DR   Genevestigator; Q5DU62; -.
DR   GO; GO:0005923; C:tight junction; IDA:MGI.
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.
FT   NON_TER       1      1
SQ   SEQUENCE   992 AA;  106245 MW;  657121D30F215487 CRC64;
     YRDVSITNMT TSFRDGLAFC AILHRHRPDL INFSALRKEN IYENNKLAFQ VAEEQLGIPA
     LLDAEDMVAL KVPDRLSILT YVSQYYNYFH GRSPIGGMAG IKRPSSDSTE ELSGKKGLSQ
     PAKLPSPAQT QRSPLSPART NPVVQRNEGG SQRPSPKAAP GTAGSSVSSI CGVCGKHVHL
     VQRHLADGRL YHRSCFRCKQ CSSTLHSGAY RATGEPGVFV CTHHSSEVTS VSPKSSNLAS
     RKPGGVTADT RSVGVSWTVQ EANGEGTPLR VRTAAWEHAG GNTTAKGFVQ TELKPPSTSQ
     VHVGSSAGPK LPTSTVTTTS VTSKALTHVT NSSPTGWSSP AQSSPANFNS RPVVSPSARN
     THLPGSQGQT ASKGVKTQLN LNSESSNTAV TPAWTSSASK TQQAREKFFQ TPPSAPAPAS
     APAPAPTSKV PTVVTVPTSK VPNVVTAPTS KVPTVVTVPT SKVPTVVSAP TSKVPTVVSA
     PTSKVPTVVN STNSRVTTVV NAPTSKVPTV VSATNGRVPT VVTAHTGRVP AVMNTSASKV
     SPVVDAPAQE SSREQALSVL RKALPALTGS GTQAPNRSFP ATSSVLVTLP KNEVPQKVPS
     DKLSALTTQT PNFTIKLEPS APVNVGNTAV FLQAGKKSPS ISPRVGKTSV GSRPQAEVAG
     VKGPGPISQE GQEEGPEGWR ARLKPVDKKT PAGRSLEQKE PVLAEPRIGD TSRKASSSSD
     SSVHITLTSI QHKRKPCPAG SGPSPAALSP SPSHRKKLAV PPSLDVSADW LQPEPKKQED
     GTRSCKEEKS PTRWSRERSA VLDSGLAPPG EAVTSPVRLH PDYIPQEELQ RQLQDIESQL
     DALELRGVEL EKRLRAAEGD ASEDSLMVDW FRLIHEKQLL LRLESELMYK SKDQRLEEQQ
     LDLQGELRRL MDKPEGLKSP QDRQREQELL SQYVNTVNDR SDIVDFLDED RLREQEEDQM
     LENMIQNLGL QRKKSKSFLS KIWSSKSKSG QA
//
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   CF142_MOUSE             Reviewed;         269 AA.
AC   Q5FW52; Q9D6X9;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Uncharacterized protein C6orf142 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=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   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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5FW52-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5FW52-2; Sequence=VSP_015323;
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; AK009836; BAB26534.1; -; mRNA.
DR   EMBL; BC089626; AAH89626.1; -; mRNA.
DR   IPI; IPI00553471; -.
DR   IPI; IPI00850970; -.
DR   RefSeq; NP_081426.1; NM_027150.1.
DR   UniGene; Mm.35008; -.
DR   ProteinModelPortal; Q5FW52; -.
DR   PhosphoSite; Q5FW52; -.
DR   PRIDE; Q5FW52; -.
DR   Ensembl; ENSMUST00000034910; ENSMUSP00000034910; ENSMUSG00000032355.
DR   Ensembl; ENSMUST00000093816; ENSMUSP00000091334; ENSMUSG00000032355.
DR   GeneID; 69642; -.
DR   KEGG; mmu:69642; -.
DR   UCSC; uc009qtg.1; mouse.
DR   UCSC; uc009qth.1; mouse.
DR   MGI; MGI:1916892; 2310046A06Rik.
DR   GeneTree; ENSGT00390000015862; -.
DR   HOGENOM; HBG283543; -.
DR   HOVERGEN; HBG055766; -.
DR   InParanoid; Q5FW52; -.
DR   OMA; PGNIATR; -.
DR   OrthoDB; EOG4T4CVD; -.
DR   NextBio; 329974; -.
DR   ArrayExpress; Q5FW52; -.
DR   Bgee; Q5FW52; -.
DR   CleanEx; MM_2310046A06RIK; -.
DR   Genevestigator; Q5FW52; -.
PE   2: Evidence at transcript level;
KW   Alternative splicing.
FT   CHAIN         1    269       Uncharacterized protein C6orf142 homolog.
FT                                /FTId=PRO_0000089539.
FT   COMPBIAS    215    219       Poly-Ser.
FT   VAR_SEQ     155    196       Missing (in isoform 2).
FT                                /FTId=VSP_015323.
FT   CONFLICT     88     88       E -> G (in Ref. 1; BAB26534).
FT   CONFLICT    119    119       S -> N (in Ref. 1; BAB26534).
SQ   SEQUENCE   269 AA;  29466 MW;  1F7FA9949A217E4B CRC64;
     MEFGKHEPGS SLKRNKNLEE GVTFEYSDHM TFSSESKQER VQRILDYPSE VSGRNSQQKE
     FNTKEPQGMQ KGDLFKAEYV FIVDSDGEDE ATCRQGEQGP PGGPGNIATR PKSLAISSSL
     ASDVVRPKVR GADLKTSSHP EIPHGIAPQQ KHGLALDEPA RTESNSKASV LDLPVEHSSD
     SPSRPPQTML GSETIKTPTT HPRAAGRETK YANLSSSSST ASESQLTKPG VIRPVPVKSK
     LLLRKDEEVY EPNPFSKYLE DNSGLFSEQ
//
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.
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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   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).
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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   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;
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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   RBM27_MOUSE             Reviewed;        1060 AA.
AC   Q5SFM8; Q6ZPT9; Q7TQK8; Q8C2X5; Q8C9A5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=RNA-binding protein 27;
DE   AltName: Full=Peri-implantation stem cell protein 1;
DE   AltName: Full=RNA-binding motif protein 27;
GN   Name=Rbm27; Synonyms=Kiaa1311;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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 SUBCELLULAR LOCATION.
RC   STRAIN=C57BL/6;
RX   PubMed=15741184; DOI=10.1093/nar/gki269;
RA   Kavanagh S.J., Schulz T.C., Davey P., Claudianos C., Russell C.,
RA   Rathjen P.D.;
RT   "A family of RS domain proteins with novel subcellular localization
RT   and trafficking.";
RL   Nucleic Acids Res. 33:1309-1322(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 326-1060 (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 197-849 (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] OF 132-1060 (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).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus speckle.
CC       Note=Incorporated into the nuclear speckles and to speckles
CC       proximal to the nuclear periphery. Also localizes to punctate
CC       structures in the cytoplasm termed cytospeckles.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5SFM8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SFM8-2; Sequence=VSP_022462;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q5SFM8-3; Sequence=VSP_022463;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The RRM domain mediates integration into cytospeckles.
CC   -!- SIMILARITY: Contains 1 C3H1-type zinc finger.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH54080.1; Type=Frameshift; Positions=131, 143;
CC       Sequence=BAC31304.2; Type=Frameshift; Positions=310;
CC       Sequence=BAC39993.1; Type=Erroneous initiation;
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DR   EMBL; AY461716; AAS19274.1; -; mRNA.
DR   EMBL; AK129330; BAC98140.1; -; mRNA.
DR   EMBL; AK042613; BAC31304.2; ALT_FRAME; mRNA.
DR   EMBL; AK087759; BAC39993.1; ALT_INIT; mRNA.
DR   EMBL; BC054080; AAH54080.1; ALT_FRAME; mRNA.
DR   IPI; IPI00454079; -.
DR   IPI; IPI00515687; -.
DR   IPI; IPI00828892; -.
DR   RefSeq; NP_766214.2; NM_172626.2.
DR   UniGene; Mm.329400; -.
DR   ProteinModelPortal; Q5SFM8; -.
DR   STRING; Q5SFM8; -.
DR   PhosphoSite; Q5SFM8; -.
DR   PRIDE; Q5SFM8; -.
DR   Ensembl; ENSMUST00000046972; ENSMUSP00000041688; ENSMUSG00000024491.
DR   Ensembl; ENSMUST00000091920; ENSMUSP00000089540; ENSMUSG00000024491.
DR   Ensembl; ENSMUST00000115550; ENSMUSP00000111212; ENSMUSG00000024491.
DR   GeneID; 225432; -.
DR   KEGG; mmu:225432; -.
DR   UCSC; uc008etr.1; mouse.
DR   UCSC; uc008ets.1; mouse.
DR   CTD; 225432; -.
DR   MGI; MGI:2147194; Rbm27.
DR   eggNOG; roNOG12924; -.
DR   GeneTree; ENSGT00510000046929; -.
DR   HOGENOM; HBG447183; -.
DR   HOVERGEN; HBG057372; -.
DR   InParanoid; Q5SFM8; -.
DR   OrthoDB; EOG4FJ88J; -.
DR   ArrayExpress; Q5SFM8; -.
DR   Bgee; Q5SFM8; -.
DR   CleanEx; MM_RBM27; -.
DR   Genevestigator; Q5SFM8; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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; 1.
DR   Gene3D; G3DSA:1.20.1390.10; PWI; 1.
DR   Pfam; PF01480; PWI; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Isopeptide bond;
KW   Metal-binding; Nucleus; Phosphoprotein; RNA-binding; Ubl conjugation;
KW   Zinc; Zinc-finger.
FT   CHAIN         1   1060       RNA-binding protein 27.
FT                                /FTId=PRO_0000273045.
FT   DOMAIN      600    674       RRM.
FT   ZN_FING     273    301       C3H1-type.
FT   COILED      810    887       Potential.
FT   COMPBIAS    131    201       Arg-rich.
FT   COMPBIAS    311    417       Pro-rich.
FT   MOD_RES     447    447       Phosphothreonine (By similarity).
FT   MOD_RES     566    566       Phosphoserine (By similarity).
FT   CROSSLNK    653    653       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   VAR_SEQ     427    482       RQPMYSREHGAAASERLQLGTPPPLLAARLVPPRNLMGSSI
FT                                GYHTSVSSPTPLVPD -> N (in isoform 2).
FT                                /FTId=VSP_022462.
FT   VAR_SEQ     632    730       Missing (in isoform 3).
FT                                /FTId=VSP_022463.
FT   CONFLICT    214    214       P -> S (in Ref. 3; BAC31304 and 4;
FT                                AAH54080).
FT   CONFLICT    304    304       V -> L (in Ref. 3; BAC31304).
FT   CONFLICT    909    909       D -> Y (in Ref. 2; BAC98140).
SQ   SEQUENCE   1060 AA;  118562 MW;  012E0E38CA350DD9 CRC64;
     MLIEDVDALK SWLAKLLEPI CDADPSALAN YVVALVKKDK PEKELKAFCA DQLDVFLQKE
     TSGFVDKLFE SLYTKNYLPP LEPVKPEPKP LVQEKEEIKE EVFQEPAEEE RDTRKKKYPS
     PQKSRSESSE RRTREKKRED GKWRDYERYY ERNELYREKY DWRRGRSKSR SKSRGLSRSR
     SRSRGRSKDR DPNRNVEHRE RSKFKSERND LESPYVPVSA PPPSSSEQYS SGAQSIPSTV
     TVIAPAHHSE NTTESWSNYY NNHSSSNSFG RNPPPKRRCR DYDERGFCVL GDLCQFDHGN
     DPLVVDEVAL PSMIPFPPPP PGLPPPPPPG MLMPPMPGPG PGPGPGPGPG PGPGPGPGHS
     MRLPVPQGHG QPPPSVVLPI PRPPISQSSL INSRDQPGTS AVPNLAPVGA RLPPPLPQNL
     LYTVSERQPM YSREHGAAAS ERLQLGTPPP LLAARLVPPR NLMGSSIGYH TSVSSPTPLV
     PDTYEPDGYN PEAPSITSSG RSQYRQFFSR AQTQRPNLIG LTSGDMDANP RAANIVIQTE
     PPVPVSVNSN VTRVVLEPES RKRAISGLEG PLTKKPWLGK QGNNNQSKPG FLRKNHYTNT
     KLEVKKIPQE LNNITKLNEH FSKFGTIVNI QVAFKGDPEA ALIQYLTNEE ARKAISSTEA
     VLNNRFIRVL WHRENNEQPA LQSSAQILLQ QQHTLSHLSQ QHHSLPQHLH PQQVMVTQSS
     PSSVHGGIQK MMGKPQTSGA YVLNKVPVKH RLGHASTNQS DTSHLLNQTG GSSGEDCPVF
     STPGHPKTIY SSSNLKAPSK LCSGSKSHDV QEVLKKKQEA MKLQQDMRKK KQEMLEKQIE
     CQKMLISKLE KNKNMKPEER ANIMKTLKEL GEKISQLKDE LKTSSTVSTP SKVKTKTEAQ
     KELLDTELDL HKRLSSGEDT TELRKKLSQL QVEAARLGIL PVGRGKTISS QGRGRGRGRG
     RGRGSLNHMV VDHRPKALPG GGFIEEEKDE LLQHFSATNQ ASKFKDRRLQ ISWHKPKVPS
     ISTETEEEEV KEEETETSDL FLHDDDDEDE DEYESRSWRR
//
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   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   -----------------------------------------------------------------------
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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   ANR40_MOUSE             Reviewed;         363 AA.
AC   Q5SUE8; Q5SUF0; Q8R595; Q9CU71;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Ankyrin repeat domain-containing protein 40;
GN   Name=Ankrd40;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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=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 7-363 (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   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=3;
CC       Name=1;
CC         IsoId=Q5SUE8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SUE8-2; Sequence=VSP_019555, VSP_019556;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q5SUE8-3; Sequence=VSP_019554, VSP_019557;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 2 ANK repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; AL645965; CAI25946.1; -; Genomic_DNA.
DR   EMBL; AL645965; CAI25947.1; -; Genomic_DNA.
DR   EMBL; AL645965; CAI25948.1; -; Genomic_DNA.
DR   EMBL; BC023133; AAH23133.1; -; mRNA.
DR   EMBL; AK017451; BAB30748.1; -; mRNA.
DR   IPI; IPI00272417; -.
DR   IPI; IPI00623774; -.
DR   IPI; IPI00648088; -.
DR   RefSeq; NP_082075.2; NM_027799.2.
DR   RefSeq; NP_666136.1; NM_146024.1.
DR   UniGene; Mm.141054; -.
DR   ProteinModelPortal; Q5SUE8; -.
DR   SMR; Q5SUE8; 6-93.
DR   PhosphoSite; Q5SUE8; -.
DR   PRIDE; Q5SUE8; -.
DR   Ensembl; ENSMUST00000021227; ENSMUSP00000021227; ENSMUSG00000020864.
DR   Ensembl; ENSMUST00000051221; ENSMUSP00000061637; ENSMUSG00000020864.
DR   Ensembl; ENSMUST00000107818; ENSMUSP00000103448; ENSMUSG00000020864.
DR   GeneID; 71452; -.
DR   KEGG; mmu:71452; -.
DR   UCSC; uc007kyl.1; mouse.
DR   CTD; 71452; -.
DR   MGI; MGI:1918702; Ankrd40.
DR   eggNOG; roNOG15576; -.
DR   GeneTree; ENSGT00390000007792; -.
DR   HOGENOM; HBG715451; -.
DR   HOVERGEN; HBG058022; -.
DR   InParanoid; Q5SUE8; -.
DR   OMA; QNEVNGW; -.
DR   OrthoDB; EOG4PRSR8; -.
DR   PhylomeDB; Q5SUE8; -.
DR   NextBio; 333805; -.
DR   ArrayExpress; Q5SUE8; -.
DR   Bgee; Q5SUE8; -.
DR   CleanEx; MM_ANKRD40; -.
DR   Genevestigator; Q5SUE8; -.
DR   GermOnline; ENSMUSG00000020864; 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; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ANK repeat; Phosphoprotein; Repeat.
FT   CHAIN         1    363       Ankyrin repeat domain-containing protein
FT                                40.
FT                                /FTId=PRO_0000244369.
FT   REPEAT        9     38       ANK 1.
FT   REPEAT       43     72       ANK 2.
FT   COMPBIAS    100    103       Poly-Glu.
FT   COMPBIAS    144    242       Pro-rich.
FT   MOD_RES     176    176       Phosphoserine.
FT   VAR_SEQ     316    324       DKDVARLQD -> IKDEPRPWN (in isoform 3).
FT                                /FTId=VSP_019554.
FT   VAR_SEQ     316    322       DKDVARL -> KRCIHTD (in isoform 2).
FT                                /FTId=VSP_019555.
FT   VAR_SEQ     323    363       Missing (in isoform 2).
FT                                /FTId=VSP_019556.
FT   VAR_SEQ     325    363       Missing (in isoform 3).
FT                                /FTId=VSP_019557.
FT   CONFLICT      7      7       Q -> E (in Ref. 3; BAB30748).
FT   CONFLICT     11     11       Q -> E (in Ref. 3; BAB30748).
FT   CONFLICT     40     40       N -> K (in Ref. 3; BAB30748).
SQ   SEQUENCE   363 AA;  40560 MW;  7F45DD06268FE157 CRC64;
     MSALLEQKEQ QERLREAAAL GDIREVQKLV ESGVDVNSQN EVNGWTCLHW ACKRNHGQVV
     SYLLQSGADR EILTTKGEMP VQLTSRREIR KIMGVEEADE EEEIPQLKKE SELPFVPNYL
     ANPAFPFIYT PAAEDSTQLQ NGGPSPPPVS PPADSSPPLL PPTETPLLGA FPRDHSSLAL
     VQNGDISAPS AILRTPESTK PGPVCQPPVS QNRSLFSVPS KPPVSLEPQN GTYAGPAPAF
     QPFFFTGAFP FNMQELVLKV RIQNPSLREN DFIEIELDRQ ELTYQELLRV SCCELGVNPD
     QVEKIRKLPN TLLRKDKDVA RLQDFQELEL VLMISDNNFL FRNAASTLTE RPCYNRRASK
     LTY
//
ID   GGNB2_MOUSE             Reviewed;         696 AA.
AC   Q5SV77; A4QPD5; B7ZP33; Q5SV75; Q5SV76; Q5SV78; Q6GVH6; Q6P9J4;
AC   Q920N4;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=Gametogenetin-binding protein 2;
DE   AltName: Full=Dioxin-inducible factor 3;
DE            Short=DIF-3;
DE   AltName: Full=Protein ZNF403;
GN   Name=Ggnbp2; Synonyms=Zfp403, Znf403;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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   INDUCTION.
RX   MEDLINE=21585518; PubMed=11728448; DOI=10.1016/S0014-5793(01)03039-3;
RA   Ohbayashi T., Oikawa K., Iwata R., Kameta A., Evine K., Isobe T.,
RA   Matsuda Y., Mimura J., Fujii-Kuriyama Y., Kuroda M., Mukai K.;
RT   "Dioxin induces a novel nuclear factor, DIF-3, that is implicated in
RT   spermatogenesis.";
RL   FEBS Lett. 508:341-344(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH GGN.
RX   PubMed=15642376; DOI=10.1016/j.febslet.2004.10.112;
RA   Zhang J., Wang Y., Zhou Y., Cao Z., Huang P., Lu B.;
RT   "Yeast two-hybrid screens imply that GGNBP1, GGNBP2 and OAZ3 are
RT   potential interaction partners of testicular germ cell-specific
RT   protein GGN1.";
RL   FEBS Lett. 579:559-566(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 4).
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, 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 be involved in spermatogenesis.
CC   -!- SUBUNIT: Interacts with isoform 1 of GGN.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle. Note=Associated with
CC       vesicular structures.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q5SV77-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SV77-2; Sequence=VSP_019180;
CC       Name=3;
CC         IsoId=Q5SV77-3; Sequence=VSP_019179, VSP_019180;
CC         Note=Ref.1 (BAB71783) sequence is in conflict in position:
CC         219:G->GG;
CC       Name=4;
CC         IsoId=Q5SV77-4; Sequence=VSP_019179;
CC   -!- TISSUE SPECIFICITY: Testis-specific.
CC   -!- DEVELOPMENTAL STAGE: Abundantly expressed during spermatogenesis.
CC       Not detected in newborn animals, in which spermatogenesis has not
CC       yet progressed beyond the earliest stages.
CC   -!- INDUCTION: By dioxin (2,3,7,8-Tetrachlorodibenzo-p-dioxin).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH60738.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=CAI24983.1; Type=Erroneous gene model prediction;
CC       Sequence=CAI25484.1; Type=Erroneous gene model prediction;
CC       Sequence=CAI25487.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB064543; BAB71783.1; -; mRNA.
DR   EMBL; AY633741; AAT47120.1; -; mRNA.
DR   EMBL; AL596083; CAI24981.1; -; Genomic_DNA.
DR   EMBL; AL645623; CAI24981.1; JOINED; Genomic_DNA.
DR   EMBL; AL596083; CAI24982.1; -; Genomic_DNA.
DR   EMBL; AL645623; CAI24982.1; JOINED; Genomic_DNA.
DR   EMBL; AL596083; CAI24983.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL645623; CAI24983.1; JOINED; Genomic_DNA.
DR   EMBL; AL645623; CAI25484.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL645623; CAI25485.1; -; Genomic_DNA.
DR   EMBL; AL596083; CAI25485.1; JOINED; Genomic_DNA.
DR   EMBL; AL645623; CAI25486.1; -; Genomic_DNA.
DR   EMBL; AL596083; CAI25486.1; JOINED; Genomic_DNA.
DR   EMBL; AL645623; CAI25487.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL596083; CAI25487.1; JOINED; Genomic_DNA.
DR   EMBL; BC060738; AAH60738.1; ALT_SEQ; mRNA.
DR   EMBL; BC139772; AAI39773.1; -; mRNA.
DR   EMBL; BC145605; AAI45606.1; -; mRNA.
DR   EMBL; BC150801; AAI50802.1; -; mRNA.
DR   IPI; IPI00120796; -.
DR   IPI; IPI00753575; -.
DR   IPI; IPI00759965; -.
DR   IPI; IPI00970364; -.
DR   RefSeq; NP_694784.2; NM_153144.2.
DR   UniGene; Mm.356653; -.
DR   MINT; MINT-1215939; -.
DR   STRING; Q5SV77; -.
DR   PhosphoSite; Q5SV77; -.
DR   PRIDE; Q5SV77; -.
DR   Ensembl; ENSMUST00000100685; ENSMUSP00000098251; ENSMUSG00000020530.
DR   Ensembl; ENSMUST00000100686; ENSMUSP00000098252; ENSMUSG00000020530.
DR   Ensembl; ENSMUST00000108081; ENSMUSP00000103716; ENSMUSG00000020530.
DR   GeneID; 217039; -.
DR   KEGG; mmu:217039; -.
DR   UCSC; uc007kqu.1; mouse.
DR   UCSC; uc007kqv.1; mouse.
DR   CTD; 217039; -.
DR   MGI; MGI:2387356; Ggnbp2.
DR   GeneTree; ENSGT00390000009552; -.
DR   HOVERGEN; HBG082524; -.
DR   OrthoDB; EOG447FSP; -.
DR   NextBio; 375530; -.
DR   ArrayExpress; Q5SV77; -.
DR   Bgee; Q5SV77; -.
DR   CleanEx; MM_GGNBP2; -.
DR   Genevestigator; Q5SV77; -.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
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   Alternative splicing; Cytoplasmic vesicle; Developmental protein;
KW   Differentiation; Phosphoprotein; Spermatogenesis.
FT   CHAIN         1    696       Gametogenetin-binding protein 2.
FT                                /FTId=PRO_0000239349.
FT   MOD_RES     360    360       Phosphoserine.
FT   VAR_SEQ     176    176       G -> GEGSSSSVSSEKLSTDKRSSEDHRKDSKCRIIFHYG
FT                                PFQGTAR (in isoform 3 and isoform 4).
FT                                /FTId=VSP_019179.
FT   VAR_SEQ     282    282       G -> GYE (in isoform 2 and isoform 3).
FT                                /FTId=VSP_019180.
FT   CONFLICT    510    510       D -> N (in Ref. 4; AAI45606/AAI50802).
SQ   SEQUENCE   696 AA;  78970 MW;  C4F3976169B8646C CRC64;
     MARLVAVCRD GEEEFPFERR QIPLYIDDTL TMVMEFPDNV LNLDGHQNNG AQLKQFIQRH
     SMLKQQDLSI AMVVTSREVL SALSQLVPCV GCRRSVERLF SQLVESGNPA LEPLTVGPKG
     VLSLTRSCMT DAKKLYTLFY VHGSKLNDMI DAIPKSKKNK RCQLHSLDTH KPKPLGGCWM
     DVWELMSQEC RDEVVLIDSS CLLETLETYL RKHRFCTDCK NKVLRAYNIL IGELDCSKEK
     GYCAALYEGL RCCPHERHIH VCCETDFIAH LLGRAEPEFA GGRRERHAKT IDIAQEEVLT
     CLGIHLYERL HRIWQKLRAE EQTWQMLFYL GVDALRKSFE MTVEKVQGIS RLEQLCEEFS
     EEERVRELKQ EKKRQKRKNR RKNKCVCDTP ASLHTADEKA VSREKETDFI ENSCNACGSA
     EDGETCVEVM VTSENTSCTC PSSGNLLGSP KIKKGMSPHC NGSDCGYSSS MEGSETGSRE
     GSDVACTEGI CNHDEHGEDS CVHHCEDKED DGDSCVECWA NSEENNIKGK NKKKKKKSKM
     LKCDEHIQKL GSCITDPGNR ETSGNTMHTV FHRDKTKDAH PESCCSTEKG GQPLPWFEHR
     KSVPQFTEPT EMSFGPDSGK GAKSLVELLD ESECTSDEEI FISQDEIQSF MANNQSFYSN
     REQYRQHLKE KFNKYCRLND HKRPVCSGWL TTAGAN
//
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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;
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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   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   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.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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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   Q5SXC4_MOUSE            Unreviewed;       518 AA.
AC   Q5SXC4;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 53.
DE   SubName: Full=Vascular endothelial zinc finger 1;
GN   Name=Vezf1; ORFNames=RP23-199A2.1-001;
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   Sycamore N.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL593853; CAI24418.1; -; Genomic_DNA.
DR   IPI; IPI00129531; -.
DR   RefSeq; NP_057895.2; NM_016686.3.
DR   UniGene; Mm.46628; -.
DR   ProteinModelPortal; Q5SXC4; -.
DR   SMR; Q5SXC4; 56-99, 172-288.
DR   STRING; Q5SXC4; -.
DR   PRIDE; Q5SXC4; -.
DR   Ensembl; ENSMUST00000018521; ENSMUSP00000018521; ENSMUSG00000018377.
DR   GeneID; 22344; -.
DR   KEGG; mmu:22344; -.
DR   NMPDR; fig|10090.3.peg.25012; -.
DR   UCSC; uc007kvf.1; mouse.
DR   CTD; 22344; -.
DR   MGI; MGI:1313291; Vezf1.
DR   HOGENOM; HBG717200; -.
DR   HOVERGEN; HBG058083; -.
DR   InParanoid; Q5SXC4; -.
DR   OMA; RPKKTPT; -.
DR   NextBio; 302617; -.
DR   ArrayExpress; Q5SXC4; -.
DR   Bgee; Q5SXC4; -.
DR   Genevestigator; Q5SXC4; -.
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:0001525; P:angiogenesis; IMP:MGI.
DR   GO; GO:0001885; P:endothelial cell 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; 5.
DR   SMART; SM00355; ZnF_C2H2; 6.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   518 AA;  56557 MW;  26E09F405088D937 CRC64;
     MEANWTAFLF QAHEASHHQQ QAAQNSLLPL LSSAVEPPDQ KPLLPIPITQ KPQAAPETLK
     DAIGIKKEKP KTSFVCTYCS KAFRDSYHLR RHQSCHTGIK LVSRAKKTPT TVVPLISTIA
     GDSSRTSLVS TIAGILSTVT TSSSGTNPSS SASTTSMPVP QSVKKPSKPV KKNHACEMCG
     KAFRDVYHLN RHKLSHSDEK PFECPICNQR FKRKDRMTYH VRSHEGGITK PYTCSVCGKG
     FSRPDHLSCH VKHVHSTERP FKCQTCTAAF ATKDRLRTHM VRHEGKVSCN ICGKLLSAAY
     ITSHLKTHGQ SQSINCNTCK QGISKTCMSE ETSNQKQQQQ QQQQQQQQQQ QHVTSWPGKQ
     VETLRLWEEA VKARKKEAAN LCQTSTAATT PVTLTTPFNI TSSVSSGTMS NPVTVAAAMS
     MRSPVNVSSA VNITSPMNIG HPVTITSPLA MTSPLTLTTP VNLPTPVTAP VNIAHPVTIT
     SPMNLPTPMT LAAPLNIAMR PVESMPFLPQ ALPTSPPW
//
ID   Q5SXF9_MOUSE            Unreviewed;      1197 AA.
AC   Q5SXF9;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   11-JAN-2011, entry version 44.
DE   SubName: Full=Misshapen-like kinase 1 (Zebrafish);
DE   Flags: Fragment;
GN   Name=Mink1; ORFNames=DN-183N8.7-004, RP23-122P1.6-004;
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   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.
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DR   EMBL; AL592547; CAI24007.1; -; Genomic_DNA.
DR   EMBL; CR933736; CAM28126.1; -; Genomic_DNA.
DR   IPI; IPI00230171; -.
DR   UniGene; Mm.42967; -.
DR   ProteinModelPortal; Q5SXF9; -.
DR   STRING; Q5SXF9; -.
DR   Ensembl; ENSMUST00000072237; ENSMUSP00000072091; ENSMUSG00000020827.
DR   Ensembl; ENSMUST00000136663; ENSMUSP00000117959; ENSMUSG00000020827.
DR   MGI; MGI:1355329; Mink1.
DR   HOGENOM; HBG715124; -.
DR   HOVERGEN; HBG036506; -.
DR   InParanoid; Q5SXF9; -.
DR   ArrayExpress; Q5SXF9; -.
DR   Bgee; Q5SXF9; -.
DR   Genevestigator; Q5SXF9; -.
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; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00036; CNH; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   Kinase; Transferase.
FT   NON_TER       1      1
SQ   SEQUENCE   1197 AA;  134941 MW;  543AB8CB16195F9B CRC64;
     KVIHRDIKGQ NVLLTENAEV KLVDFGVSAQ LDRTVGRRNT FIGTPYWMAP EVIACDENPD
     ATYDYRSDIW SLGITAIEMA EGAPPLCDMH PMRALFLIPR NPPPRLKSKK WSKKFTDFID
     TCLIKTYLSR PPTEQLLKFP FIRDQPTERQ VRIQLKDHID RSRKKRGEKE ETEYEYSGSE
     EEDDSHGEEG EPSSIMNVPG ESTLRREFLR LQQENKSNSE ALKQQQQLQQ QQQRDPEAHI
     KHLLHQRQRR IEEQKEERRR VEEQQRRERE QRKLQEKEQQ RRLEDMQALR REEERRQAER
     EQEYKRKQLE EQRQSERLQR QLQQEHAYLK SLQQQQQQQQ LQKQQQQQQQ ILPGDRKPLY
     HYGRGINPAD KPAWAREVEE RARMNKQQNS PLAKAKPSSA GPEPPISQAS PSPPGPLSQT
     PPMQRPVEPQ EGPHKSLVAH RVPLKPYAAP VPRSQSLQDQ PTRNLAAFPA SHDPDPAAVP
     TPTATPSARG AVIRQNSDPT SEGPGPSPNP PSWVRPDNEA PPKVPQRTSS IATALNTSGA
     GGSRPAQAVR ARPRSNSAWQ IYLQRRAERG TPKPPGPPAQ PPGPPNASSN PDLRRSDPGW
     ERSDSVLPAS HGHLPQAGSL ERNRNRVGAS TKLDSSPVLS PGNKAKPEDH RSRPGRPASY
     KRAIGEDFVL LKERTLDEAP KPPKKAMDYS SSSEEVESSE EEEEEGDGEP SEGSRDTPGG
     RDGDTDSVST MVVHDVEEIS GTQPSYGGGT MVVQRTPEEE RSLLLADSNG YTNLPDVVQP
     SHSPTENSKG QSPPTKDGGS DYQSRGLVKA PGKSSFTMFV DLGIYQPGGS GDTIPITALV
     GGEGGRLDQL QFDVRKGSVV NVNPTNTRAH SETPEIRKYK KRFNSEILCA ALWGVNLLVG
     TENGLMLLDR SGQGKVYGLI GRRRFQQMDV LEGLNLLITI SGKRNKLRVY YLSWLRNKIL
     HNDPEVEKKQ GWTTVGDMEG CGHYRVVKYE RIKFLVIALK NSVEVYAWAP KPYHKFMAFK
     SFADLPHRPL LVDLTVEEGQ RLKVIYGSSA GFHAVDVDSG NSYDIYIPVH IQSQITPHAI
     IFLPNTDGME MLLCYEDEGV YVNTYGRIIK DVVLQWGEMP TSVAYICSNQ IMGWGEKAIE
     IRSVETGHLD GVFMHKRAQR LKFLCERNDK VFFASVRSGG SSQVYFMTLN RNCIMNW
//
ID   Q5XJV5_MOUSE            Unreviewed;      2069 AA.
AC   Q5XJV5;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   08-MAR-2011, entry version 50.
DE   SubName: Full=Nuclear receptor coactivator 6;
GN   Name=Ncoa6; ORFNames=RP23-32O9.2-001, mCG_21081;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; 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.
RA   Clark S.;
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; BC083187; AAH83187.1; -; mRNA.
DR   EMBL; AL844852; CAM18924.1; -; Genomic_DNA.
DR   EMBL; AL845325; CAM18924.1; JOINED; Genomic_DNA.
DR   EMBL; AL845325; CAM21110.1; -; Genomic_DNA.
DR   EMBL; AL844852; CAM21110.1; JOINED; Genomic_DNA.
DR   EMBL; CH466551; EDL06121.1; -; Genomic_DNA.
DR   IPI; IPI00123351; -.
DR   RefSeq; NP_062799.2; NM_019825.2.
DR   UniGene; Mm.27592; -.
DR   ProteinModelPortal; Q5XJV5; -.
DR   STRING; Q5XJV5; -.
DR   PRIDE; Q5XJV5; -.
DR   Ensembl; ENSMUST00000043126; ENSMUSP00000045386; ENSMUSG00000038369.
DR   Ensembl; ENSMUST00000109670; ENSMUSP00000105295; ENSMUSG00000038369.
DR   GeneID; 56406; -.
DR   KEGG; mmu:56406; -.
DR   NMPDR; fig|10090.3.peg.7241; -.
DR   UCSC; uc008nkm.1; mouse.
DR   CTD; 56406; -.
DR   MGI; MGI:1929915; Ncoa6.
DR   HOGENOM; HBG716152; -.
DR   HOVERGEN; HBG052586; -.
DR   InParanoid; Q5XJV5; -.
DR   OMA; MMLMMQQ; -.
DR   PhylomeDB; Q5XJV5; -.
DR   NextBio; 312534; -.
DR   ArrayExpress; Q5XJV5; -.
DR   Bgee; Q5XJV5; -.
DR   Genevestigator; Q5XJV5; -.
DR   GO; GO:0005667; C:transcription factor complex; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0007420; P:brain development; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0060716; P:labyrinthine layer blood vessel development; IMP:MGI.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:MGI.
PE   2: Evidence at transcript level;
KW   Receptor.
SQ   SEQUENCE   2069 AA;  219958 MW;  018B0C0F6886A200 CRC64;
     MVLDDLPNFE DIYTSLCSST MGDSEVEFDS GLEDDDTKSD SILEDSTIFV AFKGNIDDKD
     FKWKLDAILK NVPNLLHMES SKLKVQKVEP WNSVRVTFNI PREAAERLRI LAQSNNQQLR
     DLGILSVQIE GEGAINLALG QNRSQDVRMN GPVASGNSVR MEAGFPMASG PGLIRMTSPA
     AVMTPQGGNM SSSMMAPGPN PELQPRTPRP ASQSDAMDPL LSGLHIQQQS HPSGSLPPAH
     HSMQPVPVNR QMNPANFPQL QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQLQTRPLQQ
     HQQQPQGIRP QFTAPTQVPV PPGWNQLPSG ALQPPPAQGS LGTMTTNQGW KKAPLPSPMQ
     AQLQARPSLA TVQTPSHPPP PYPFGSQQAS QAHTNFPQMS NPGQFTAPQM KGLQGGPSRV
     PTPLQQPHLT NKSPASSPSS FQQGSPASSP TVNQTQQQMG PRPPQNNPLS QGFQQPVSSP
     GRNPMVQQGN VPPNFMVMQQ QPPNQGPQSL HPGLGGMPKR LPPGFSAGQA NPNFMQGQVP
     STTAATPGNS GALQLQANQN VQHAGGQGAG PPQNQMQVSH GPPNMMQPSL MGIHGNINNQ
     QAGSSGVPQV TLGNMQGQPQ QGPPSQLMGM HQQIVPSQGQ MAQQQGTLNP QNPMILSRAQ
     LMPQGQMMVN AQNQNLGPSP QRMTPPKQML PQQGPQMMAP HNQMMGPQGQ VLLQQNPMIE
     QIMTNQMQGN KAQFNSQNQS NVMPGPAQIM RGPTPNMQGN MVQFTGQMSG QMLPQQGPVN
     NSPSQVMGIQ GQVLRPPGPS PHMAQQHNDP VTTANNDVNL SQMMPDVSMQ QASMVPPHVQ
     SMQGNSASGS HFSGHGVSFN APFGGAPNGS QMSCGQNPGF PVNKDVTLTS PLLVNLLQSD
     ISAGHFGVNN KQNNTNANKP KKKKPPRKKK NCHQDLNTPD NRPTGLEEVD QQSLPGEQGI
     NLDTTGPKLP DFSNRPPGYP TQPVEQRPLP QMPPQLMQHV APPPQPPQQQ PQPQLPQQQQ
     PPPPSQPQSQ QQQQQQQMMM MLMMQQDPKS IRLPVSQNVH PPRGPLNPDS QRMPVQQSGN
     VPVMVGLQGP ASVPPSPDKQ RMPMSVNTPM GSNSRKMVYQ ENPQNSSSSP LGEMSSLPEA
     SGSEVPSVAG GPNNMPSHLV VSQNQLMMTG PKPGPSPLSA TQGATPQQPP VNSLPSSHGH
     HFPNVAAPTQ TSRPKTPNRA SPRPYYPQTP NNRPPSTEPS EISLSPERLN ASIAGLFPPQ
     INIPLPPRPN LNRGFDQQGL NPTTLKAIGQ APSNLTITNP PNFAAPQAHK LDSVVVNSGK
     QSNPGTTKRA SPSNSRRSSP GSSRKTTPSP GRQNSKAPKL TLASQTSTTM LQNMELPRNV
     LVGPTPLANP PLPGSFPNNT GLNPQNPTVP VPAMGTVLED NKESVNIPQD SDCQNAQGRK
     EQVNTELKVV PTQEAKMAVP EDQSKKDGQP LDPNKLPSVE ENKNLMSPAM REAPTSLSQL
     LDNSGAPNVT IKPPGLTDLE VTPPVVSGED LRKASVIPTL QDPPSKEPST SLSSPHSSEP
     CSTLARSELS EVSSNTAPSI PPVMSRPVSS SSISTPLPPN QITVFVTSNP ITTSSNTSAA
     LPTHLQSALM STVVTMPNVG NKVMVSEGQS AAQSNARPQF ITPVFINSSS IIQVMKGSQP
     STIPATPLTT NSGLMPPSVA VVGPLHIPQN IKFSSAPVTP NVPSSSPAPN IQTGRPLVLS
     SRATPVQLPS PPCTSSPVVA PNPSVQQVKE LNPDEASPQT NTSADQSTLP PSQPTTVVSP
     LLTNSPGSSA NRRSPVSSSK GKGKVDKIGQ ILLTKACKKV TGSLEKGEEQ YGADGETEGP
     GLEITTPGLM GTEQCSTELD SKTPTPSAPT LLKMTSSPMG PSSTSTGPIL PGGALPTSVR
     SIVTTLVPSE LISTAPTTKG NHGGVTSEPL AGGLVEEKVG SHPELLPSIA PSQNLAPKET
     PATALQGSVA RPELEANAAI ASGQSCEPKE IVEKSKTLTS RRNSRTEEPT MASESVENGH
     RKRSSRPASA SSSTKDITGA VQSKRRKSK
//
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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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   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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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   ITF2_MOUSE              Reviewed;         670 AA.
AC   Q60722; Q60721; Q62211; Q64072; Q80UE8;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 103.
DE   RecName: Full=Transcription factor 4;
DE            Short=TCF-4;
DE   AltName: Full=Class A helix-loop-helix transcription factor ME2;
DE   AltName: Full=Immunoglobulin transcription factor 2;
DE            Short=ITF-2;
DE            Short=MITF-2;
DE   AltName: Full=SL3-3 enhancer factor 2;
DE            Short=SEF-2;
GN   Name=Tcf4; Synonyms=Itf2, Sef2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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=95075243; PubMed=7984047; DOI=10.1016/0169-328X(94)90297-6;
RA   Soosaar A., Chiaramello A., Zuber M.X., Neuman T.;
RT   "Expression of basic-helix-loop-helix transcription factor ME2 during
RT   brain development and in the regions of neuronal plasticity in the
RT   adult brain.";
RL   Brain Res. Mol. Brain Res. 25:176-180(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RX   MEDLINE=96216452; PubMed=8631961; DOI=10.1074/jbc.271.7.3555;
RA   Skerjanc I.S., Truong J., Filion P., McBurney M.W.;
RT   "A splice variant of the ITF-2 transcript encodes a transcription
RT   factor that inhibits MyoD activity.";
RL   J. Biol. Chem. 271:3555-3561(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=97133297; PubMed=8978694;
RA   Pscherer A., Doerflinger U., Kirfel J., Gawlas K., Rueschoff J.,
RA   Buettner R., Schuele R.;
RT   "The helix-loop-helix transcription factor SEF-2 regulates the
RT   activity of a novel initiator element in the promoter of the human
RT   somatostatin receptor II gene.";
RL   EMBO J. 15:6680-6690(1996).
RN   [4]
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   [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 HIVEP2.
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).
CC   -!- FUNCTION: Transcription factor that binds to the immunoglobulin
CC       enchancer Mu-E5/KE5-motif. Isoform 2 inhibits MYOD1 activation of
CC       the cardiac alpha-actin promoter. Binds to the E-box present in
CC       the somatostatin receptor 2 initiator element (SSTR2-INR) to
CC       activate transcription. May have a regulatory function in
CC       developmental processes as well as during neuronal plasticity.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another
CC       bHLH protein. Isoform 2 seems to form inactive heterodimers with
CC       MYOD1. Interacts with HIVEP2.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=2; Synonyms=MITF-2B;
CC         IsoId=Q60722-1; Sequence=Displayed;
CC       Name=1; Synonyms=MITF-2A;
CC         IsoId=Q60722-2; Sequence=VSP_002113, VSP_002114;
CC       Name=3; Synonyms=MITF-2B-delta;
CC         IsoId=Q60722-3; Sequence=VSP_002115;
CC   -!- TISSUE SPECIFICITY: Expressed in the cerebral cortex, Purkinje and
CC       granule cell layers of the cerebellum, olfactory neuroepithelium,
CC       pyramidal cells of hippocampal layers CA1-CA4, and in the granular
CC       cells of the dentate gyrus.
CC   -!- DEVELOPMENTAL STAGE: Expressed in proliferative zones during
CC       development and in the adult in areas of neuronal plasticity. At
CC       embryonic day 12 (E12), expression is localized in the cortex,
CC       cerebellum, pons, medulla and spinal cord. From E18 to adulthood,
CC       high levels of expression are found in the pyramidal cells of
CC       hippocampal layers CA1-CA4, and in the granular cells of the
CC       dentate gyrus. At postnatal day 7, expression is high in the
CC       visual cortex and in the subependymal region extending from the
CC       anterior lateral ventricle into the olfactory bulb.
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; S75870; AAB32662.1; -; mRNA.
DR   EMBL; U16321; AAC52414.1; -; mRNA.
DR   EMBL; U16322; AAC52415.1; -; mRNA.
DR   EMBL; X91753; CAA62868.1; -; mRNA.
DR   EMBL; AK081012; BAC38116.1; -; mRNA.
DR   EMBL; BC043050; AAH43050.1; -; mRNA.
DR   IPI; IPI00120128; -.
DR   IPI; IPI00400417; -.
DR   IPI; IPI00400418; -.
DR   PIR; I52648; I52648.
DR   RefSeq; NP_001077436.1; NM_001083967.1.
DR   RefSeq; NP_038713.1; NM_013685.2.
DR   UniGene; Mm.4269; -.
DR   ProteinModelPortal; Q60722; -.
DR   SMR; Q60722; 568-627.
DR   IntAct; Q60722; 1.
DR   MINT; MINT-2567893; -.
DR   STRING; Q60722; -.
DR   PhosphoSite; Q60722; -.
DR   PRIDE; Q60722; -.
DR   Ensembl; ENSMUST00000078486; ENSMUSP00000077577; ENSMUSG00000053477.
DR   Ensembl; ENSMUST00000114978; ENSMUSP00000110629; ENSMUSG00000053477.
DR   Ensembl; ENSMUST00000114985; ENSMUSP00000110636; ENSMUSG00000053477.
DR   GeneID; 21413; -.
DR   KEGG; mmu:21413; -.
DR   UCSC; uc008fnq.1; mouse.
DR   UCSC; uc008fns.1; mouse.
DR   CTD; 21413; -.
DR   MGI; MGI:98506; Tcf4.
DR   GeneTree; ENSGT00510000046438; -.
DR   HOVERGEN; HBG003854; -.
DR   OrthoDB; EOG4Z62N3; -.
DR   PhylomeDB; Q60722; -.
DR   NextBio; 300700; -.
DR   ArrayExpress; Q60722; -.
DR   Bgee; Q60722; -.
DR   CleanEx; MM_TCF4; -.
DR   Genevestigator; Q60722; -.
DR   GermOnline; ENSMUSG00000053477; Mus musculus.
DR   GO; GO:0005667; C:transcription factor complex; IDA:BHF-UCL.
DR   GO; GO:0070888; F:E-box binding; IDA:BHF-UCL.
DR   GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:BHF-UCL.
DR   GO; GO:0001011; F:sequence-specific DNA binding RNA polymerase recruiting transcription factor activity; IDA:BHF-UCL.
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:BHF-UCL.
DR   GO; GO:0001087; F:TFIIB-class binding transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0001093; F:TFIIB-class transcription factor binding; IDA:BHF-UCL.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR   GO; GO:0016986; F:transcription initiation factor activity; IDA:BHF-UCL.
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   GO; GO:0065004; P:protein-DNA complex assembly; IDA:BHF-UCL.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:BHF-UCL.
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   Activator; Alternative splicing; Developmental protein; DNA-binding;
KW   Nucleus; Phosphoprotein; Transcription; Transcription regulation.
FT   CHAIN         1    670       Transcription factor 4.
FT                                /FTId=PRO_0000127257.
FT   DOMAIN      378    399       Leucine-zipper.
FT   DOMAIN      580    621       Helix-loop-helix motif.
FT   DNA_BIND    567    579       Basic motif.
FT   REGION        1     83       Essential for MYOD1 inhibition.
FT   REGION      622    645       Class A specific domain.
FT   COMPBIAS    227    230       Poly-Ser.
FT   MOD_RES     371    371       Phosphoserine (By similarity).
FT   VAR_SEQ       1    159       Missing (in isoform 1).
FT                                /FTId=VSP_002113.
FT   VAR_SEQ     160    182       LHSSAMEVQTKKVRKVPPGLPSS -> MYCAYTIPGMGGNS
FT                                LMYYYNGKA (in isoform 1).
FT                                /FTId=VSP_002114.
FT   VAR_SEQ     545    548       Missing (in isoform 3).
FT                                /FTId=VSP_002115.
FT   CONFLICT    159    159       P -> S (in Ref. 3; CAA62868).
FT   CONFLICT    180    180       P -> A (in Ref. 3; CAA62868).
FT   CONFLICT    238    238       G -> A (in Ref. 1; AAB32662).
SQ   SEQUENCE   670 AA;  71625 MW;  F21CF79FDC0BF09E CRC64;
     MHHQQRMAAL GTDKELSDLL DFSAMFSPPV SSGKNGPTSL ASGHFTGSNV EDRSSSGSWG
     TGGHPSPSRN YGDGTPYDHM TSRDLGSHDN LSPPFVNSRI QSKTERGSYS SYGRENVQGC
     HQQSLLGGDM DMGNPGTLSP TKPGSQYYQY SSNNARRRPL HSSAMEVQTK KVRKVPPGLP
     SSVYAPSAST ADYNRDSPGY PSSKPAASTF PSSFFMQDGH HSSDPWSSSS GMNQPGYGGM
     LGNSSHIPQS SSYCSLHPHE RLSYPSHSSA DINSSLPPMS TFHRSGTNHY STSSCTPPAN
     GTDSIMANRG TGAAGSSQTG DALGKALASI YSPDHTNNSF SSNPSTPVGS PPSLSAGTAV
     WSRNGGQASS SPNYEGPLHS LQSRIEDRLE RLDDAIHVLR NHAVGPSTAV PGGHGDMHGI
     MGPSHNGAMG SLGSGYGTSL LSANRHSLMV GAHREDGVAL RGSHSLLPNQ VPVPQLPVQS
     ATSPDLNPPQ DPYRGMPPGL QGQSVSSGSS EIKSDDEGDE NLQDTKSSED KKLDDDKKDI
     KSITRSRSSN NDDEDLTPEQ KAEREKERRM ANNARERLRV RDINEAFKEL GRMVQLHLKS
     DKPQTKLLIL HQAVAVILSL EQQVRERNLN PKAACLKRRE EEKVSSEPPP LSLAGPHPGM
     GDAANHMGQM
//
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.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   MERTK_MOUSE             Reviewed;         994 AA.
AC   Q60805; Q62194;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=Tyrosine-protein kinase Mer;
DE            EC=2.7.10.1;
DE   AltName: Full=Proto-oncogene c-Mer;
DE   AltName: Full=Receptor tyrosine kinase MerTK;
DE   Flags: Precursor;
GN   Name=Mertk; Synonyms=Mer;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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=95303502; PubMed=7784083;
RA   Graham D.K., Bowman G.W., Dawson T.L., Stanford W.L., Earp H.S.,
RA   Snodgrass H.R.;
RT   "Cloning and developmental expression analysis of the murine c-mer
RT   tyrosine kinase.";
RL   Oncogene 10:2349-2359(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 472-994.
RC   STRAIN=CD-1; TISSUE=Testis;
RA   Dowds C.A., Burks D.J., Saling P.M.;
RT   "A cDNA encoding part of a novel putative receptor tyrosine kinase.";
RL   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBUNIT: Interacts (upon activation) with TNK2; stimulates TNK2
CC       autophosphorylation (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Seems to be expressed predominantly if not
CC       exclusively in the monocytic lineage.
CC   -!- DEVELOPMENTAL STAGE: Expressed during most, if not all, stages of
CC       embryological development beginning in the morula and blastocyst
CC       and progressing through the yolk sac and fetal liver stages.
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   -----------------------------------------------------------------------
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DR   EMBL; U21301; AAA80222.1; -; mRNA.
DR   EMBL; L11625; AAA85355.1; -; mRNA.
DR   IPI; IPI00121254; -.
DR   PIR; I49276; I49276.
DR   RefSeq; NP_032613.1; NM_008587.1.
DR   UniGene; Mm.239655; -.
DR   ProteinModelPortal; Q60805; -.
DR   SMR; Q60805; 92-487, 570-858.
DR   STRING; Q60805; -.
DR   PhosphoSite; Q60805; -.
DR   PRIDE; Q60805; -.
DR   Ensembl; ENSMUST00000014505; ENSMUSP00000014505; ENSMUSG00000014361.
DR   GeneID; 17289; -.
DR   KEGG; mmu:17289; -.
DR   UCSC; uc008mgt.1; mouse.
DR   CTD; 17289; -.
DR   MGI; MGI:96965; Mertk.
DR   HOGENOM; HBG444090; -.
DR   HOVERGEN; HBG006346; -.
DR   InParanoid; Q60805; -.
DR   OMA; TGPKHIP; -.
DR   OrthoDB; EOG4Z8XW3; -.
DR   PhylomeDB; Q60805; -.
DR   BRENDA; 2.7.10.1; 244.
DR   NextBio; 291808; -.
DR   ArrayExpress; Q60805; -.
DR   Bgee; Q60805; -.
DR   CleanEx; MM_MERTK; -.
DR   Genevestigator; Q60805; -.
DR   GermOnline; ENSMUSG00000014361; 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:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:EC.
DR   GO; GO:0043277; P:apoptotic cell clearance; IMP: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: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; 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   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 4.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00409; IG; 2.
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   2: Evidence at transcript level;
KW   ATP-binding; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Proto-oncogene;
KW   Receptor; Repeat; Signal; Transferase; Transmembrane;
KW   Transmembrane helix; Tyrosine-protein kinase.
FT   SIGNAL        1     18       Potential.
FT   CHAIN        19    994       Tyrosine-protein kinase Mer.
FT                                /FTId=PRO_0000024444.
FT   TOPO_DOM     19    497       Extracellular (Potential).
FT   TRANSMEM    498    518       Helical; (Potential).
FT   TOPO_DOM    519    994       Cytoplasmic (Potential).
FT   DOMAIN       75    181       Ig-like C2-type 1.
FT   DOMAIN      192    268       Ig-like C2-type 2.
FT   DOMAIN      279    374       Fibronectin type-III 1.
FT   DOMAIN      378    477       Fibronectin type-III 2.
FT   DOMAIN      582    852       Protein kinase.
FT   NP_BIND     588    596       ATP (By similarity).
FT   ACT_SITE    718    718       Proton acceptor (By similarity).
FT   BINDING     610    610       ATP (By similarity).
FT   MOD_RES     538    538       Phosphoserine (By similarity).
FT   MOD_RES     608    608       Phosphoserine (By similarity).
FT   MOD_RES     749    749       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     924    924       Phosphotyrosine (By similarity).
FT   MOD_RES     963    963       Phosphoserine (By similarity).
FT   MOD_RES     965    965       Phosphoserine (By similarity).
FT   MOD_RES     974    974       Phosphoserine (By similarity).
FT   CARBOHYD     91     91       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    108    108       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    165    165       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    202    202       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    210    210       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    229    229       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    289    289       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    311    311       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    324    324       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    331    331       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    349    349       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    384    384       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    390    390       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    437    437       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    449    449       N-linked (GlcNAc...) (Potential).
FT   DISULFID    109    170       By similarity.
FT   DISULFID    213    257       By similarity.
FT   CONFLICT    473    476       IIIP -> SARA (in Ref. 2).
FT   CONFLICT    516    516       I -> V (in Ref. 2; AAA85355).
SQ   SEQUENCE   994 AA;  110157 MW;  603C09FA11F76FE0 CRC64;
     MVLAPLLLGL LLLPALWSGG TAEKWEETEL DQLFSGPLPG RLPVNHRPFS APHSSRDQLP
     PPQTGRSHPA HTAAPQVTST ASKLLPPVAF NHTIGHIVLS EHKNVKFNCS INIPNTYQET
     AGISWWKDGK ELLGAHHSIT QFYPDEEGVS IIALFSIASV QRSDNGSYFC KMKVNNREIV
     SDPIYVEVQG LPYFIKQPES VNVTRNTAFN LTCQAVGPPE PVNIFWVQNS SRVNEKPERS
     PSVLTVPGLT ETAVFSCEAH NDKGLTVSKG VHINIKVIPS PPTEVHILNS TAHSILVSWV
     PGFDGYSPLQ NCSIQVKEAD RLSNGSVMVF NTSASPHLYE IQQLQALANY SIAVSCRNEI
     GWSAVSPWIL ASTTEGAPSV APLNITVFLN ESNNILDIRW TKPPIKRQDG ELVGYRISHV
     WESAGTYKEL SEEVSQNGSW AQIPVQIHNA TCTVRIAAIT KGGIGPFSEP VNIIIPEHSK
     VDYAPSSTPA PGNTDSMFII LGCFCGFILI GLILCISLAL RRRVQETKFG GAFSEEDSQL
     VVNYRAKKSF CRRAIELTLQ SLGVSEELQN KLEDVVIDRN LLVLGKVLGE GEFGSVMEGN
     LKQEDGTSQK VAVKTMKLDN FSQREIEEFL SEAACMKDFN HPNVIRLLGV CIELSSQGIP
     KPMVILPFMK YGDLHTFLLY SRLNTGPKYI HLQTLLKFMM DIAQGMEYLS NRNFLHRDLA
     ARNCMLRDDM TVCVADFGLS KKIYSGDYYR QGRIAKMPVK WIAIESLADR VYTSKSDVWA
     FGVTMWEITT RGMTPYPGVQ NHEMYDYLLH GHRLKQPEDC LDELYDIMYS CWSADPLDRP
     TFSVLRLQLE KLSESLPDAQ DKESIIYINT QLLESCEGIA NGPSLTGLDM NIDPDSIIAS
     CTPGAAVSVV TAEVHENNLR EERYILNGGN EEWEDVSSTP FAAVTPEKDG VLPEDRLTKN
     GVSWSHHSTL PLGSPSPDEL LFVDDSLEDS EVLM
//
ID   NCOA2_MOUSE             Reviewed;        1462 AA.
AC   Q61026; O09001; P97759;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 2.
DT   11-JAN-2011, entry version 112.
DE   RecName: Full=Nuclear receptor coactivator 2;
DE            Short=NCoA-2;
DE   AltName: Full=Glucocorticoid receptor-interacting protein 1;
DE            Short=GRIP-1;
DE   AltName: Full=Transcriptional intermediary factor 2;
GN   Name=Ncoa2; Synonyms=Grip1, Tif2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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 NR3C2.
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=97265407; PubMed=9111344;
RA   Hong H., Kohli K., Garabedian M.J., Stallcup M.R.;
RT   "GRIP1, a transcriptional coactivator for the AF-2 transactivation
RT   domain of steroid, thyroid, retinoid, and vitamin D receptors.";
RL   Mol. Cell. Biol. 17:2735-2744(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 322-1119.
RC   STRAIN=ICR; TISSUE=Embryo;
RX   MEDLINE=96209838; PubMed=8643509; DOI=10.1073/pnas.93.10.4948;
RA   Hong H., Kohli K., Trivedi A., Johnson D.L., Stallcup M.R.;
RT   "GRIP1, a novel mouse protein that serves as a transcriptional
RT   coactivator in yeast for the hormone binding domains of steroid
RT   receptors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:4948-4952(1996).
RN   [4]
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   [5]
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   [6]
RP   FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH EP300 AND NCOA2.
RX   PubMed=11997499; DOI=10.1128/MCB.22.11.3621-3632.2002;
RA   Lee Y.-H., Koh S.S., Zhang X., Cheng X., Stallcup M.R.;
RT   "Synergy among nuclear receptor coactivators: selective requirement
RT   for protein methyltransferase and acetyltransferase activities.";
RL   Mol. Cell. Biol. 22:3621-3632(2002).
RN   [7]
RP   INTERACTION WITH CASP8AP2.
RX   PubMed=12477726; DOI=10.1074/jbc.M209234200;
RA   Kino T., Chrousos G.P.;
RT   "Tumor necrosis factor alpha receptor- and Fas-associated FLASH
RT   inhibit transcriptional activity of the glucocorticoid receptor by
RT   binding to and interfering with its interaction with p160 type nuclear
RT   receptor coactivators.";
RL   J. Biol. Chem. 278:3023-3029(2003).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-699, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., 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-716, 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-493, 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 for steroid receptors and
CC       nuclear receptors. Coactivator of the steroid binding domain (AF-
CC       2) but not of the modulating N-terminal domain (AF-1). Required
CC       with NCOA1 to control energy balance between white and brown
CC       adipose tissues.
CC   -!- SUBUNIT: Interacts with NR3C1. Present in a complex containing
CC       NCOA3, IKKA, IKKB, IKBKG and CREBBP. Interacts (via C-terminus)
CC       with CREBBP. Interacts with ESR1, RARA and RXRA (By similarity).
CC       Interacts with HIF1A, NCOA1, APEX, NR3C2, and CARM1. Present in a
CC       complex containing CARM1 and EP300/P300. Interacts with CASP8AP2
CC       and TTLL5/STAMP. Interacts with PSMB9 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- DOMAIN: Contains four Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. The
CC       LXXLL motifs are essential for the association with nuclear
CC       receptors and are, at least in part, functionally redundant (By
CC       similarity).
CC   -!- DOMAIN: The LLXXLXXXL motif is involved in transcriptional
CC       coactivation and CREBBP/CBP binding (By similarity).
CC   -!- DOMAIN: Contains 2 C-terminal transcription activation domains
CC       (AD1 and AD2) that can function independently (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
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.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB61575.1; Type=Frameshift; Positions=251, 256, 302, 321, 959, 964, 983;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; U39060; AAC53151.1; -; mRNA.
DR   EMBL; AF000582; AAB61575.1; ALT_FRAME; mRNA.
DR   IPI; IPI00116968; -.
DR   PIR; T30193; T30193.
DR   PIR; T42639; T42639.
DR   UniGene; Mm.2537; -.
DR   PDB; 1L2I; X-ray; 1.95 A; C/D=686-698.
DR   PDB; 1OSV; X-ray; 2.50 A; C/D/E=741-752.
DR   PDB; 1WM0; X-ray; 2.90 A; Y=684-697.
DR   PDB; 2Q6J; X-ray; 2.70 A; C/D=686-698.
DR   PDB; 2QA6; X-ray; 2.60 A; C/D=686-698.
DR   PDB; 2QA8; X-ray; 1.85 A; C/D=686-698.
DR   PDB; 2QAB; X-ray; 1.89 A; C/D=686-698.
DR   PDB; 2QGT; X-ray; 2.15 A; C/D=686-698.
DR   PDB; 2QGW; X-ray; 2.39 A; C/D=686-698.
DR   PDB; 2QH6; X-ray; 2.70 A; C/D=686-698.
DR   PDB; 2QPY; X-ray; 2.50 A; B=744-753.
DR   PDB; 2QR9; X-ray; 2.00 A; C/D=686-698.
DR   PDB; 2QSE; X-ray; 1.85 A; C/D=686-698.
DR   PDB; 2QXM; X-ray; 2.30 A; C/D=686-698.
DR   PDB; 3MNE; X-ray; 1.96 A; B=740-752.
DR   PDB; 3MNO; X-ray; 1.55 A; B=740-752.
DR   PDB; 3MNP; X-ray; 1.50 A; B=740-752.
DR   PDBsum; 1L2I; -.
DR   PDBsum; 1OSV; -.
DR   PDBsum; 1WM0; -.
DR   PDBsum; 2Q6J; -.
DR   PDBsum; 2QA6; -.
DR   PDBsum; 2QA8; -.
DR   PDBsum; 2QAB; -.
DR   PDBsum; 2QGT; -.
DR   PDBsum; 2QGW; -.
DR   PDBsum; 2QH6; -.
DR   PDBsum; 2QPY; -.
DR   PDBsum; 2QR9; -.
DR   PDBsum; 2QSE; -.
DR   PDBsum; 2QXM; -.
DR   PDBsum; 3MNE; -.
DR   PDBsum; 3MNO; -.
DR   PDBsum; 3MNP; -.
DR   ProteinModelPortal; Q61026; -.
DR   SMR; Q61026; 28-86, 119-173, 267-376, 1071-1113.
DR   DIP; DIP-5979N; -.
DR   MINT; MINT-236676; -.
DR   STRING; Q61026; -.
DR   PhosphoSite; Q61026; -.
DR   PRIDE; Q61026; -.
DR   Ensembl; ENSMUST00000006037; ENSMUSP00000006037; ENSMUSG00000005886.
DR   UCSC; uc007aim.1; mouse.
DR   MGI; MGI:1276533; Ncoa2.
DR   eggNOG; roNOG09892; -.
DR   HOGENOM; HBG755348; -.
DR   HOVERGEN; HBG052583; -.
DR   InParanoid; Q61026; -.
DR   ArrayExpress; Q61026; -.
DR   Bgee; Q61026; -.
DR   CleanEx; MM_GRIP1; -.
DR   CleanEx; MM_NCOA2; -.
DR   Genevestigator; Q61026; -.
DR   GermOnline; ENSMUSG00000005886; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0035257; F:nuclear hormone receptor binding; IEA:InterPro.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0030375; F:thyroid hormone receptor coactivator activity; IDA:MGI.
DR   GO; GO:0016564; F:transcription repressor activity; IDA: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; 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; IPR001610; PAC.
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; 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; SM00086; PAC; 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; Acetylation; Activator; Nucleus; Phosphoprotein; Repeat;
KW   Transcription; Transcription regulation.
FT   CHAIN         1   1462       Nuclear receptor coactivator 2.
FT                                /FTId=PRO_0000094403.
FT   DOMAIN       17     20       Helix-loop-helix motif.
FT   DOMAIN      119    183       PAS.
FT   DNA_BIND     21     84       Basic motif.
FT   REGION      691    743       CASP8AP2-binding.
FT   MOTIF       641    645       LXXLL motif 1.
FT   MOTIF       690    694       LXXLL motif 2.
FT   MOTIF       745    749       LXXLL motif 3.
FT   MOTIF       878    882       LXXLL motif 4.
FT   MOTIF      1079   1087       LLXXLXXXL motif.
FT   MOD_RES      29     29       Phosphoserine (By similarity).
FT   MOD_RES     493    493       Phosphoserine.
FT   MOD_RES     565    565       Phosphoserine (By similarity).
FT   MOD_RES     636    636       N6-acetyllysine (By similarity).
FT   MOD_RES     640    640       N6-acetyllysine (By similarity).
FT   MOD_RES     699    699       Phosphoserine.
FT   MOD_RES     716    716       Phosphoserine.
FT   MOD_RES     736    736       Phosphoserine (By similarity).
FT   MOD_RES     780    780       N6-acetyllysine (By similarity).
FT   MOD_RES     785    785       N6-acetyllysine (By similarity).
FT   CONFLICT     51     51       D -> E (in Ref. 2; AAB61575).
FT   CONFLICT    140    141       SE -> FR (in Ref. 2; AAB61575).
FT   CONFLICT    194    194       T -> S (in Ref. 2; AAB61575).
FT   CONFLICT    256    256       V -> I (in Ref. 2; AAB61575).
FT   CONFLICT    286    286       S -> T (in Ref. 2; AAB61575).
FT   CONFLICT    420    420       G -> S (in Ref. 2; AAB61575).
FT   CONFLICT    512    512       S -> N (in Ref. 2; AAB61575).
FT   CONFLICT    594    594       E -> K (in Ref. 2; AAB61575).
FT   CONFLICT    607    608       EE -> KK (in Ref. 2; AAB61575).
FT   CONFLICT    864    864       R -> C (in Ref. 2; AAB61575).
FT   CONFLICT    869    869       T -> S (in Ref. 2; AAB61575).
FT   CONFLICT    884    884       N -> Y (in Ref. 2; AAB61575).
FT   CONFLICT    972    972       M -> K (in Ref. 2; AAB61575).
FT   CONFLICT    980    980       M -> K (in Ref. 2; AAB61575).
FT   CONFLICT    991    991       R -> G (in Ref. 2; AAB61575).
FT   CONFLICT    996    996       P -> L (in Ref. 2; AAB61575).
FT   CONFLICT   1407   1407       C -> G (in Ref. 2; AAB61575).
FT   CONFLICT   1446   1446       P -> L (in Ref. 2; AAB61575).
FT   HELIX       689    695
FT   HELIX       743    749
SQ   SEQUENCE   1462 AA;  158512 MW;  ACA018979FCDCAB5 CRC64;
     MSGMGENTSD PSRAETRKRK ECPDQLGPSP KRSTEKRNRE QENKYIEELA DLIFANFNDI
     DNFNFKPDKC AILKETVKQI RQIKEQEKAA AANIDEVQKS DVSSTGQGVI DKDALGPMML
     EALDGFFFVV NLEGSVVFVS ENVTQYLRYN QEELMNKSVY SILHVGDHTE FVKNLLPKSM
     VNGGSWSGEP PRRTSHTFNC RMLVKPLPDS EEEGHDSQEA HQKYEAMQCF AVSQPKSIKE
     EGEDLQSCLI CVARRVPMKE RPTLPSSESF TTRQDLQGKI TSLDTSTMRA AMKPGWEDLV
     RRCIQKFHTQ HEGESLSYAK RHHHEVLRQG LAFSQIYRFS LSDGTLVAAQ TKSKLIRSQT
     TNEPQLVISL HMLHREQNVC VMNPDLTGQA MGKPLNPISS SSPAHQALCS GNPGQDMTLG
     SNINFPMNGP KEQMGMPMGR FGGSGGMNHV SGMQATTPQG SNYALKMNSP SQSSPGMNPG
     QASSVLSPRQ RMSPGVAGSP RIPPSQFSPA GSLHSPVGVC SSTGNSHSYT NSSLNALQAL
     SEGHGVSLGS SLASPDLKMG NLQNSPVNMN PPPLSKMGSL DSKDCFGLYG EPSEGTTGQA
     EASCHPEEQK GPNDSSMPQA ASGDRAEGHS RLHDSKGQTK LLQLLTTKSD QMEPSPLPSS
     LSDTNKDSTG SLPGPGSTHG TSLKEKHKIL HRLLQDSSSP VDLAKLTAEA TGKELSQESS
     STAPGSEVTV KQEPASPKKK ENALLRYLLD KDDTKDIGLP EITPKLERLD SKTDPASNTK
     LIAMKTVKEE VSFEPSDQPG SELDNLEEIL DDLQNSQLPQ LFPDTRPGAP TGSVDKQAII
     NDLMQLTADS SPVPPAGAQK AALRMSQSTF NNPRPGQLGR LLPNQNLPLD ITLQSPTGAG
     PFPPIRNSSP YSVIPQPGMM GNQGMLGSQG NLGNNSTGMI GSSTSRPSMP SGEWAPQSPA
     VRVTCAATTG AMNRPVQGGM IRNPTASIPM RANSQPGQRQ MLQSQVMNIG PSELEMNMGG
     PQYNQQQAPP NQTAPWPESI LPIDQASFAS QNRQPFGSSP DDLLCPHPAA ESPSDEGALL
     DQLYLALRNF DGLEEIDRAL GIPELVSQSQ AVDAEQFSSQ ESSIMLEQKP PVFPQQYASQ
     AQMAQGGYNP MQDPNFHTMG QRPNYTTLRM QPRPGLRPTG IVQNQPNQLR LQLQHRLQAQ
     QNRQPLMNQI SSVSNVNLTL RPGVPTQAPI NAQMLAQRQR EILNQHLRQR QMQQQVQQRT
     LMMRGQGLNV TPSMVAPAGL PAAMSNPRIP QANAQQFPFP PNYGISQQPD PGFTGATTPQ
     SPLMSPRMAH TQSPMMQQSQ ANPAYQPTSD MNGWAQGSMG GNSMFSQQSP PHFGQQANTS
     MYSNNMNISV SMATNTGGLS SMNQMTCQMS MTSVTSVPTS GLPSMGPEQV NDPALRGGNL
     FPNQLPGMDM IKQEGDASRK YC
//
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   CNTN2_MOUSE             Reviewed;        1040 AA.
AC   Q61330; Q6NZJ4; Q7TSJ5;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 2.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Contactin-2;
DE   AltName: Full=Axonal glycoprotein TAG-1;
DE   AltName: Full=Axonin-1;
DE   AltName: Full=Transient axonal glycoprotein 1;
DE            Short=TAX-1;
DE   Flags: Precursor;
GN   Name=Cntn2; Synonyms=Tax;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; 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 664-881.
RC   STRAIN=ICR; TISSUE=Embryo;
RA   Wolfer D., Giger R.J.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in the initial growth and guidance of
CC       axons. May be involved in cell adhesion (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor (By
CC       similarity). Note=Attached to the neuronal membrane by a GPI-
CC       anchor and is also released from neurons (By similarity).
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.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC066106; AAH66106.1; -; mRNA.
DR   EMBL; BC053033; AAH53033.1; -; mRNA.
DR   EMBL; X81365; CAA57130.1; -; mRNA.
DR   IPI; IPI00119970; -.
DR   RefSeq; NP_796103.2; NM_177129.5.
DR   UniGene; Mm.480329; -.
DR   ProteinModelPortal; Q61330; -.
DR   SMR; Q61330; 36-1000.
DR   IntAct; Q61330; 2.
DR   STRING; Q61330; -.
DR   PRIDE; Q61330; -.
DR   Ensembl; ENSMUST00000086521; ENSMUSP00000083707; ENSMUSG00000053024.
DR   GeneID; 21367; -.
DR   KEGG; mmu:21367; -.
DR   UCSC; uc007cpa.1; mouse.
DR   CTD; 21367; -.
DR   MGI; MGI:104518; Cntn2.
DR   GeneTree; ENSGT00550000074380; -.
DR   HOGENOM; HBG444805; -.
DR   HOVERGEN; HBG051047; -.
DR   InParanoid; Q61330; -.
DR   OMA; ECFAFGN; -.
DR   OrthoDB; EOG490786; -.
DR   NextBio; 300578; -.
DR   ArrayExpress; Q61330; -.
DR   Bgee; Q61330; -.
DR   CleanEx; MM_CNTN2; -.
DR   Genevestigator; Q61330; -.
DR   GermOnline; ENSMUSG00000053024; Mus musculus.
DR   GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0044224; C:juxtaparanode region of axon; IDA:BHF-UCL.
DR   GO; GO:0043209; C:myelin sheath; IDA:BHF-UCL.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0033268; C:node of Ranvier; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IDA:MGI.
DR   GO; GO:0001948; F:glycoprotein binding; IDA:MGI.
DR   GO; GO:0043621; F:protein self-association; IPI:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0007411; P:axon guidance; IGI:MGI.
DR   GO; GO:0007413; P:axonal fasciculation; IMP:MGI.
DR   GO; GO:0022010; P:central nervous system myelination; IMP:MGI.
DR   GO; GO:0021853; P:cerebral cortex GABAergic interneuron migration; IMP:MGI.
DR   GO; GO:0045163; P:clustering of voltage-gated potassium channels; IMP:BHF-UCL.
DR   GO; GO:0071206; P:establishment of protein localization to juxtaparanode region of axon; IDA:BHF-UCL.
DR   GO; GO:0007612; P:learning; IMP:MGI.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IGI:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0060168; P:positive regulation of adenosine receptor signaling pathway; IMP:MGI.
DR   GO; GO:0010954; P:positive regulation of protein maturation by peptide bond cleavage; IDA:MGI.
DR   GO; GO:0031623; P:receptor internalization; IDA:MGI.
DR   GO; GO:0048710; P:regulation of astrocyte differentiation; IMP:MGI.
DR   GO; GO:0031133; P:regulation of axon diameter; IMP:MGI.
DR   GO; GO:0048168; P:regulation of neuronal synaptic plasticity; 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; 9.
DR   Pfam; PF00041; fn3; 3.
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; 4.
DR   PROSITE; PS50835; IG_LIKE; 6.
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     30       By similarity.
FT   CHAIN        31   1014       Contactin-2.
FT                                /FTId=PRO_0000014697.
FT   PROPEP     1015   1040       Removed in mature form (Potential).
FT                                /FTId=PRO_0000014698.
FT   DOMAIN       39    130       Ig-like C2-type 1.
FT   DOMAIN      135    224       Ig-like C2-type 2.
FT   DOMAIN      241    324       Ig-like C2-type 3.
FT   DOMAIN      329    413       Ig-like C2-type 4.
FT   DOMAIN      419    506       Ig-like C2-type 5.
FT   DOMAIN      511    605       Ig-like C2-type 6.
FT   DOMAIN      609    705       Fibronectin type-III 1.
FT   DOMAIN      712    809       Fibronectin type-III 2.
FT   DOMAIN      814    910       Fibronectin type-III 3.
FT   DOMAIN      914   1004       Fibronectin type-III 4.
FT   MOTIF       796    798       Cell attachment site (Potential).
FT   COMPBIAS    608    614       Gly/Pro-rich.
FT   LIPID      1014   1014       GPI-anchor amidated serine (Potential).
FT   CARBOHYD     78     78       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    200    200       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    206    206       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    463    463       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    479    479       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    500    500       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    527    527       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    777    777       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    832    832       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    920    920       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    942    942       N-linked (GlcNAc...) (Potential).
FT   DISULFID     63    113       By similarity.
FT   DISULFID    157    209       By similarity.
FT   DISULFID    263    308       By similarity.
FT   DISULFID    350    397       By similarity.
FT   CONFLICT    665    665       I -> M (in Ref. 2; CAA57130).
FT   CONFLICT    861    861       A -> R (in Ref. 2; CAA57130).
FT   CONFLICT    881    881       Y -> N (in Ref. 2; CAA57130).
SQ   SEQUENCE   1040 AA;  113217 MW;  012C05DDF7F97462 CRC64;
     MGAPARKRAS LLLLLLATMA LVSSPGWSFS QGTPATFGPV FEEQPVGLLF PEESAEDQVT
     LACRARASPP ATYRWKMNGT EMNLEPGSRH QLMGGNLVIM SPTKAQDAGV YQCLASNPVG
     TVVSKEAVLR FGFLQEFSKE ERDPVKTHEG WGVMLPCNPP AHYPGLSYRW LLNEFPNFIP
     TDGRHFVSQT TGNLYIARTN ASDLGNYSCL ATSHLDFSTK SVFSKFAQLN LAAEDPRLFA
     PSIKARFPPE TYALVGQQVT LECFAFGNPV PRIKWRKVDG SLSPQWGTAE PTLQIPSVSF
     EDEGTYECEA ENSKGRDTVQ GRIIVQAQPE WLKVISDTEA DIGSNLRWGC AAAGKPRPMV
     RWLRNGEPLA SQNRVEVLAG DLRFSKLNLE DSGMYQCVAE NKHGTIYASA ELAVQALAPD
     FRQNPVRRLI PAARGGEISI PCQPRAAPKA TILWSKGTEI LGNSTRVTVT LDGTLIIRNI
     SRSDEGKYTC FAENFMGKAN STGILSVRDA TKITLAPSSA DINVGDNLTL QCHASHDPTM
     DLTFTWTLDD FPVDFDKPGG HYRRASVKET IGDLTILNAQ LRHGGTYTCM AQTVVDGASK
     EATVLVRGPP GPPGGVVVRD IGDTTVQLSW SRGFDNHSPI AKYTLQARTP PSGKWKQVRT
     NPVNIEGNAE TAQVLGLMPW MDYEFRVSAS NILGTGEPSG PSSRIRTKEA VPSVAPSGLS
     GGGGAPGELT INWTPMSREY QNGDGFGYLL SFRRQGSSSW QTARVPGADT QYFVYSNDSI
     HPYTPFEVKI RSYNRRGDGP ESLTAIVYSA EEEPKVAPAK VWAKGSSSSE MNVSWEPVLQ
     DMNGILLGYE IRYWKAGDKE AAADRVRTAG LDSSARVTGL YPNTKYHVTV RAYNRAGTGP
     ASPSADAMTM KPPPRRPPGN ISWTFSSSSL SLKWDPVVPL RNESTVTGYK MLYQNDLQPT
     PMLHLTSKNW IEIPVPEDIG HALVQIRTTG PGGDGIPAEV HIVRNGGTSM MVESSAVRPA
     HPGPVFSCMV ILMLAGCQRL
//
ID   KCNA4_MOUSE             Reviewed;         654 AA.
AC   Q61423;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Potassium voltage-gated channel subfamily A member 4;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv1.4;
GN   Name=Kcna4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; 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=AKR;
RX   MEDLINE=94292198; PubMed=8020965; DOI=10.1006/geno.1994.1153;
RA   Wymore R.S., Korenberg J.R., Kinoshita K.D., Aiyar J., Coyne C.,
RA   Chen X.N., Hustad C.M., Copeland N.G., Gutman G.A., Jenkins N.A.,
RA   Chandy K.G.;
RT   "Genomic organization, nucleotide sequence, biophysical properties,
RT   and localization of the voltage-gated K+ channel gene KCNA4/Kv1.4 to
RT   mouse chromosome 2/human 11p14 and mapping of KCNC1/Kv3.1 to mouse
RT   7/human 11p14.3-p15.2 and KCNA1/Kv1.1 to human 12p13.";
RL   Genomics 20:191-202(1994).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
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. Binds PDZ
CC       domains of DLG1, DLG2 and DLG4. Interacts with SIGMAR1 (By
CC       similarity). Part of a complex containing KCNA1, KCNAB1 and LGI1
CC       (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. Kv1.4/KCNA4 sub-subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; U03723; AAB60668.1; -; Genomic_DNA.
DR   IPI; IPI00121102; -.
DR   PIR; S09045; S09045.
DR   UniGene; Mm.142718; -.
DR   ProteinModelPortal; Q61423; -.
DR   SMR; Q61423; 1-75, 176-572.
DR   MINT; MINT-1780501; -.
DR   STRING; Q61423; -.
DR   PhosphoSite; Q61423; -.
DR   PRIDE; Q61423; -.
DR   Ensembl; ENSMUST00000037012; ENSMUSP00000037958; ENSMUSG00000042604.
DR   Ensembl; ENSMUST00000111060; ENSMUSP00000106689; ENSMUSG00000042604.
DR   MGI; MGI:96661; Kcna4.
DR   eggNOG; roNOG09711; -.
DR   HOGENOM; HBG445693; -.
DR   HOVERGEN; HBG052230; -.
DR   InParanoid; Q61423; -.
DR   OrthoDB; EOG4QRH3T; -.
DR   ArrayExpress; Q61423; -.
DR   Bgee; Q61423; -.
DR   Genevestigator; Q61423; -.
DR   GermOnline; ENSMUSG00000042604; Mus musculus.
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   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    654       Potassium voltage-gated channel subfamily
FT                                A member 4.
FT                                /FTId=PRO_0000053982.
FT   TRANSMEM    309    327       Helical; Name=Segment S1; (Potential).
FT   TRANSMEM    372    393       Helical; Name=Segment S2; (Potential).
FT   TRANSMEM    405    425       Helical; Name=Segment S3; (Potential).
FT   TRANSMEM    444    462       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TRANSMEM    479    498       Helical; Name=Segment S5; (Potential).
FT   TRANSMEM    540    562       Helical; Name=Segment S6; (Potential).
FT   MOTIF       525    530       Selectivity filter (By similarity).
FT   MOTIF       652    654       PDZ-binding (By similarity).
FT   COMPBIAS     38     50       Poly-Ala.
FT   COMPBIAS     62     65       Poly-His.
FT   COMPBIAS     83     89       Poly-Arg.
FT   COMPBIAS    123    137       Poly-Glu.
FT   COMPBIAS    162    166       Poly-Gly.
FT   COMPBIAS    434    437       Poly-Gln.
FT   MOD_RES     122    122       Phosphoserine.
FT   MOD_RES     600    600       Phosphoserine; by PKA (Potential).
FT   CARBOHYD    182    182       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    353    353       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    643    643       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   654 AA;  73474 MW;  8693651A30BD36D4 CRC64;
     MEVAMVSAES SGCNSHMPYG YAAQARARER ERLAHSRAAA AAAVAAATAA VEGTGGSGGG
     PHHHHQTRGA YSSHDPQGSR GSRRRRRQRT EKKKLHHRQS SFPHCSDLMP SGSEEKILRE
     LSEEEEDEEE EEEEEEEGRF YYSEEDHGDG CSYTDLLPQE DGGGGGYSSV RYSDCCERVV
     INVSGLRFET QMKTLAQFPE TLLGDPEKRT QYFDPLRNEY FFDRNRPSFD AILYYYQSGG
     RLKRPVNVPF DIFTEEVKFY QLGEEALLKF REDEGFVREE EDRALPENEF KKQIWLLFEY
     PESSSPARGI AIVSVLVILI SIVIFCLETL PEFRDDRDLI MALSAGGHSR LLNDTSAPHL
     ENSGHTIFND PFFIVETVCI VWFSFEFVVR CFACTSQALF FKNIMNIIDI VSILPYFITL
     GTDLAQQQGG GNGQQQQAMS FAILRIIRLV RVFRIFKLSR HSKGLQILGH TLRASMRELG
     LLIFFLFIGV ILFSSAVYFA EADEPTTHFQ SIPDAFWWAV VTMTTVGYGD MKPITVGGKI
     VGSLCAIAGV LTIALPVPVI VSNFNYFYHR ETENEEQTQL TQNAVSCPYL PSNLLKKFRS
     STSSSLGDKS EYLEMEEGVK ESLCGKEEKC QGKGDDSETD KNNCSNAKAV ETDV
//
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.
CC   -----------------------------------------------------------------------
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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   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   -----------------------------------------------------------------------
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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   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.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
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   MAFK_MOUSE              Reviewed;         156 AA.
AC   Q61827; Q60600;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Transcription factor MafK;
DE   AltName: Full=Erythroid transcription factor NF-E2 p18 subunit;
GN   Name=Mafk; Synonyms=Nfe2u;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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=95221427; PubMed=7706310; DOI=10.1074/jbc.270.13.7615;
RA   Igarashi K., Itoh K., Motohashi H., Hayashi N., Matuzaki Y.,
RA   Nakauchi H., Nishizawa M., Yamamoto M.;
RT   "Activity and expression of murine small Maf family protein MafK.";
RL   J. Biol. Chem. 270:7615-7624(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=DBA; TISSUE=Hematopoietic;
RX   MEDLINE=94089658; PubMed=8265578; DOI=10.1073/pnas.90.24.11488;
RA   Andrews N.C., Kotkow K.J., Ney P.A., Erdjument-Bromage H., Tempst P.,
RA   Orkin S.H.;
RT   "The ubiquitous subunit of erythroid transcription factor NF-E2 is a
RT   small basic-leucine zipper protein related to the v-maf oncogene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:11488-11492(1993).
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).
CC   -!- FUNCTION: Since they lack a putative transactivation domain, the
CC       small Mafs behave as transcriptional repressors when they dimerize
CC       among themselves. However, they seem to serve as transcriptional
CC       activators by dimerizing with other (usually larger) basic-zipper
CC       proteins and recruiting them to specific DNA-binding sites. Small
CC       Maf proteins heterodimerize with Fos and may act as competitive
CC       repressors of the NF-E2 transcription factor.
CC   -!- SUBUNIT: Homodimer or heterodimer. It can form high affinity
CC       heterodimers with members of the CNC-bZIP family such as NFE2,
CC       NFE2L1/NRF1, NFE2L2/NRF2 and NFE2L3/NRF3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle and
CC       placenta. Also expressed in erythroid cells.
CC   -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily.
CC   -!- SIMILARITY: Contains 1 bZIP domain.
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DR   EMBL; D42124; BAA07704.1; -; mRNA.
DR   EMBL; U01036; AAC52132.1; -; mRNA.
DR   EMBL; BC014295; AAH14295.1; -; mRNA.
DR   IPI; IPI00126148; -.
DR   PIR; A49391; A49391.
DR   PIR; A56124; A56124.
DR   RefSeq; NP_034887.1; NM_010757.2.
DR   UniGene; Mm.157313; -.
DR   ProteinModelPortal; Q61827; -.
DR   SMR; Q61827; 24-111.
DR   DIP; DIP-46345N; -.
DR   STRING; Q61827; -.
DR   PhosphoSite; Q61827; -.
DR   PRIDE; Q61827; -.
DR   Ensembl; ENSMUST00000018287; ENSMUSP00000018287; ENSMUSG00000018143.
DR   Ensembl; ENSMUST00000110836; ENSMUSP00000106460; ENSMUSG00000018143.
DR   GeneID; 17135; -.
DR   KEGG; mmu:17135; -.
DR   UCSC; uc009ahd.1; mouse.
DR   CTD; 17135; -.
DR   MGI; MGI:99951; Mafk.
DR   GeneTree; ENSGT00550000074549; -.
DR   HOGENOM; HBG715194; -.
DR   HOVERGEN; HBG001725; -.
DR   InParanoid; Q61827; -.
DR   OMA; RGPVTPT; -.
DR   OrthoDB; EOG4X3H2R; -.
DR   PhylomeDB; Q61827; -.
DR   NextBio; 291344; -.
DR   ArrayExpress; Q61827; -.
DR   Bgee; Q61827; -.
DR   Genevestigator; Q61827; -.
DR   GermOnline; ENSMUSG00000018143; Mus musculus.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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; IDA:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IDA:MGI.
DR   InterPro; IPR008917; Euk_TF_DNA-bd.
DR   InterPro; IPR004827; TF_bZIP.
DR   InterPro; IPR004826; TF_Maf.
DR   Pfam; PF03131; bZIP_Maf; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF47454; Euk_transcr_DNA; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   DNA-binding; Nucleus; Phosphoprotein; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    156       Transcription factor MafK.
FT                                /FTId=PRO_0000076504.
FT   DOMAIN       86    114       Leucine-zipper.
FT   DNA_BIND     51     76       Basic motif.
FT   MOD_RES      25     25       Phosphoserine (By similarity).
FT   CONFLICT     36     37       EL -> DV (in Ref. 2; AAC52132).
SQ   SEQUENCE   156 AA;  17537 MW;  39F98F8A257F46CB CRC64;
     MTTNPKPNKA LKVKKEAGEN APVLSDDELV SMSVRELNQH LRGLTKEEVT RLKQRRRTLK
     NRGYAASCRI KRVTQKEELE RQRVELQQEV EKLARENSSM RLELDALRSK YEALQTFART
     VARGPVTPTK VATTSVITIV KSAELSSTSV PFSAAS
//
ID   M3K7_MOUSE              Reviewed;         579 AA.
AC   Q62073;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 101.
DE   RecName: Full=Mitogen-activated protein kinase kinase kinase 7;
DE            EC=2.7.11.25;
DE   AltName: Full=Transforming growth factor-beta-activated kinase 1;
DE            Short=TGF-beta-activated kinase 1;
GN   Name=Map3k7; Synonyms=Tak1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=96123277; PubMed=8533096; DOI=10.1126/science.270.5244.2008;
RA   Yamaguchi K., Shirakabe K., Shibuya H., Irie K., Ohishi I., Ueno N.,
RA   Taniguchi T., Nishida E., Matsumoto K.;
RT   "Identification of a member of the MAPKKK family as a potential
RT   mediator of TGF-beta signal transduction.";
RL   Science 270:2008-2011(1995).
RN   [2]
RP   INTERACTION WITH PPM1L.
RX   MEDLINE=22552457; PubMed=12556533; DOI=10.1074/jbc.M211474200;
RA   Li M.G., Katsura K., Nomiyama H., Komaki K., Ninomiya-Tsuji J.,
RA   Matsumoto K., Kobayashi T., Tamura S.;
RT   "Regulation of the interleukin-1-induced signaling pathways by a novel
RT   member of the protein phosphatase 2C family (PP2Cepsilon).";
RL   J. Biol. Chem. 278:12013-12021(2003).
RN   [3]
RP   FUNCTION, UBIQUITINATION, AND PROTEASOMAL DEGRADATION.
RX   PubMed=16157589; DOI=10.1074/jbc.M505671200;
RA   Kaur S., Wang F., Venkatraman M., Arsura M.;
RT   "X-linked inhibitor of apoptosis (XIAP) inhibits c-Jun N-terminal
RT   kinase 1 (JNK1) activation by transforming growth factor beta1 (TGF-
RT   beta1) through ubiquitin-mediated proteosomal degradation of the TGF-
RT   beta1-activated kinase 1 (TAK1).";
RL   J. Biol. Chem. 280:38599-38608(2005).
RN   [4]
RP   UBIQUITINATION, INTERACTION WITH CYLD, AND DEUBIQUITINATION BY CYLD.
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
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-412, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., 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-389 AND SER-412, 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 a protein kinase signal transduction
CC       cascade. Mediator of TRAF6 and TGF-beta signal transduction.
CC       Activates IKBKB and MAPK8 in response to TRAF6 signaling.
CC       Stimulates NF-kappa-B activation and the p38 MAPK pathway. In
CC       osmotic stress signaling, plays a major role in the activation of
CC       MAPK8/JNK, but not that of NF-kappa-B.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activated by 'Lys-63'-linked
CC       polyubiquitination. Activated by proinflammatory cytokines and in
CC       response to physical and chemical stresses, including osmotic
CC       stress, oxidative stress, arsenic and ultraviolet light
CC       irradiation (By similarity).
CC   -!- SUBUNIT: Binds both upstream activators and downstream substrates
CC       in multimolecular complexes. Interacts with TAB1/MAP3K7IP1 and
CC       TAB2/MAP3K7IP2. Identified in the TRIKA2 complex composed of
CC       MAP3K7, TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2. Interacts with PPM1L.
CC       Interaction with PP2A and PPP6C leads to its repressed activity.
CC       Interacts with TRAF6 and TAB1/MAP3K7IP1; during IL-1 signaling.
CC       Interacts with TAOK1 and TAOK2; interaction with TAOK2 interferEs
CC       with MAP3K7 interaction with IKKA, thus preventing NF-kappa-B
CC       activation. Interacts with WDR34 (via WD domains). Interacts with
CC       RBCK1 (By similarity). Interacts with CYLD.
CC   -!- INTERACTION:
CC       Q99K90:Map3k7ip2; NbExp=4; IntAct=EBI-1775345, EBI-1775124;
CC       Q9WVI9-2:Mapk8ip1; NbExp=1; IntAct=EBI-1775345, EBI-288464;
CC       Q8CF89:Tab1; NbExp=1; IntAct=EBI-1775345, EBI-1778503;
CC       Q9NYJ8:TAB2 (xeno); NbExp=1; IntAct=EBI-1775345, EBI-358708;
CC       Q8N5C8:TAB3 (xeno); NbExp=1; IntAct=EBI-1775345, EBI-359964;
CC       Q86Y07-1:VRK2 (xeno); NbExp=2; IntAct=EBI-1775345, EBI-1207633;
CC   -!- PTM: Association with TAB1/MAP3K7IP1 promotes autophosphorylation
CC       and subsequent activation. Association with TAB2/MAP3K7IP2, itself
CC       associated with free unanchored Lys-63 polyubiquitin chain,
CC       promotes autophosphorylation and subsequent activation of MAP3K7.
CC       Dephosphorylation at Thr-187 by PP2A and PPP6C leads to
CC       inactivation (By similarity).
CC   -!- PTM: Ubiquitinated, leading to proteasomal degradation. Requires
CC       'Lys-63'-linked polyubiquitination for autophosphorylation and
CC       subsequent activation. 'Lys-63'-linked ubiquitination does not
CC       lead to proteasomal degradation. Deubiquitinated by CYLD, a
CC       protease that selectively cleaves 'Lys-63'-linked ubiquitin
CC       chains.
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; D76446; BAA11184.1; -; mRNA.
DR   IPI; IPI00121080; -.
DR   RefSeq; NP_766276.1; NM_172688.3.
DR   UniGene; Mm.258589; -.
DR   ProteinModelPortal; Q62073; -.
DR   SMR; Q62073; 31-305.
DR   IntAct; Q62073; 16.
DR   STRING; Q62073; -.
DR   PhosphoSite; Q62073; -.
DR   PRIDE; Q62073; -.
DR   Ensembl; ENSMUST00000080933; ENSMUSP00000079734; ENSMUSG00000028284.
DR   GeneID; 26409; -.
DR   KEGG; mmu:26409; -.
DR   UCSC; uc008sep.1; mouse.
DR   CTD; 26409; -.
DR   MGI; MGI:1346877; Map3k7.
DR   GeneTree; ENSGT00600000084194; -.
DR   HOVERGEN; HBG003485; -.
DR   BRENDA; 2.7.11.25; 244.
DR   NextBio; 304393; -.
DR   ArrayExpress; Q62073; -.
DR   Bgee; Q62073; -.
DR   CleanEx; MM_MAP3K7; -.
DR   Genevestigator; Q62073; -.
DR   GermOnline; ENSMUSG00000028284; 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:0004708; F:MAP kinase kinase activity; IDA:MGI.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR   GO; GO:0007252; P:I-kappaB phosphorylation; ISS:UniProtKB.
DR   GO; GO:0000165; P:MAPKKK cascade; IDA:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IGI:MGI.
DR   GO; GO:0001841; P:neural tube formation; IMP:MGI.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IGI:MGI.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; IGI:MGI.
DR   GO; GO:0043507; P:positive regulation of JUN kinase activity; ISS:UniProtKB.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR017421; MAPKKK7.
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   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PIRSF; PIRSF038168; MAPKKK7; 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; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase;
KW   Ubl conjugation.
FT   CHAIN         1    579       Mitogen-activated protein kinase kinase
FT                                kinase 7.
FT                                /FTId=PRO_0000086253.
FT   DOMAIN       36    291       Protein kinase.
FT   NP_BIND      42     50       ATP (By similarity).
FT   COMPBIAS      8     16       Poly-Ser.
FT   ACT_SITE    156    156       Proton acceptor (By similarity).
FT   BINDING      63     63       ATP (By similarity).
FT   MOD_RES     184    184       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     187    187       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     192    192       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     389    389       Phosphoserine.
FT   MOD_RES     412    412       Phosphoserine.
FT   MOD_RES     417    417       Phosphothreonine (By similarity).
FT   MOD_RES     428    428       Phosphoserine (By similarity).
SQ   SEQUENCE   579 AA;  64228 MW;  97C8F6F3C8E283EE CRC64;
     MSTASAASSS SSSSASEMIE APSQVLNFEE IDYKEIEVEE VVGRGAFGVV CKAKWRAKDV
     AIKQIESESE RKAFIVELRQ LSRVNHPNIV KLYGACLNPV CLVMEYAEGG SLYNVLHGAE
     PLPYYTAAHA MSWCLQCSQG VAYLHSMQPK ALIHRDLKPP NLLLVAGGTV LKICDFGTAC
     DIQTHMTNNK GSAAWMAPEV FEGSNYSEKC DVFSWGIILW EVITRRKPFD EIGGPAFRIM
     WAVHNGTRPP LIKNLPKPIE SLMTRCWSKD PSQRPSMEEI VKIMTHLMRY FPGADEPLQY
     PCQYSDEGQS NSATSTGSFM DIASTNTSNK SDTNMEQVPA TNDTIKRLES KLLKNQAKQQ
     SESGRLSLGA SRGSSVESLP PTSEGKRMSA DMSEIEARIV ATAGNGQPRR RSIQDLTVTG
     TEPGQVSSRS SSPSVRMITT SGPTSEKPAR SHPWTPDDST DTNGSDNSIP MAYLTLDHQL
     QPLAPCPNSK ESMAVFEQHC KMAQEYMKVQ TEIALLLQRK QELVAELDQD EKDQQNTSRL
     VQEHKKLLDE NKSLSTYYQQ CKKQLEVIRS QQQKRQGTS
//
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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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   SEM4B_MOUSE             Reviewed;         823 AA.
AC   Q62179; Q4PKI6; Q69ZB7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Semaphorin-4B;
DE   AltName: Full=Semaphorin-C;
DE            Short=Sema C;
DE   Flags: Precursor;
GN   Name=Sema4b; Synonyms=Kiaa1745, Semac, SemC;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=NZW/LacJ; TISSUE=Thymus;
RA   Duke-Cohan J.S.;
RT   "Re-examination of 5' end of mouse semaphorin 4B (Sema4B).";
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 42-823.
RC   STRAIN=NMRI; TISSUE=Brain;
RX   MEDLINE=95267431; PubMed=7748561; DOI=10.1016/0896-6273(95)90332-1;
RA   Pueschel A.W., Adams R.H., Betz H.;
RT   "Murine semaphorin D/collapsin is a member of a diverse gene family
RT   and creates domains inhibitory for axonal extension.";
RL   Neuron 14:941-948(1995).
RN   [4]
RP   INTERACTION WITH GIPC.
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-780, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., 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-397, 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: Inhibits axonal extension by providing local signals to
CC       specify territories inaccessible for growing axons.
CC   -!- SUBUNIT: Interacts with GIPC PDZ domain.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- DEVELOPMENTAL STAGE: Expressed from day 10 in the embryo. Low
CC       levels found between days 10-12. Expression peaks on day 13 with
CC       moderate levels from then until birth.
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32527.1; 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; DQ073331; AAY82464.1; -; mRNA.
DR   EMBL; AK173249; BAD32527.1; ALT_INIT; mRNA.
DR   EMBL; X85992; CAA59984.1; -; mRNA.
DR   IPI; IPI00464135; -.
DR   PIR; I48746; I48746.
DR   RefSeq; NP_038687.2; NM_013659.4.
DR   UniGene; Mm.275909; -.
DR   ProteinModelPortal; Q62179; -.
DR   SMR; Q62179; 29-661.
DR   IntAct; Q62179; 2.
DR   MINT; MINT-1350466; -.
DR   STRING; Q62179; -.
DR   PhosphoSite; Q62179; -.
DR   PRIDE; Q62179; -.
DR   Ensembl; ENSMUST00000032754; ENSMUSP00000032754; ENSMUSG00000030539.
DR   GeneID; 20352; -.
DR   KEGG; mmu:20352; -.
DR   UCSC; uc009hzp.1; mouse.
DR   CTD; 20352; -.
DR   MGI; MGI:107559; Sema4b.
DR   eggNOG; roNOG10257; -.
DR   HOGENOM; HBG717343; -.
DR   HOVERGEN; HBG061165; -.
DR   InParanoid; Q62179; -.
DR   OMA; CVFTMKD; -.
DR   OrthoDB; EOG4CNQQF; -.
DR   PhylomeDB; Q62179; -.
DR   NextBio; 298211; -.
DR   ArrayExpress; Q62179; -.
DR   Bgee; Q62179; -.
DR   Genevestigator; Q62179; -.
DR   GermOnline; ENSMUSG00000030539; 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: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   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     30       Potential.
FT   CHAIN        31    823       Semaphorin-4B.
FT                                /FTId=PRO_0000042162.
FT   TOPO_DOM     31    703       Extracellular (Potential).
FT   TRANSMEM    704    724       Helical; (Potential).
FT   TOPO_DOM    725    823       Cytoplasmic (Potential).
FT   DOMAIN       34    510       Sema.
FT   DOMAIN      512    582       PSI.
FT   DOMAIN      589    649       Ig-like C2-type.
FT   COMPBIAS    744    767       Pro-rich.
FT   MOD_RES     780    780       Phosphoserine.
FT   MOD_RES     804    804       Phosphoserine (By similarity).
FT   MOD_RES     816    816       Phosphoserine (By similarity).
FT   CARBOHYD     53     53       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     56     56       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     83     83       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    129    129       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    397    397       N-linked (GlcNAc...).
FT   CARBOHYD    512    512       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    567    567       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    615    615       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    680    680       N-linked (GlcNAc...) (Potential).
FT   DISULFID    107    118       By similarity.
FT   DISULFID    136    145       By similarity.
FT   DISULFID    273    386       By similarity.
FT   DISULFID    297    346       By similarity.
FT   DISULFID    596    642       By similarity.
FT   CONFLICT    171    171       R -> H (in Ref. 3; CAA59984).
FT   CONFLICT    232    233       YV -> TS (in Ref. 3; CAA59984).
FT   CONFLICT    246    246       K -> R (in Ref. 1; AAY82464).
FT   CONFLICT    327    328       FY -> SI (in Ref. 3; CAA59984).
FT   CONFLICT    544    544       Q -> K (in Ref. 1; AAY82464).
FT   CONFLICT    692    692       A -> D (in Ref. 3; CAA59984).
FT   CONFLICT    722    722       F -> L (in Ref. 1; AAY82464).
FT   CONFLICT    760    760       G -> C (in Ref. 1; AAY82464).
SQ   SEQUENCE   823 AA;  91392 MW;  051589B4DFAE9883 CRC64;
     MGRASRSAVL RRALLLLLLL LLLRTTTTRA LGPRISVPLG SEERLIRKFE AENISNYTAL
     LLSQDGKTLY VGAREALFAL NSNLSFLPGG EYQELLWSAD ADRKQQCSFK GKDPKRDCQN
     YIKILLPLNS SHLLTCGTAA FSPLCAYIHI ASFTLAQDEA GNVILEDGKG RCPFDPNFKS
     TALVVDGELY TGTVSSFQGN DPAISRSQSS RPTKTESSLN WLQDPAFVAS AYVPESLGSP
     IGDDDKIYFF FSETGQEFEF FENTIVSRVA RVCKGDEGGE RVLQQRWTSF LKAQLLCSRP
     DDGFPFNVLQ DVFTLNPNPQ DWRKTLFYGV FTSQWHRGTT EGSAICVFTM NDVQKAFDGL
     YKKVNRETQQ WYTETHQVPT PRPGACITNS ARERKINSSL QLPDRVLNFL KDHFLMDGQV
     RSRLLLLQPR ARYQRVAVHR VPGLHSTYDV LFLGTGDGRL HKAVTLSSRV HIIEELQIFP
     QGQPVQNLLL DSHGGLLYAS SHSGVVQVPV ANCSLYPTCG DCLLARDPYC AWTGSACRLA
     SLYQPDLASR PWTQDIEGAS VKELCKNSSY KARFLVPGKP CKQVQIQPNT VNTLACPLLS
     NLATRLWVHN GAPVNASASC RVLPTGDLLL VGSQQGLGVF QCWSIEEGFQ QLVASYCPEV
     MEEGVMDQKN QRDGTPVIIN TSRVSAPAGG RASWGADKSY WNEFLVMCTL FVFAMVLLFL
     FFLYRHRDGM KLFLKQGECA SVHPKTRPIV LPPETRPLNG VGPPSTPLDH RGYQALSDSS
     PGPRVFTESE KRPLSIQDSF VEVSPVCPRP RVRLGSEIRD SVV
//
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   TAF6_MOUSE              Reviewed;         678 AA.
AC   Q62311;
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=Transcription initiation factor TFIID subunit 6;
DE   AltName: Full=Transcription initiation factor TFIID 70 kDa subunit;
DE            Short=TAF(II)70;
DE            Short=TAFII-70;
DE            Short=TAFII70;
DE   AltName: Full=Transcription initiation factor TFIID 80 kDa subunit;
DE            Short=TAF(II)80;
DE            Short=TAFII-80;
DE            Short=TAFII80;
DE   AltName: Full=p80;
GN   Name=Taf6; Synonyms=Taf2e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=95394377; PubMed=7665100; DOI=10.1016/0378-1119(95)00285-E;
RA   Umehara T., Kida S., Horikoshi M.;
RT   "Isolation of a cDNA encoding a mouse TFIID subunit containing histone
RT   H4 homology.";
RL   Gene 161:301-302(1995).
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: TAFs are components of the transcription factor IID
CC       (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII
CC       complex (TFTC). TIIFD is multimeric protein complex that plays a
CC       central role in mediating promoter responses to various activators
CC       and repressors (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, TAF1/TAFII250, TAF9/TAFII31 AND
CC       TAF12/TAFII20. The TAF6/TAFII70-TAF9/TAFII31 heterodimer forms an
CC       octamer complex with the TAF4B/TFII105-TAF12/TFIID20 heterodimer.
CC       Also interacts with the GTFs, TFIIEalpha/GTF2E1 and
CC       TFIIFalpha/GTF2F1. Component of the TFTC-HAT complex. 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 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the TAF6 family.
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DR   EMBL; D49439; BAA08417.1; -; mRNA.
DR   EMBL; BC058583; AAH58583.1; -; mRNA.
DR   IPI; IPI00124566; -.
DR   PIR; JC4245; JC4245.
DR   RefSeq; NP_033341.1; NM_009315.3.
DR   UniGene; Mm.248517; -.
DR   ProteinModelPortal; Q62311; -.
DR   SMR; Q62311; 9-76.
DR   DIP; DIP-493N; -.
DR   MINT; MINT-269059; -.
DR   STRING; Q62311; -.
DR   PhosphoSite; Q62311; -.
DR   PRIDE; Q62311; -.
DR   Ensembl; ENSMUST00000048698; ENSMUSP00000048016; ENSMUSG00000036980.
DR   Ensembl; ENSMUST00000110936; ENSMUSP00000106561; ENSMUSG00000036980.
DR   GeneID; 21343; -.
DR   KEGG; mmu:21343; -.
DR   NMPDR; fig|10090.3.peg.12664; -.
DR   UCSC; uc009aew.1; mouse.
DR   CTD; 21343; -.
DR   MGI; MGI:109129; Taf6.
DR   eggNOG; roNOG14545; -.
DR   GeneTree; ENSGT00530000063704; -.
DR   HOGENOM; HBG506890; -.
DR   HOVERGEN; HBG012489; -.
DR   InParanoid; Q62311; -.
DR   OMA; SCEAKRA; -.
DR   OrthoDB; EOG4MKNG0; -.
DR   PhylomeDB; Q62311; -.
DR   NextBio; 300524; -.
DR   ArrayExpress; Q62311; -.
DR   Bgee; Q62311; -.
DR   Genevestigator; Q62311; -.
DR   GermOnline; ENSMUSG00000036980; Mus musculus.
DR   GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0003702; F:RNA polymerase II transcription factor activity; IEA:InterPro.
DR   GO; GO:0051090; P:regulation of transcription factor activity; IEA:InterPro.
DR   GO; GO:0006352; P:transcription initiation, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR011442; DUF1546.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR004823; TAF_TATA-bd.
DR   Gene3D; G3DSA:1.10.20.10; Histone-fold; 1.
DR   Pfam; PF07571; DUF1546; 1.
DR   Pfam; PF02969; TAF; 1.
DR   SMART; SM00803; TAF; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
PE   2: Evidence at transcript level;
KW   Nucleus; Phosphoprotein; Transcription; Transcription regulation.
FT   CHAIN         1    678       Transcription initiation factor TFIID
FT                                subunit 6.
FT                                /FTId=PRO_0000118874.
FT   MOD_RES     626    626       Phosphoserine (By similarity).
FT   MOD_RES     634    634       Phosphoserine (By similarity).
FT   MOD_RES     636    636       Phosphoserine (By similarity).
FT   MOD_RES     653    653       Phosphoserine (By similarity).
FT   MOD_RES     660    660       Phosphothreonine (By similarity).
FT   MOD_RES     673    673       Phosphoserine (By similarity).
SQ   SEQUENCE   678 AA;  72673 MW;  2F454DA3A29B410D CRC64;
     MAEEKKLKLS NTVLPSESMK VVAESMGIAQ IQEETCQLLT DEVSYRIKEI AQDALKFMHM
     GKRQKLTTSD IDYALKLKNV EPLYGFHAQE FIPFRFASGG GRELYFYEEK EVDLSDIINT
     PLPRVPLDVC LKAHWLSIEG CQPAIPENPP PAPKEQQKAE ATEPLKSAKP GQEEDGPLKG
     KGQGAAAADG KGKEKKAPPL LEGAPFRLKP RSIHELSVEQ QLYYKEITEA CVGSCEAKRA
     EALQSIATDP GLYQMLPRFS TFISEGVRVN VVQNNLALLI YLMRMVKALM DNPTLYLEKY
     VHELIPAVMT CIVSRQLCLR PDVDNHWALR DFAARLVAQI CKHFSTTTNN IQSRITKTFT
     KSWVDEKTPW TTRYGSIAGL AELGHDVIKT LILPRLQQEG ERIRSVLDGP VLSNIDRIGA
     DHVQSLLLKH CAPVLAKLRP PPDNQDAYRG EFGSLGPLLC SHVVKARAQA ALQAQQVNRT
     TLTITQPRPT LTLSQAPQPG PRTPGLLKVP GSIALPVQTL VSARAAAPPQ PSPPPTKFIV
     MSSSSSASST QQVLSLSTSA PGSGSTTTSP VTTTVPSVQP IVKLVSTATT APPSTAPAGS
     GSVQKYIVVS LPPTGEGKGG PPSHPSPVPP SSSSPSPLGG STLCGGKQEA GDSPPPAPGT
     PKANGSQPTG PGSPQPAL
//
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;
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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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   SH3G1_MOUSE             Reviewed;         368 AA.
AC   Q62419;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Endophilin-A2;
DE   AltName: Full=Endophilin-2;
DE   AltName: Full=SH3 domain protein 2B;
DE   AltName: Full=SH3 domain-containing GRB2-like protein 1;
DE   AltName: Full=SH3p8;
GN   Name=Sh3gl1; Synonyms=Sh3d2b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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   PROTEIN SEQUENCE OF 228-239, 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-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).
CC   -!- FUNCTION: Implicated in endocytosis. May recruit other proteins to
CC       membranes with high curvature (By similarity).
CC   -!- SUBUNIT: Interacts with ARC, SYNJ1 and DNM1. Interacts with
CC       PDCD6IP (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 neurons
CC       (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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DR   EMBL; U58885; AAC71775.1; -; mRNA.
DR   IPI; IPI00312752; -.
DR   RefSeq; NP_038692.1; NM_013664.2.
DR   UniGene; Mm.1773; -.
DR   ProteinModelPortal; Q62419; -.
DR   SMR; Q62419; 30-252, 305-368.
DR   IntAct; Q62419; 4.
DR   MINT; MINT-238674; -.
DR   STRING; Q62419; -.
DR   PhosphoSite; Q62419; -.
DR   PRIDE; Q62419; -.
DR   Ensembl; ENSMUST00000003268; ENSMUSP00000003268; ENSMUSG00000003200.
DR   GeneID; 20405; -.
DR   KEGG; mmu:20405; -.
DR   UCSC; uc008daq.1; mouse.
DR   CTD; 20405; -.
DR   MGI; MGI:700010; Sh3gl1.
DR   GeneTree; ENSGT00550000074464; -.
DR   HOGENOM; HBG447412; -.
DR   HOVERGEN; HBG052866; -.
DR   InParanoid; Q62419; -.
DR   OMA; IRGQVKN; -.
DR   OrthoDB; EOG4C2H9V; -.
DR   PhylomeDB; Q62419; -.
DR   NextBio; 298376; -.
DR   ArrayExpress; Q62419; -.
DR   Bgee; Q62419; -.
DR   CleanEx; MM_SH3GL1; -.
DR   Genevestigator; Q62419; -.
DR   GermOnline; ENSMUSG00000003200; 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; IPR001452; SH3_domain.
DR   Pfam; PF03114; BAR; 1.
DR   Pfam; PF00018; SH3_1; 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   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Direct protein sequencing; Endocytosis;
KW   Endosome; Lipid-binding; Membrane; Phosphoprotein; SH3 domain.
FT   CHAIN         1    368       Endophilin-A2.
FT                                /FTId=PRO_0000146745.
FT   DOMAIN       18    249       BAR.
FT   DOMAIN      306    365       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    250       Potential.
FT   MOD_RES     287    287       Phosphoserine (By similarity).
FT   MOD_RES     288    288       Phosphoserine.
SQ   SEQUENCE   368 AA;  41518 MW;  3F753B1669086353 CRC64;
     MSVAGLKKQF YKASQLVSEK VGGAEGTKLD DDFKDMEKKV DVTSKAVAEV LVRTIEYLQP
     NPASRAKLTM LNTVSKIRGQ VKNPGYPQSE GLLGECMVRH GKELGGESNF GDALLDAGES
     MKRLAEVKDS LDIEVKQNFI DPLQNLCDKD LKEIQHHLKK LEGRRLDFDY KKKRQGKIPD
     EELRQALEKF EESKEVAETS MHNLLETDIE QVSQLSALVD AQLDYHRQAV QILEELADKL
     KRRVREASSR PKREFKPRPR EPFELGELEQ PNGGFPCAPA PKITASSSFR SSDKPIRMPS
     KSMPPLDQPS CKALYDFEPE NDGELGFREG DLITLTNQID ENWYEGMLHG QSGFFPLSYV
     QVLVPLPQ
//
ID   TLE4_MOUSE              Reviewed;         773 AA.
AC   Q62441; Q9JKQ9;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 4.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Transducin-like enhancer protein 4;
DE   AltName: Full=Grg-4;
DE   AltName: Full=Groucho-related protein 4;
GN   Name=Tle4; Synonyms=Grg4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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   PAX5.
RC   TISSUE=Embryo;
RX   MEDLINE=20271869; PubMed=10811620; DOI=10.1093/emboj/19.10.2292;
RA   Eberhard D., Jimenez G., Heavey B., Busslinger M.;
RT   "Transcriptional repression by Pax5 (BSAP) through interaction with
RT   corepressors of the Groucho family.";
RL   EMBO J. 19:2292-2303(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 197-773.
RX   MEDLINE=97047314; PubMed=8892234; DOI=10.1016/0925-4773(96)00582-5;
RA   Koop K.E., Macdonald L.M., Lobe C.G.;
RT   "Transcripts of Grg4, a murine groucho-related gene, are detected in
RT   adjacent tissues to other murine neurogenic gene homologues during
RT   embryonic development.";
RL   Mech. Dev. 59:73-87(1996).
RN   [3]
RP   SEQUENCE REVISION.
RA   Lobe C.G., Koop K.E., Macdonald L.M.;
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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).
CC   -!- FUNCTION: Transcriptional corepressor that binds to a number of
CC       transcription factors. Inhibits the transcriptional activation
CC       mediated by PAX5, and by CTNNB1 and TCF family members in Wnt
CC       signaling. The effects of full-length TLE family members may be
CC       modulated by association with dominant-negative AES (By
CC       similarity).
CC   -!- SUBUNIT: Homooligomer and heterooligomer with other family members
CC       (By similarity). Binds PAX5, LEF1, TCF7, TCF7L1 and TCF7L2.
CC   -!- INTERACTION:
CC       Q95RW8:Optix (xeno); NbExp=1; IntAct=EBI-2297871, EBI-2297912;
CC       Q62233:Six3; NbExp=2; IntAct=EBI-2297871, EBI-2297327;
CC       Q9QZ28:Six6; NbExp=1; IntAct=EBI-2297871, EBI-348987;
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- PTM: Phosphorylated. PAX5 binding increases phosphorylation.
CC   -!- SIMILARITY: Belongs to the WD repeat Groucho/TLE family.
CC   -!- SIMILARITY: Contains 7 WD repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF43203.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; AF229633; AAF43203.1; ALT_INIT; mRNA.
DR   EMBL; U61363; AAC97070.1; -; mRNA.
DR   IPI; IPI00407702; -.
DR   RefSeq; NP_035730.2; NM_011600.2.
DR   UniGene; Mm.103638; -.
DR   ProteinModelPortal; Q62441; -.
DR   SMR; Q62441; 441-773.
DR   IntAct; Q62441; 4.
DR   STRING; Q62441; -.
DR   PhosphoSite; Q62441; -.
DR   PRIDE; Q62441; -.
DR   Ensembl; ENSMUST00000052011; ENSMUSP00000057527; ENSMUSG00000024642.
DR   GeneID; 21888; -.
DR   KEGG; mmu:21888; -.
DR   UCSC; uc008gwk.1; mouse.
DR   CTD; 21888; -.
DR   MGI; MGI:104633; Tle4.
DR   HOVERGEN; HBG004689; -.
DR   InParanoid; Q62441; -.
DR   OrthoDB; EOG4MGS6V; -.
DR   NextBio; 301416; -.
DR   ArrayExpress; Q62441; -.
DR   Bgee; Q62441; -.
DR   Genevestigator; Q62441; -.
DR   GermOnline; ENSMUSG00000024642; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IC:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003705; F:sequence-specific enhancer binding RNA polymerase II transcription factor activity; IGI:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IDA:MGI.
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; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Nucleus; Phosphoprotein; Repeat; Repressor;
KW   Transcription; Transcription regulation; WD repeat;
KW   Wnt signaling pathway.
FT   CHAIN         1    773       Transducin-like enhancer protein 4.
FT                                /FTId=PRO_0000051284.
FT   REPEAT      485    523       WD 1.
FT   REPEAT      531    570       WD 2.
FT   REPEAT      575    614       WD 3.
FT   REPEAT      617    656       WD 4.
FT   REPEAT      658    697       WD 5.
FT   REPEAT      699    738       WD 6.
FT   REPEAT      740    773       WD 7.
FT   REGION      207    274       CCN domain.
FT   COMPBIAS      1    137       Gln-rich (Q domain).
FT   COMPBIAS    138    205       Gly/Pro-rich (GP domain).
FT   MOD_RES     206    206       Phosphoserine (By similarity).
FT   MOD_RES     208    208       Phosphoserine (By similarity).
FT   MOD_RES     237    237       N6-acetyllysine (By similarity).
FT   MOD_RES     243    243       Phosphotyrosine (By similarity).
FT   MOD_RES     245    245       Phosphoserine (By similarity).
FT   MOD_RES     250    250       Phosphoserine; by CK2 (Potential).
FT   MOD_RES     265    265       Phosphoserine; by CDK1 (Potential).
FT   MOD_RES     281    281       N6-acetyllysine (By similarity).
FT   MOD_RES     292    292       Phosphoserine (By similarity).
FT   MOD_RES     305    305       Phosphoserine (By similarity).
FT   CONFLICT    197    199       RDR -> QTN (in Ref. 2; AAC97070).
FT   CONFLICT    405    405       A -> R (in Ref. 2; AAC97070).
FT   CONFLICT    454    455       SA -> RS (in Ref. 2; AAC97070).
FT   CONFLICT    608    609       NQ -> KE (in Ref. 2; AAC97070).
SQ   SEQUENCE   773 AA;  83787 MW;  5A0090789774CACC CRC64;
     MIRDLSKMYP QTRHPAPHQP AQPFKFTISE SCDRIKEEFQ FLQAQYHSLK LECEKLASEK
     TEMQRHYVMY YEMSYGLNIE MHKQAEIVKR LNAICAQVIP FLSQEHQQQV VQAVERAKQV
     TMAELNAIIG QQLQAQHLSH GHGLPVPLTP HPSGLQPPAI PPIGSSAGLL ALSSALGGQS
     HLPIKDEKKH HDNDHQRDRD SIKSSSVSPS ASFRGSEKHR NSTDYSSESK KQKTEEKEIA
     ARYDSDGEKS DDNLVVDVSN EDPSSPRGSP AHSPRENGLD KTRLLKKDAP ISPASVASSS
     STPSSKSKEL SLNEKSTTPV SKSNTPTPRT DAPTPGSNST PGLRPVPGKP PGVDPLASSL
     RTPMAVPCPY PTPFGIVPHA GMNGELTSPG AAYAGLHNIS PQMSAAAAAA AAAAAYGRSP
     VVGFDPHHHM RVPAIPPNLT GIPGGKPAYS FHVSADGQMQ PVPFPPDALI GPGIPRHARQ
     INTLNHGEVV CAVTISNPTR HVYTGGKGCV KVWDISHPGN KSPVSQLDCL NRDNYIRSCR
     LLPDGRTLIV GGEASTLSIW DLAAPTPRIK AELTSSAPAC YALAISPDSK VCFSCCSDGN
     IAVWDLHNQT LVRQFQGHTD GASCIDISND GTKLWTGGLD NTVRSWDLRE GRQLQQHDFT
     SQIFSLGYCP TGEWLAVGME NSNVEVLHVT KPDKYQLHLH ESCVLSLKFA HCGKWFVSTG
     KDNLLNAWRT PYGASIFQSK ESSSVLSCDI SVDDKYIVTG SGDKKATVYE VIY
//
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   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   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
CC   Distributed under the Creative Commons Attribution-NoDerivs License
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   DOPO_MOUSE              Reviewed;         621 AA.
AC   Q64237;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Dopamine beta-hydroxylase;
DE            EC=1.14.17.1;
DE   AltName: Full=Dopamine beta-monooxygenase;
DE   Contains:
DE     RecName: Full=Soluble dopamine beta-hydroxylase;
GN   Name=Dbh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=93080618; PubMed=1280432; DOI=10.1016/0006-291X(92)91598-K;
RA   Nakano T., Kobayashi K., Saito S., Fujita K., Nagatsu T.;
RT   "Mouse dopamine beta-hydroxylase: primary structure deduced from the
RT   cDNA sequence and exon/intron organization of the gene.";
RL   Biochem. Biophys. Res. Commun. 189:590-599(1992).
CC   -!- FUNCTION: Conversion of dopamine to noradrenaline.
CC   -!- CATALYTIC ACTIVITY: 3,4-dihydroxyphenethylamine + ascorbate + O(2)
CC       = noradrenaline + dehydroascorbate + H(2)O.
CC   -!- COFACTOR: Binds 1 PQQ per subunit (By similarity).
CC   -!- COFACTOR: Binds 2 copper ions per subunit (By similarity).
CC   -!- PATHWAY: Catecholamine biosynthesis; (R)-noradrenaline
CC       biosynthesis; (R)-noradrenaline from dopamine: step 1/1.
CC   -!- SUBUNIT: Homotetramer composed of two non-covalently bound
CC       disulfide-linked dimers (By similarity).
CC   -!- SUBCELLULAR LOCATION: Soluble dopamine beta-hydroxylase:
CC       Cytoplasmic vesicle, secretory vesicle lumen (By similarity).
CC       Cytoplasmic vesicle, secretory vesicle, chromaffin granule lumen
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC       membrane; Single-pass type II membrane protein (By similarity).
CC       Cytoplasmic vesicle, secretory vesicle, chromaffin granule
CC       membrane; Single-pass type II membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the copper type II ascorbate-dependent
CC       monooxygenase family.
CC   -!- SIMILARITY: Contains 1 DOMON 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; S50200; AAB24330.1; -; mRNA.
DR   IPI; IPI00132202; -.
DR   PIR; JC1346; JC1346.
DR   UniGene; Mm.167781; -.
DR   ProteinModelPortal; Q64237; -.
DR   STRING; Q64237; -.
DR   PhosphoSite; Q64237; -.
DR   PRIDE; Q64237; -.
DR   Ensembl; ENSMUST00000000910; ENSMUSP00000000910; ENSMUSG00000000889.
DR   MGI; MGI:94864; Dbh.
DR   GeneTree; ENSGT00530000063085; -.
DR   HOVERGEN; HBG005519; -.
DR   InParanoid; Q64237; -.
DR   OrthoDB; EOG4SN1ND; -.
DR   BRENDA; 1.14.17.1; 244.
DR   ArrayExpress; Q64237; -.
DR   Bgee; Q64237; -.
DR   CleanEx; MM_DBH; -.
DR   Genevestigator; Q64237; -.
DR   GermOnline; ENSMUSG00000000889; Mus musculus.
DR   GO; GO:0034466; C:chromaffin granule lumen; IEA:UniProtKB-SubCell.
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:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004500; F:dopamine beta-monooxygenase activity; IEA:EC.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0048149; P:behavioral response to ethanol; IMP:MGI.
DR   GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
DR   GO; GO:0001816; P:cytokine production; IMP:MGI.
DR   GO; GO:0042420; P:dopamine catabolic process; IMP:MGI.
DR   GO; GO:0042596; P:fear response; IMP:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0006548; P:histidine catabolic process; IEA:InterPro.
DR   GO; GO:0042309; P:homoiothermy; IMP:MGI.
DR   GO; GO:0002443; P:leukocyte mediated immunity; IMP:MGI.
DR   GO; GO:0050900; P:leukocyte migration; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0042711; P:maternal behavior; IMP:MGI.
DR   GO; GO:0007613; P:memory; IMP:MGI.
DR   GO; GO:0042421; P:norepinephrine biosynthetic process; IMP:MGI.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:MGI.
DR   GO; GO:0042981; P:regulation of apoptosis; IMP:MGI.
DR   GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR   GO; GO:0048265; P:response to pain; IMP:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   InterPro; IPR014784; Cu2_ascorb_mOase-like_C.
DR   InterPro; IPR020611; Cu2_ascorb_mOase_CS-1.
DR   InterPro; IPR014783; Cu2_ascorb_mOase_CS-2.
DR   InterPro; IPR000323; Cu2_ascorb_mOase_N.
DR   InterPro; IPR005018; DOMON_domain.
DR   InterPro; IPR000945; Dopamine_b_mOase.
DR   InterPro; IPR008977; PHM_PNGase_F-fold_dom.
DR   Gene3D; G3DSA:2.60.120.230; Cu2_ascorb_mOase_core; 1.
DR   Gene3D; G3DSA:2.60.120.310; Cu2_ascorb_mOase_core; 1.
DR   PANTHER; PTHR10157; Dopamine_b_mOase; 1.
DR   Pfam; PF01082; Cu2_monooxygen; 1.
DR   Pfam; PF03351; DOMON; 1.
DR   PRINTS; PR00767; DBMONOXGNASE.
DR   SMART; SM00664; DoH; 1.
DR   SUPFAM; SSF49742; PHM_PNGase_F; 2.
DR   PROSITE; PS00084; CU2_MONOOXYGENASE_1; 1.
DR   PROSITE; PS00085; CU2_MONOOXYGENASE_2; 1.
DR   PROSITE; PS50836; DOMON; 1.
PE   2: Evidence at transcript level;
KW   Catecholamine biosynthesis; Copper; Cytoplasmic vesicle;
KW   Disulfide bond; Glycoprotein; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Phosphoprotein; PQQ; Signal-anchor; Transmembrane;
KW   Transmembrane helix; Vitamin C.
FT   CHAIN         1    621       Dopamine beta-hydroxylase.
FT                                /FTId=PRO_0000006357.
FT   CHAIN        44    621       Soluble dopamine beta-hydroxylase
FT                                (Potential).
FT                                /FTId=PRO_0000308210.
FT   TOPO_DOM      1     20       Cytoplasmic (Potential).
FT   TRANSMEM     21     41       Helical; Signal-anchor for type II
FT                                membrane protein; (Potential).
FT   TOPO_DOM     42    621       Intragranular (Potential).
FT   DOMAIN       61    177       DOMON.
FT   ACT_SITE    234    234       Potential.
FT   ACT_SITE    416    416       Potential.
FT   METAL       266    266       Copper A (By similarity).
FT   METAL       267    267       Copper A (By similarity).
FT   METAL       337    337       Copper A (By similarity).
FT   METAL       416    416       Copper B (By similarity).
FT   METAL       418    418       Copper B (By similarity).
FT   METAL       491    491       Copper B (By similarity).
FT   MOD_RES     350    350       Phosphoserine; by CaMK (Potential).
FT   CARBOHYD     68     68       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    188    188       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    476    476       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    570    570       N-linked (GlcNAc...) (Potential).
FT   DISULFID    158    600       By similarity.
FT   DISULFID    236    287       By similarity.
FT   DISULFID    273    299       By similarity.
FT   DISULFID    394    507       By similarity.
FT   DISULFID    398    569       By similarity.
FT   DISULFID    470    492       By similarity.
FT   DISULFID    532    532       Interchain (By similarity).
FT   DISULFID    534    534       Interchain (By similarity).
SQ   SEQUENCE   621 AA;  70187 MW;  1EF8B1E3149C55C4 CRC64;
     MQAHLSHQPC WSSLPSPSVR EAASMYGTAV AIFLVILVAA LRGSEPPESP FPYHIPLDPE
     GILELSWNVS YVQEIIHFQL QVQGLRAGVL FGMSDRGEME NADLIMLWSD GDRAYFADAW
     SDRKGQIHLD SQQDYQLLQA QRTRDGLSLL FKRPFVTCDP KDYVIEDDTV HLVYGILEEP
     FQSLEAINTS GLHTGLLRVQ LLKSEVPTPS MPEDVQTMDI RAPDILIPDN EQTYWCYITE
     LPPRFPRHHI IMYEAIVTEG NEALVHHMEV FQCAAESEDF PQFNGPCDSK MKPDRLNYCR
     HVLAAWALGA KAFYYPKEAG VPFGGPGSSP FLRLEVHYHN PRKIQGRQDS SGIRLPYTAT
     LRRYDAGIME LGLVYTPLMA IPPQETAFVL TGYCTDKCTQ MALQDSGIHI FASQLHTHLT
     GRKVVTVLAR DGQERKEVNR DNHYSPHFRE IRMLKKVVTV YPGDVLITSC TYNTENKTLA
     TVGGFGILEE MCVNYVHYYP QTELELCKSA VDDGFLQKYF HMVNRFSSEE VCTCPQASVP
     QQFSSVPWNS FNRNMLKALY DYAPISMHCN KTSAVRFPGE WNLQPLPKIT STLEEPTPRC
     PIRQTQSPAN PTVPITTGGR C
//
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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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   CGT_MOUSE               Reviewed;         541 AA.
AC   Q64676; Q61634; Q91W57;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 2.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=2-hydroxyacylsphingosine 1-beta-galactosyltransferase;
DE            EC=2.4.1.45;
DE   AltName: Full=Ceramide UDP-galactosyltransferase;
DE   AltName: Full=Cerebroside synthase;
DE   AltName: Full=UDP-galactose-ceramide galactosyltransferase;
DE   Flags: Precursor;
GN   Name=Ugt8; Synonyms=Cgt, Ugt4, Ugt8a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; 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   PubMed=8661123; DOI=10.1006/geno.1996.0341;
RA   Coetzee T., Li X., Fujita N., Marcus J., Suzuki K., Francke U.,
RA   Popko B.;
RT   "Molecular cloning, chromosomal mapping, and characterization of the
RT   mouse UDP-galactose:ceramide galactosyltransferase gene.";
RL   Genomics 35:215-222(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=BALB/c; TISSUE=Leukocyte;
RX   PubMed=8661124; DOI=10.1006/geno.1996.0342;
RA   Bosio A., Binczek E., Stoffel W.;
RT   "Molecular cloning and characterization of the mouse CGT gene encoding
RT   UDP-galactose ceramide-galactosyltransferase (cerebroside
RT   synthetase).";
RL   Genomics 35:223-226(1996).
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=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: Catalyzes the transfer of galactose to ceramide, a key
CC       enzymatic step in the biosynthesis of galactocerebrosides, which
CC       are abundant sphingolipids of the myelin membrane of the central
CC       nervous system and peripheral nervous system.
CC   -!- CATALYTIC ACTIVITY: UDP-galactose + 2-(2-hydroxyacyl)sphingosine =
CC       UDP + 1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine.
CC   -!- PATHWAY: Sphingolipid metabolism; galactosylceramide biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase 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; U48896; AAC53576.1; -; Genomic_DNA.
DR   EMBL; U48892; AAC53576.1; JOINED; Genomic_DNA.
DR   EMBL; U48893; AAC53576.1; JOINED; Genomic_DNA.
DR   EMBL; U48894; AAC53576.1; JOINED; Genomic_DNA.
DR   EMBL; X92122; CAA63090.1; -; mRNA.
DR   EMBL; X92123; CAA63091.1; -; Genomic_DNA.
DR   EMBL; X92124; CAA63091.1; JOINED; Genomic_DNA.
DR   EMBL; X92125; CAA63091.1; JOINED; Genomic_DNA.
DR   EMBL; X92126; CAA63091.1; JOINED; Genomic_DNA.
DR   EMBL; X92177; CAA63091.1; JOINED; Genomic_DNA.
DR   EMBL; AK137364; BAE23325.1; -; mRNA.
DR   EMBL; BC016885; AAH16885.1; -; mRNA.
DR   IPI; IPI00136915; -.
DR   RefSeq; NP_035804.2; NM_011674.4.
DR   UniGene; Mm.306021; -.
DR   ProteinModelPortal; Q64676; -.
DR   SMR; Q64676; 267-435.
DR   STRING; Q64676; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PhosphoSite; Q64676; -.
DR   PRIDE; Q64676; -.
DR   Ensembl; ENSMUST00000057944; ENSMUSP00000050852; ENSMUSG00000032854.
DR   GeneID; 22239; -.
DR   KEGG; mmu:22239; -.
DR   UCSC; uc008rfy.1; mouse.
DR   CTD; 22239; -.
DR   MGI; MGI:109522; Ugt8a.
DR   eggNOG; roNOG07351; -.
DR   GeneTree; ENSGT00560000076760; -.
DR   HOGENOM; HBG446523; -.
DR   HOVERGEN; HBG098341; -.
DR   InParanoid; Q64676; -.
DR   OMA; NCDMIVG; -.
DR   OrthoDB; EOG4KKZ2Q; -.
DR   PhylomeDB; Q64676; -.
DR   BRENDA; 2.4.1.45; 244.
DR   NextBio; 302297; -.
DR   ArrayExpress; Q64676; -.
DR   Bgee; Q64676; -.
DR   CleanEx; MM_UGT8A; -.
DR   Genevestigator; Q64676; -.
DR   GermOnline; ENSMUSG00000032854; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003851; F:2-hydroxyacylsphingosine 1-beta-galactosyltransferase activity; IEA:EC.
DR   GO; GO:0008120; F:ceramide glucosyltransferase activity; TAS:MGI.
DR   GO; GO:0009247; P:glycolipid biosynthetic process; TAS:MGI.
DR   GO; GO:0042552; P:myelination; TAS:MGI.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   PANTHER; PTHR11926; UDP_glucos_trans; 1.
DR   Pfam; PF00201; UDPGT; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosyltransferase; Membrane; Signal; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21    541       2-hydroxyacylsphingosine 1-beta-
FT                                galactosyltransferase.
FT                                /FTId=PRO_0000036065.
FT   TRANSMEM    472    492       Helical; (Potential).
FT   CARBOHYD     78     78       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    333    333       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    442    442       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    335    335       T -> S (in Ref. 1; AAC53576).
FT   CONFLICT    458    458       R -> H (in Ref. 2; CAA63090/CAA63091).
FT   CONFLICT    511    511       E -> K (in Ref. 2; CAA63090/CAA63091).
FT   CONFLICT    524    524       R -> P (in Ref. 2; CAA63090/CAA63091).
FT   CONFLICT    533    534       RV -> HI (in Ref. 2; CAA63090/CAA63091).
FT   CONFLICT    541    541       R -> K (in Ref. 2; CAA63090/CAA63091).
SQ   SEQUENCE   541 AA;  61249 MW;  0E3436597F8810D0 CRC64;
     MKSYTPYFML LWSAVGIARA AKIIIVPPIM FESHLYIFKT LASALHERGH HTVLLLSEGR
     DIAPSNHYSL QRYPGIFNST TSDAFLQSKM RNIFSGRLTA VELVDILDHY TKNCDMMVGN
     QALIQGLKKE KFDLLLVDPN DMCGFVIAHL LGVKYAVFST GLWYPAEVGA PAPLAYVPEF
     NSLLTDRMNF LERMKNTGVY LISRIGVSFL VLPKYERIMQ KYNLLPAKSM YDLVHGSSLW
     MLCTDVALEF PRPTLPNVVY VGGILTKPAS PLPEDLQRWV SGAQEHGFVL VSFGAGVKYL
     SEDIANKLAG ALGRLPQKVI WRFSGTKPKN LGNNTKLIEW LPQNDLLGHS NIRAFLSHGG
     LNSIFETMYH GVPVVGIPLF GDHYDTMTRV QAKGMGILLE WNTVTEGELY DALVKVINNP
     SYRQRAQKLS EIHKDQPGHP VNRTTYWIDY ILRHDGARHL RSAVHQISFC QYFLLDIAFV
     LLLGAVLLYF ILSYVTKFIY RKIKSLWSKN EHSTVNGHYQ NGIRNGKYKG NGRVKHEKKV
     R
//
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   SBNO1_MOUSE             Reviewed;        1390 AA.
AC   Q689Z5; Q3KQK3; Q8BVN5;
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=Protein strawberry notch homolog 1;
DE            Short=mSno1;
GN   Name=Sbno1; Synonyms=Sno1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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/6J; TISSUE=Head;
RX   PubMed=17045962; DOI=10.1016/j.bbrc.2006.09.135;
RA   Baba K., Dekimoto H., Muraoka D., Agata K., Terashima T.,
RA   Katsuyama Y.;
RT   "A mouse homologue of strawberry notch is transcriptionally regulated
RT   by reelin signal.";
RL   Biochem. Biophys. Res. Commun. 350:842-849(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-784 (ISOFORM 2).
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-716 (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   PROTEIN SEQUENCE OF 790-809, 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-765 AND SER-766, 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=2;
CC       Name=1;
CC         IsoId=Q689Z5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q689Z5-2; Sequence=VSP_030299;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and testis.
CC       Expressed in the hippocampus, olfactory bulb, and cerebellum. Low
CC       expression detected in lung, heart, liver, skin, colon and kidney.
CC   -!- DEVELOPMENTAL STAGE: At E11 expressed throughout the entire
CC       neuroepithelium. In the developing brain, expresssed in the
CC       forebrain, tectum, cerebellum, striatum and olfactory bulb. At
CC       E15.5 expressed in the cortex; the dorsal part of the
CC       telencephalon becomes laminated, and expression is observed in the
CC       upper and ventricular layers. At E18.5 expression in the
CC       ventricular zone is weak.
CC   -!- MISCELLANEOUS: Expression is down-regulated in Reln-null embryos.
CC       Expression in P19 cell line was up-regulated by treatment with
CC       Reln.
CC   -!- SIMILARITY: Belongs to the SBNO family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI06157.1; 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; AB188811; BAD38625.1; -; mRNA.
DR   EMBL; AK077133; BAC36636.1; -; mRNA.
DR   EMBL; BC106156; AAI06157.1; ALT_SEQ; mRNA.
DR   IPI; IPI00661508; -.
DR   IPI; IPI00880835; -.
DR   UniGene; Mm.23879; -.
DR   UniGene; Mm.439104; -.
DR   ProteinModelPortal; Q689Z5; -.
DR   STRING; Q689Z5; -.
DR   PhosphoSite; Q689Z5; -.
DR   PRIDE; Q689Z5; -.
DR   Ensembl; ENSMUST00000065263; ENSMUSP00000066808; ENSMUSG00000038095.
DR   UCSC; uc008zpp.1; mouse.
DR   MGI; MGI:2384298; Sbno1.
DR   HOVERGEN; HBG108461; -.
DR   InParanoid; Q689Z5; -.
DR   OrthoDB; EOG48WC16; -.
DR   ArrayExpress; Q689Z5; -.
DR   Bgee; Q689Z5; -.
DR   CleanEx; MM_SBNO1; -.
DR   Genevestigator; Q689Z5; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   InterPro; IPR006935; Restrct_endonuc_I_R/III_Res.
DR   Pfam; PF04851; ResIII; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil;
KW   Direct protein sequencing; Phosphoprotein.
FT   CHAIN         1   1390       Protein strawberry notch homolog 1.
FT                                /FTId=PRO_0000314556.
FT   COILED      840    867       Potential.
FT   COMPBIAS    781    790       Poly-Lys.
FT   MOD_RES     147    147       N6-acetyllysine (By similarity).
FT   MOD_RES     212    212       Phosphoserine (By similarity).
FT   MOD_RES     411    411       N6-acetyllysine (By similarity).
FT   MOD_RES     690    690       Phosphoserine (By similarity).
FT   MOD_RES     691    691       Phosphoserine (By similarity).
FT   MOD_RES     695    695       Phosphoserine (By similarity).
FT   MOD_RES     765    765       Phosphoserine.
FT   MOD_RES     766    766       Phosphoserine.
FT   MOD_RES     791    791       Phosphoserine (By similarity).
FT   MOD_RES     812    812       Phosphoserine (By similarity).
FT   MOD_RES    1219   1219       N6-acetyllysine (By similarity).
FT   VAR_SEQ      79     79       Q -> QQ (in isoform 2).
FT                                /FTId=VSP_030299.
FT   CONFLICT     13     13       L -> S (in Ref. 1; BAD38625).
FT   CONFLICT     22     22       D -> G (in Ref. 1; BAD38625).
FT   CONFLICT    179    179       T -> A (in Ref. 1; BAD38625).
FT   CONFLICT    496    496       T -> A (in Ref. 1; BAD38625).
FT   CONFLICT    735    735       S -> P (in Ref. 1; BAD38625).
SQ   SEQUENCE   1390 AA;  153738 MW;  D811435E1E72CE02 CRC64;
     MVEPGQDLLL AALSESGISP NDLFDVDGGD AGLATPTPPS VQQSVPLSAL ELGLETEAAV
     PVKQEPEPMS TPALLNVRQP PSTTTFVLNQ INQLPTLGST IVMTKTPPAT TNRQTITLTK
     FIQTTANTRP SVSAPAVRNA MPAAPSKDQV QLKDLLKNNS LNELMKLKPP ANIAQPVATA
     ATDVSNGAVK KESSNKEVAR IWINDMKMRS FSPTMKVPVV KEEDEPEEED EEEMGHAETY
     AEYMPIKLKI GLRHPDAVVE TSSLSSVTPP DVWYKTSISE ETIDNGWLSA LQLEAVTYAA
     QQHETFLPNG DRAGFLIGDG AGVGKGRTIA GIIYENYLLS RKRALWFSVS NDLKYDAERD
     LRDIGAKNIL VHSLNKFKYG KISSKHNGSV KKGVIFATYS SLIGESQSGG KYKTRLKQLL
     HWCGDDFDGV IVFDECHKAK NLCPVGSSKP TKTGLAVLEL QNKLPKARVV YASATGASEP
     RNMAYMNRLG IWGEGTPFRE FSDFIQAVER RGVGAMEIVA MDMKLRGMYI ARQLSFTGVT
     FKIEEVLLSQ SYVKMYNKAV KLWVIARERF QQAADLIDAE QRMKKSMWGQ FWSAHQRFFK
     YLCIASKVKR VVQLAREEIK NGKCVVIGLQ STGEARTLEA LEEGGGELND FVSTAKGVLQ
     SLIEKHFPAP DRKKLYSLLG IDLTAPSNNS SPRDSPCKEN KIKKRKGEEI TREAKKARKV
     GGLTGSSSDD SGSESVSDND ESDYESSKNM SSGDDDDFNP FRDESSEDNE DDPWLIRKDH
     KKSKDKKKKK SIDPDSIQSA LLASGLGSKR PSFSSAPVIS PASNSAPANS NSNSNSSLVT
     SQDAVERAQQ MKKDLLDKLE KLAEDLPPNT LDELIDELGG PENVAEMTGR KGRVVSNDDG
     SISYESRSEL DVPVEILNIT EKQRFMDGDK NIAIISEAAS SGISLQADRR AKNQRRRVHM
     TLELPWSADR AIQQFGRTHR SNQVTAPEYV FLISELAGEQ RFASIVAKRL EGLGALTHGD
     RRATESRDLS RFNFDNKYGR NALEIVMKSI VNLDSPMVSP PPDYPGEFFK DVRQGLIGVG
     LINVEDRSGI LTLDKDYNNI GKFLNRILGM EVHQQNALFQ YFADTLTAVV QNAKKSGRYD
     MGILDLGSGD EKVRKSDVKK FLTPGYSTSG HVELYTISVE RGMSWEEATK IWAELTGPDD
     GFYLSLQIRN NKKTAILVKE VNPKKKLFLI YRPNTGKQLK LEIYADLKKK YKKVVSDDAL
     VHWLDQYNSS ADTCTHAYWR GNCKKASLGL VCEIGLRCRT YYVLCGSVLS VWTKVEGVLA
     SVSGTNVKMQ IVRLRTEDGQ RIVGLIIPAN CVSPLVNLLS TSDQSQQLAV QQKQLWQQHH
     PQSITNLSNL
//
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   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.
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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   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.
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CC   -----------------------------------------------------------------------
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.
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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   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   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;
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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   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;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   JHD2C_MOUSE             Reviewed;        2350 AA.
AC   Q69ZK6; Q6NV48; Q8BUF5; Q8C4I5; Q8C5Q9;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=Probable JmjC domain-containing histone demethylation protein 2C;
DE            EC=1.14.11.-;
DE   AltName: Full=Jumonji domain-containing protein 1C;
GN   Name=Jmjd1c; Synonyms=Jhdm2c, Kiaa1380;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; 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 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] OF 1-141; 1112-1832 AND
RP   1967-2350.
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] OF 968-2350 (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   [4]
RP   PROTEIN SEQUENCE OF 1032-1054, 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-135, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., 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 histone demethylase that specifically
CC       demethylates 'Lys-9' of histone H3, thereby playing a central role
CC       in histone code. Demethylation of Lys residue generates
CC       formaldehyde and succinate. May be involved in hormone-dependent
CC       transcriptional activation, by participating in recruitment to
CC       androgen-receptor target genes (By similarity).
CC   -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q69ZK6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q69ZK6-2; Sequence=VSP_018306;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate
CC       the association with nuclear receptors (By similarity).
CC   -!- SIMILARITY: Belongs to the JHDM2 histone demethylase family.
CC   -!- SIMILARITY: Contains 1 JmjC domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH68318.1; Type=Frameshift; Positions=1075;
CC       Sequence=BAC36783.1; Type=Erroneous termination; Positions=2326; Note=Translated as Leu;
CC       Sequence=BAC38410.1; Type=Erroneous initiation;
CC       Sequence=BAD32440.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK173162; BAD32440.1; ALT_INIT; mRNA.
DR   EMBL; AK077400; BAC36783.1; ALT_SEQ; mRNA.
DR   EMBL; AK082106; BAC38410.1; ALT_INIT; mRNA.
DR   EMBL; AK085500; BAC39458.1; -; mRNA.
DR   EMBL; BC068318; AAH68318.1; ALT_FRAME; mRNA.
DR   IPI; IPI00749954; -.
DR   IPI; IPI00755780; -.
DR   UniGene; Mm.23846; -.
DR   ProteinModelPortal; Q69ZK6; -.
DR   STRING; Q69ZK6; -.
DR   PhosphoSite; Q69ZK6; -.
DR   PRIDE; Q69ZK6; -.
DR   Ensembl; ENSMUST00000051446; ENSMUSP00000056227; ENSMUSG00000037876.
DR   Ensembl; ENSMUST00000095573; ENSMUSP00000093230; ENSMUSG00000037876.
DR   UCSC; uc007fls.1; mouse.
DR   MGI; MGI:1918614; Jmjd1c.
DR   eggNOG; roNOG05729; -.
DR   GeneTree; ENSGT00530000063039; -.
DR   HOGENOM; HBG717439; -.
DR   HOVERGEN; HBG079631; -.
DR   InParanoid; Q69ZK6; -.
DR   OrthoDB; EOG447FS9; -.
DR   ArrayExpress; Q69ZK6; -.
DR   Bgee; Q69ZK6; -.
DR   CleanEx; MM_JMJD1C; -.
DR   Genevestigator; Q69ZK6; -.
DR   GermOnline; ENSMUSG00000037876; 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: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:0016568; P:chromatin modification; IEA:UniProtKB-KW.
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; IPR013129; TF_JmjC.
DR   InterPro; IPR003347; TF_JmjC_AAH.
DR   Pfam; PF02373; JmjC; 1.
DR   SMART; SM00558; JmjC; 1.
DR   PROSITE; PS51184; JMJC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Chromatin regulator; Dioxygenase;
KW   Direct protein sequencing; Iron; Metal-binding; Nucleus;
KW   Oxidoreductase; Phosphoprotein; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1   2350       Probable JmjC domain-containing histone
FT                                demethylation protein 2C.
FT                                /FTId=PRO_0000234375.
FT   DOMAIN     2084   2308       JmjC.
FT   ZN_FING    1657   1682       C6-type (Potential).
FT   MOTIF      1876   1880       LXXLL motif.
FT   METAL      2146   2146       Iron; catalytic (By similarity).
FT   METAL      2148   2148       Iron; catalytic (By similarity).
FT   METAL      2276   2276       Iron; catalytic (By similarity).
FT   MOD_RES     135    135       Phosphoserine.
FT   MOD_RES     191    191       Phosphoserine (By similarity).
FT   MOD_RES     194    194       Phosphoserine (By similarity).
FT   MOD_RES     197    197       Phosphoserine (By similarity).
FT   MOD_RES     369    369       N6-acetyllysine (By similarity).
FT   MOD_RES     457    457       Phosphoserine (By similarity).
FT   MOD_RES     460    460       Phosphoserine (By similarity).
FT   VAR_SEQ    1824   2120       Missing (in isoform 2).
FT                                /FTId=VSP_018306.
FT   CONFLICT   1506   1506       P -> S (in Ref. 3; AAH68318).
FT   CONFLICT   1715   1715       P -> L (in Ref. 2; BAC38410).
FT   CONFLICT   2189   2189       I -> R (in Ref. 2; BAC36783 and 3;
FT                                AAH68318).
SQ   SEQUENCE   2350 AA;  260580 MW;  ACC779965F8F2EFA CRC64;
     MQGPYSLNGY RVRVYRQDSA TQWFTGIITH HDLFTRTMIV MNDQVLEPQN VDPSMVQMTF
     LDDVVHSLLK GENIGITSRR RSRASQNIST VHGHYTRAQA NSPRPAMNSQ AAVPKQNTHQ
     QQQQRSIRPN KRKGSDSSIP DEEKMKEDKY DCVSRGENPK GKNKHVVTKR RKPEEAEKRL
     SMKRLRTDNA SDASESSDAE SSSKRVTETS SSEPMPEYEP KNKVTSKVNG EEGQSQAAEE
     AGEETLIDTR PPWDQMQEDK NHNEGEKPKS TDSHLQDKMT LRSSEQATVA DHNSNDSVLQ
     ECNVENQRTV ELLPKDRLVS RTPTPKCVTD IKNDTHSERA AQENLNTFGL QTPENMDPNV
     SDSKHSNAKY LETAKQDCDQ SWVSDVVKVD LTQSSVTNAP SGSDKRDTEK ERNHYVSYMS
     SLSAVSVTED QLHKRSPPPE TIKAKLTTSV DTQKAKSSSS PEVVKPKITH SPDSVKSKAA
     YGNSQAVGER RLANKIEHEL SRGSFHPVPT RGSALETTKS PLIIDKNEHF TVYRDPALIG
     SETGANHISP FLSQHPFSLH SSSHRTCLNP GTHHPALTPG PHLLAGSTSQ TPLPTINTHP
     LTSGPHHPVH HPHLLPTVLP GVPTASLLGG HPRLESAHAS SLSHLALAHQ QQQQLLQHQS
     PHLLGQAHPS ASYNQLGLYP IIWQYPNGTH AYSGLGLPSS KWVHPENAVN AEASLRRNSP
     SPWLHQPTPV TSADGIGLLS HIPVRPSSAE PHRPHKITVH SSPPLTKTLA DHHKEELERK
     AFMEPLRSNA STSVKGDLDL NRSQAGKDCH LHRHFVGPRP PQETGERLNK YKEEHRRILQ
     ESIDVAPFTT KIKGHEVERE NYSRVVPSSS SPKSHAIKQD KDVDRSVSEI YKMKHSVPQS
     LPQSNYFTTL SNSVVNEPPR SYPSKEVSNI YTEKQNNNLS ATANPQTHSF ISSLSKPPPL
     IKHQPESESL VGKIPDHLPH QSASHSVTTF RSDCRSPTHL TVSSTNALRS MPALHRAPVF
     HPPIHHSLER KESSYSSLSP PTLTPVMPVN AGGKVQESQK PPTLIPEPKD SQSNFKNSSD
     QSLTEMWRSN NNLNREKAEW PVEKSSGKSQ AAVASVIVRP PSSTKVDSVP SVPLASKDRV
     CERSSSGANK TDYLKPEAGE TGRIILPNVN LESAHVKSEK NFEAVSQGNV PVSVMSAVNV
     VSTTKADVFT SAATTTSVSS LSSAETSYSL SNTISASTPF ECTSSKSVVS QAVAQAKDCT
     VSTAVPGTLA CSKTGSAVQP GSGFSGTTDF IHLKKHKAAL AAAQFKNSSV SEAELNTVRN
     QTVAASLPLD STMTCTASNK AISVGNGPAA QSSQPNYHTK LKKAWLTRHS EEDKNTNKME
     NSGNSVSEII KPCSVNLIAS TSNDIENRAD GRVAVDKYGR DEKVSRRKAK RTYESGSESG
     DSDESESKSE QRTKRQPKPT YKKKQNDLQK RKGEVEEDSK PNGVLSRSAK DKSKLKLQNS
     NSAGVPRSVL KDWRKVKKLK QTGESFLQDD SCCEIGPNLQ KCRECRLIRS KKGEESTHSP
     VFCRFYYFRR LSFSKNGVVR IDGFSSPDQY DDEAMSLWTH ENYEDDEVDV ETSKYILDII
     GDKFCQLVTS EKTALSWVKK DAKIAWKRAV RGVREMCDAC EATLFNVHWV CRKCGFVACL
     DCYKAKERKS SRDKELYAWM KCVKGQPHDH KHLMPTQIIP GSVLTDLLDA MHILREKYGI
     KSHCHCTNRQ NLQGGNVPTM NGVSQVLQNV LHHSNKTSVS LPESQQQNSP QKSQTNGNSS
     PGSASTDSRL TPPESQSPLH WLADLAEQKS REEKQENKEF TLEREIKEDG DQDASDSPNG
     STSPPASQSN EQGSTLRDLL TTTAGKLRVG STDAGIAFAP VYSMGTSSGK GGRTMPNILD
     DIIASVVENK IPPNKTSKIN IKSEPNEEPK ESSLPATDES NKSYRDIPHS WICDQHILWL
     KDYKNSNNWK LFKECWKQGQ PAVVSGVHKK MNISLWKAES ISLDFGDHQA DLLNCKDSIV
     SNANVKEFWD GFEEVSKRQK NKGGETVVLK LKDCPSGEDF KAMMPTRYED FLRCLPLPEY
     CNPEGKFNLA SHLPGFFVRP DLGPRLCSAY GVAAAKDHDI GTTNLHIEAS DVVNVLVYVG
     IAKGNGVLSK AGILKKFEEE ELDDVLRKIL KDSSEIPGAL WHIYAGKDVD KIREFLQKIS
     KEQGLEVLPE HDPIRDQSWY VNRKLRQRLL EEYGVRACTL IQFLGDAIVL PAGTLHQVQN
     FHSCVQVTED FVSPEHLVQS FHLTQELRLL KEEINYDDKL QVKNILYHAV KEMVRALKMH
     EDEVEDMEDT
//
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;
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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   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   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   -----------------------------------------------------------------------
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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   ARMX2_MOUSE             Reviewed;         784 AA.
AC   Q6A058; A2AKS5; Q9CXI9;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Armadillo repeat-containing X-linked protein 2;
GN   Name=Armcx2; Synonyms=Kiaa0512;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; 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; TISSUE=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).
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=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 3 ARM repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32238.1; 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; AK172960; BAD32238.1; ALT_INIT; mRNA.
DR   EMBL; AK014329; BAB29276.1; -; mRNA.
DR   EMBL; AK034185; BAC28622.1; -; mRNA.
DR   EMBL; AK044926; BAC32145.1; -; mRNA.
DR   EMBL; AL772348; CAM20586.1; -; Genomic_DNA.
DR   EMBL; BC054839; AAH54839.1; -; mRNA.
DR   IPI; IPI00469208; -.
DR   RefSeq; NP_001159869.1; NM_001166397.1.
DR   RefSeq; NP_001159870.1; NM_001166398.1.
DR   RefSeq; NP_080415.3; NM_026139.4.
DR   UniGene; Mm.285969; -.
DR   ProteinModelPortal; Q6A058; -.
DR   PRIDE; Q6A058; -.
DR   Ensembl; ENSMUST00000035559; ENSMUSP00000049147; ENSMUSG00000033436.
DR   Ensembl; ENSMUST00000113193; ENSMUSP00000108818; ENSMUSG00000033436.
DR   Ensembl; ENSMUST00000119010; ENSMUSP00000112507; ENSMUSG00000033436.
DR   GeneID; 67416; -.
DR   KEGG; mmu:67416; -.
DR   UCSC; uc009ugq.1; mouse.
DR   CTD; 67416; -.
DR   MGI; MGI:1914666; Armcx2.
DR   HOGENOM; HBG127434; -.
DR   HOVERGEN; HBG057677; -.
DR   InParanoid; Q6A058; -.
DR   OMA; VIGASAW; -.
DR   OrthoDB; EOG4BRWKX; -.
DR   PhylomeDB; Q6A058; -.
DR   ArrayExpress; Q6A058; -.
DR   Bgee; Q6A058; -.
DR   CleanEx; MM_ARMCX2; -.
DR   Genevestigator; Q6A058; -.
DR   GermOnline; ENSMUSG00000033436; 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; 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   2: Evidence at transcript level;
KW   Membrane; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN         1    784       Armadillo repeat-containing X-linked
FT                                protein 2.
FT                                /FTId=PRO_0000191365.
FT   TRANSMEM      7     27       Helical; (Potential).
FT   REPEAT      528    568       ARM 1.
FT   REPEAT      570    609       ARM 2.
FT   REPEAT      650    689       ARM 3.
FT   COMPBIAS    179    292       Pro-rich.
SQ   SEQUENCE   784 AA;  81036 MW;  3EEE7DB7EE6B0086 CRC64;
     MSRARDAGCV AAGIVIGASA WYCVYKYTRG KDQKKKRLTK PKNRASVGTG SRARAGLRAG
     FTIDLGPGFS PPNPVDIEIM NKAQGEASNL ATTVAEEVAP AAPSPKVQNG AESKVQELNG
     AKTEANLESV VMPSATCTVT PPPKVAGGLT AAEAPEIIGA PKVLEAPSTT EASGAVAAPG
     PTVSPMIAQT PGPVVPSPTI VSTGPAAIPW AVAHPGAVQS PGPAVPPMAV QSLVPAAPSW
     AVVAPPGAVY IPVAAHFAGP AAASRVTQSP GTVIPPLPPP SSVLPRGVPS VPGRTVQSPG
     AAVHPVAAQS TGVVVPPRAV QYSGAAVTSG GAAVPSGGAA TPRAAASTQR TASTEVMQVP
     RVAAATEATE TPRIGTPAMV AEASLPVHSG AAENPGTSGS SKTAATGKKA APGAHTGAIP
     KAGSATGAVP KGGGGKGGNK NRSGGKGKNR KNKVDVDELG MGFRPGDGAA AAAAASANGG
     QAFLAEIPES EEGESGWTDT ESDSDSEPDV PQRGKGKRTI PMHKRPFPYE IDEILGVRDL
     RKVLALLQKS DDPFIQQVAL LTLSNNANYS CNQETIRKLG GLPIIANMIN KTDPHIKEKA
     LMAMNNLSEN YENQGRLQVY MNKVMDDIMA SNLNSAVQVV GLKFLTNMTI TNDYQHLLVN
     SIANFFRLLS QGGGKIKVEI LKILSNFAEN PDMLKKLLGT QVPSSFSSLY NSYVESEILI
     NALTLFEIIF DNLRAEVFNY REFNKGSLFY LCTTSGVCVK KIRALANHHD LLVKVKVIKL
     VNKF
//
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   Q6A075_MOUSE            Unreviewed;       351 AA.
AC   Q6A075;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   08-FEB-2011, entry version 38.
DE   SubName: Full=MKIAA0394 protein;
DE   Flags: Fragment;
GN   Name=Gas7; Synonyms=mKIAA0394;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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   -----------------------------------------------------------------------
DR   EMBL; AK172943; BAD32221.1; -; mRNA.
DR   IPI; IPI00473740; -.
DR   UniGene; Mm.152121; -.
DR   UniGene; Mm.40338; -.
DR   ProteinModelPortal; Q6A075; -.
DR   STRING; Q6A075; -.
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   GeneTree; ENSGT00530000063207; -.
DR   HOVERGEN; HBG001320; -.
DR   InParanoid; Q6A075; -.
DR   ArrayExpress; Q6A075; -.
DR   Bgee; Q6A075; -.
DR   Genevestigator; Q6A075; -.
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   Pfam; PF00611; FCH; 1.
DR   SMART; SM00055; FCH; 1.
DR   PROSITE; PS50133; FCH; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   351 AA;  40715 MW;  940DB9E5E99E33CF CRC64;
     PIPPPTWGTT GMGKKMSNME NSFDDGSHLS PQNLGSSSPG RKQSKENTIT INCVTFPHPD
     TMPEQQLLKP TEWSYCDYFW ADKKDPQGNG TVAGFELLLQ KQLKGKQMQK EMSEFIRERI
     KIEEEYAKNL AKLSQNSLAA QEEGSLGEAW AQVKKSLADE AEVHLKFSAK LHSEVEKPLM
     NFRENFKKDM KKCDHHIADL RKQLASRYAS VEKARKALTE RQKDLEMKTQ QLEIKLSNKT
     EEDIKKARRK STQAGDDLMR CVDLYNQAQS KWFEEMVTTT LELERLEVER VEMIRQHLCQ
     YTQLRHETDM FNQSTVEPVD QLLRKVDPAK DRELWVREHK TGNIRPVDME I
//
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   Q6DD96_MOUSE            Unreviewed;       935 AA.
AC   Q6DD96;
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=Protocadherin gamma subfamily A, 7;
GN   Name=Pcdhga7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; 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: 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.
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DR   EMBL; BC077712; AAH77712.1; -; mRNA.
DR   IPI; IPI00463006; -.
DR   RefSeq; NP_291068.2; NM_033590.3.
DR   UniGene; Mm.247203; -.
DR   ProteinModelPortal; Q6DD96; -.
DR   SMR; Q6DD96; 28-141, 234-347, 358-666.
DR   PhosphoSite; Q6DD96; -.
DR   PRIDE; Q6DD96; -.
DR   GeneID; 93715; -.
DR   KEGG; mmu:93715; -.
DR   UCSC; uc008eqt.1; mouse.
DR   CTD; 93715; -.
DR   MGI; MGI:1935219; Pcdhga7.
DR   eggNOG; maNOG22550; -.
DR   HOVERGEN; HBG054878; -.
DR   NextBio; 351527; -.
DR   Genevestigator; Q6DD96; -.
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-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   935 AA;  101559 MW;  6E015096607E9F4E CRC64;
     MAPGQRGWGS HYRGFVLLSI LLGMRWEAWA GQILYSVSEE TDKGSFVGNI TKDLGLQPRE
     LAERGVRIIT KGKTQLFSLN PRSGSLVTAG RIDREELCAQ SPRCLVSFNI LIEDKMNLYP
     IEVEIMDVND NAPRFLTEEI NIKIMENAAP GVRFPLKEAT DSDVGKNSLQ RYQLSPNHHF
     SLVVQSGDDG TKYPELVLEK ALDREEEGLH HLVLTAYDGG DPLRSGTASI RVTVVDVNDH
     TPVFSLPLYQ ATVPENVPVG TRLLTVNAID LDEGIYGEVT YSFWKITPEL LQIFHLSSLT
     GELSTLKGLD YEQSSFYELE VQAQDGAGSL TKAKVLITVL DVNDNAPEVT VTSVSSPVPE
     DTPPGTVIAL FYLQDKDSGK NGEVTCSLPE NLPFKLERSI DNYYRLVTAR NLDREKMSVY
     NITLKATDGG IPPLSTETRM SIHVSDTNDN PPTFSDSSYS IYVPENNPRG ASIFSVTAQD
     PDSDKNAQVT YALAEDTIQG VPVSSYVSIN SDTGILYALG SFDYEQFRDL QLRVTARDSG
     DPPLSSNVSL KLFVLDKNDN APEILYPALP TDGSTGVELA PRSAEPGYLV TKVVAVDKDS
     GPNAWLSYRL LKASEPGLFS VGLHTGEVRT ARALLDRDAL KQNLVVVVQD HGQPPLSATV
     TLTVAVANSI PDVLADLGSI RTPSEPDDSD ITLYLVVAVA TVSCVFLVFV TVLLALRLWR
     WHKSHMLQAS SGGGLEDVPA SHFVGLDGVQ AFLQTYSHEV SLTADSRKSH IIFPQPNYVD
     TLISQDSCEK SDSLLTSIDF QECKGEAPSS QQAPPNTDWR FSQAQRPGTS GSQNGDETGT
     WPNNQFDTEM LQAMILASAS EAADGSSTLG GGAGTMGLSA RYGPQFTLQH VPDYRQNVYI
     PGSNATLTNA AGKRDGKAPA GGNGNKKKSG KKEKK
//
ID   RHG21_MOUSE             Reviewed;        1944 AA.
AC   Q6DFV3; A2AL67; Q80TD7; Q80XS1;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Rho GTPase-activating protein 21;
DE   AltName: Full=Rho GTPase-activating protein 10;
DE   AltName: Full=Rho-type GTPase-activating protein 21;
GN   Name=Arhgap21; Synonyms=Arhgap10, Kiaa1424;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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 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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 683-1944.
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 1697-1708, 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-1092, 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 ARF1.
RX   PubMed=17347647; DOI=10.1038/sj.emboj.7601634;
RA   Menetrey J., Perderiset M., Cicolari J., Dubois T., Elkhatib N.,
RA   El Khadali F., Franco M., Chavrier P., Houdusse A.;
RT   "Structural basis for ARF1-mediated recruitment of ARHGAP21 to Golgi
RT   membranes.";
RL   EMBO J. 26:1953-1962(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
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-874; SER-1424; SER-1425
RP   AND SER-1426, 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 (GAP) for RHOA
CC       and CDC42. Downstream partner of ARF1 which may control Golgi
CC       apparatus structure and function. Also required for CTNNA1
CC       recruitment to adherens junctions (By similarity).
CC   -!- SUBUNIT: Interacts with CTNNA1 (By similarity). Interacts with
CC       GTP-bound ARF1 and probably ARF6.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral
CC       membrane protein (By similarity). Cell junction (By similarity).
CC       Cytoplasmic vesicle membrane; Peripheral membrane protein (By
CC       similarity). Cytoplasm, cytoskeleton (By similarity).
CC       Note=Localization to the Golgi is dependent on interaction with
CC       GTP-bound ARF1 (By similarity).
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=CAM13451.1; Type=Erroneous gene model prediction;
CC       Sequence=CAM16533.1; Type=Erroneous gene model prediction;
CC       Sequence=CAM24301.1; Type=Erroneous gene model prediction;
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DR   EMBL; BX649226; CAM13451.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL773540; CAM13451.1; JOINED; Genomic_DNA.
DR   EMBL; AL929100; CAM13451.1; JOINED; Genomic_DNA.
DR   EMBL; AL773540; CAM16533.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL929100; CAM16533.1; JOINED; Genomic_DNA.
DR   EMBL; BX649226; CAM16533.1; JOINED; Genomic_DNA.
DR   EMBL; AL929100; CAM24301.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL773540; CAM24301.1; JOINED; Genomic_DNA.
DR   EMBL; BX649226; CAM24301.1; JOINED; Genomic_DNA.
DR   EMBL; BC043038; AAH43038.1; -; mRNA.
DR   EMBL; BC076629; AAH76629.1; -; mRNA.
DR   EMBL; AK122508; BAC65790.1; -; Transcribed_RNA.
DR   IPI; IPI00918720; -.
DR   RefSeq; NP_001074833.3; NM_001081364.3.
DR   UniGene; Mm.28507; -.
DR   UniGene; Mm.465492; -.
DR   HSSP; Q9WV48; 1Q3O.
DR   ProteinModelPortal; Q6DFV3; -.
DR   SMR; Q6DFV3; 53-164, 918-1035, 1136-1332.
DR   STRING; Q6DFV3; -.
DR   PhosphoSite; Q6DFV3; -.
DR   PRIDE; Q6DFV3; -.
DR   Ensembl; ENSMUST00000045258; ENSMUSP00000042617; ENSMUSG00000036591.
DR   Ensembl; ENSMUST00000114594; ENSMUSP00000110241; ENSMUSG00000036591.
DR   GeneID; 71435; -.
DR   KEGG; mmu:71435; -.
DR   UCSC; uc008imy.1; mouse.
DR   CTD; 71435; -.
DR   MGI; MGI:1918685; Arhgap21.
DR   GeneTree; ENSGT00600000084250; -.
DR   HOVERGEN; HBG106694; -.
DR   InParanoid; Q6DFV3; -.
DR   ArrayExpress; Q6DFV3; -.
DR   Bgee; Q6DFV3; -.
DR   CleanEx; MM_ARHGAP10; -.
DR   CleanEx; MM_ARHGAP21; -.
DR   Genevestigator; Q6DFV3; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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   Cell junction; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW   Direct protein sequencing; Golgi apparatus; GTPase activation;
KW   Membrane; Phosphoprotein.
FT   CHAIN         1   1944       Rho GTPase-activating protein 21.
FT                                /FTId=PRO_0000305246.
FT   DOMAIN       55    164       PDZ.
FT   DOMAIN      924   1033       PH.
FT   DOMAIN     1140   1332       Rho-GAP.
FT   REGION      923   1090       Interaction with ARF1 and ARF6 (By
FT                                similarity).
FT   REGION     1578   1847       Interaction with CTNNA1 (By similarity).
FT   MOD_RES      41     41       Phosphoserine.
FT   MOD_RES     453    453       Phosphoserine (By similarity).
FT   MOD_RES     469    469       Phosphoserine (By similarity).
FT   MOD_RES     471    471       Phosphoserine (By similarity).
FT   MOD_RES     874    874       Phosphoserine.
FT   MOD_RES     917    917       Phosphoserine (By similarity).
FT   MOD_RES    1083   1083       Phosphoserine (By similarity).
FT   MOD_RES    1092   1092       Phosphoserine.
FT   MOD_RES    1213   1213       Phosphoserine (By similarity).
FT   MOD_RES    1214   1214       Phosphoserine (By similarity).
FT   MOD_RES    1233   1233       Phosphotyrosine (By similarity).
FT   MOD_RES    1276   1276       Phosphothreonine (By similarity).
FT   MOD_RES    1376   1376       Phosphoserine (By similarity).
FT   MOD_RES    1424   1424       Phosphoserine.
FT   MOD_RES    1425   1425       Phosphoserine.
FT   MOD_RES    1426   1426       Phosphoserine.
FT   MOD_RES    1655   1655       Phosphoserine (By similarity).
FT   CONFLICT   1491   1491       P -> S (in Ref. 1; AAH43038, 2 and 3;
FT                                BAC65790).
SQ   SEQUENCE   1944 AA;  215743 MW;  A7F832ECD3DBC081 CRC64;
     MATHWTGLPE EDGDKLKACG AASACEVSKN KDGKDQGEPV SPSEDEPFSW PGPKTVMLKR
     TSQGFGFTLR HFIVYPPESA IQFSYKDEEN GNRGGKQRNR LEPMDTIFVK QVKEGGPAFE
     AGLCTGDRII KVNGESVIGK TYSQVIALIQ NSDTTLELSV MPKDEDILQV 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 PPPHSSKRNR
     SPTLSCRLAM LKEGPRSLLT QKPHCEETGS DSGTLLSTSS QASLLRSSTK KSTSPETKHS
     EFLSIAGTTT SDYSTTSSTT YLTSLDSSRL SPEVQSVAES KGDEADDERS ELVSEGRPVE
     TDSESEFPVF PTTLTSDRLF RGKFQEVARV 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   NOMO1_MOUSE             Reviewed;        1214 AA.
AC   Q6GQT9; Q3TKZ1; Q8BJM1; Q8BJM8; Q8BLS9; Q8K074; Q8R1I7;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=Nodal modulator 1;
DE   Flags: Precursor;
GN   Name=Nomo1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; 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=Blastocyst, 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, 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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1196 AND SER-1197, 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 antagonize Nodal signaling (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH24503.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=AAH33923.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAC38713.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; AK043279; BAC31513.1; -; mRNA.
DR   EMBL; AK082495; BAC38508.1; -; mRNA.
DR   EMBL; AK082963; BAC38713.1; ALT_INIT; mRNA.
DR   EMBL; AK166764; BAE39002.1; -; mRNA.
DR   EMBL; BC024503; AAH24503.1; ALT_INIT; mRNA.
DR   EMBL; BC033923; AAH33923.1; ALT_INIT; mRNA.
DR   EMBL; BC072630; AAH72630.1; -; mRNA.
DR   IPI; IPI00222429; -.
DR   RefSeq; NP_694697.3; NM_153057.4.
DR   UniGene; Mm.274811; -.
DR   ProteinModelPortal; Q6GQT9; -.
DR   SMR; Q6GQT9; 42-103, 133-187, 268-294, 322-389, 823-850, 954-1042.
DR   STRING; Q6GQT9; -.
DR   PhosphoSite; Q6GQT9; -.
DR   PRIDE; Q6GQT9; -.
DR   Ensembl; ENSMUST00000033121; ENSMUSP00000033121; ENSMUSG00000030835.
DR   GeneID; 211548; -.
DR   KEGG; mmu:211548; -.
DR   CTD; 211548; -.
DR   MGI; MGI:2385850; Nomo1.
DR   GeneTree; ENSGT00390000000089; -.
DR   HOGENOM; HBG358091; -.
DR   HOVERGEN; HBG023764; -.
DR   InParanoid; Q6GQT9; -.
DR   OMA; RGSEDIV; -.
DR   OrthoDB; EOG4PG602; -.
DR   ArrayExpress; Q6GQT9; -.
DR   Bgee; Q6GQT9; -.
DR   Genevestigator; Q6GQT9; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:InterPro.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR014766; CarboxyPept_regulatory_dom.
DR   InterPro; IPR019008; DUF2012.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Gene3D; G3DSA:2.60.40.1120; CarboxyPept_regulatory; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Pfam; PF09430; DUF2012; 1.
DR   SUPFAM; SSF49464; CarboxypepD_reg; 1.
DR   SUPFAM; SSF49452; CBD_4; 3.
PE   1: Evidence at protein level;
KW   Coiled coil; Glycoprotein; Membrane; Phosphoprotein; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24   1214       Nodal modulator 1.
FT                                /FTId=PRO_0000396822.
FT   TOPO_DOM     24   1150       Extracellular (Potential).
FT   TRANSMEM   1151   1167       Helical; (Potential).
FT   TOPO_DOM   1168   1214       Cytoplasmic (Potential).
FT   COILED      692    720       Potential.
FT   MOD_RES    1196   1196       Phosphoserine.
FT   MOD_RES    1197   1197       Phosphoserine.
FT   CARBOHYD     42     42       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    210    210       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    610    610       N-linked (GlcNAc...) (Potential).
FT   CONFLICT      6      6       C -> G (in Ref. 1; BAC38508).
FT   CONFLICT     62     63       DC -> GW (in Ref. 1; BAC38508).
FT   CONFLICT     75     75       Y -> V (in Ref. 1; BAC38508).
FT   CONFLICT     95     97       TNV -> PHG (in Ref. 1; BAC38508).
FT   CONFLICT    101    101       V -> G (in Ref. 1; BAC38508).
FT   CONFLICT    109    109       T -> A (in Ref. 1; BAC38508).
FT   CONFLICT    113    113       D -> G (in Ref. 1; BAC38508).
FT   CONFLICT    477    477       P -> T (in Ref. 1; BAC38508).
FT   CONFLICT    875    878       KAED -> GRVG (in Ref. 2; AAH24503).
FT   CONFLICT   1029   1029       E -> G (in Ref. 1; BAC31513).
FT   CONFLICT   1176   1176       L -> V (in Ref. 1; BAC31513).
SQ   SEQUENCE   1214 AA;  133420 MW;  0F71587617C444A7 CRC64;
     MRAGRCAAAL LLLLLSGAGR AIGSEDIVVG CGGFVKSDVE INYSLIEIKL YTKHGTLKYQ
     TDCAPNNGYF MIPLYDKGDF ILKIEPPLGW SFEPTNVELR VDGVSDICTK GGDINFLFTG
     FSVNGKVLSK GQPLGPAGVQ VSLRSTGADS KIQSTVTQPG GKFAFFKVLP GDYEILATHP
     TWALKEASTT VRVTNSNANA AGPLIVAGYN VSGSVRSDGE PMKGVKFLLF SSLVNKEDVL
     GCNVSPVSGF QPPDESLVYL CYAVSKEDGS FSFYSLPSGG YTVVPFYRGE RITFDVAPSR
     LDFTVEHDSL RIEPVFHVMG FSVTGRVLNG PDGEGVPEAV VTLNNQIKVK TKADGSFRLE
     NITTGTYTIH AQKEHLYFEM VTIKIAPNTP QLADLIATGF SICGQIAIVR SPDTIKQMSK
     YRVVLSSQDK DKALLTVDSD AHGSFCFKAK PGAYKVQVVV PEAETRAGLM LKPQVFPLTV
     TNRPVMDVAF VQFLASVSGK VSCLDTCGDL LVTLQSLSRQ GEKRSLQLSG KVNSMTFTFD
     KVLPGRYKIS IMHEDWCWRN KSLEVEVLED DVSAVEFRQT GYMLRCALSH AITLEFHQDG
     NGPENVGIYN LSRGVNRFCL SKPGVYKVTP RSCHRFEQAF YTYDTSSPSI LTLTAIRHHV
     LGTIITDKMM DVTVTIKSSI DSEPALVLGP LKSAQELRRE QQLAEIETRR QEREKNGKEE
     GEEGRARPPG QEMVDELQGP FSYDFSYWAR SGEKITVTPS SKELLFYPPS MEATVSGESC
     PGKLIEIHGK AGLFLEGQIH PELEGVEIVI SEKGASSPLI TVFTDDKGAY SVGPLHSDLE
     YTVNSQKEGY VLTAVEGTVG DFKAYALAGV SFEIKAEDDQ PLPGVLLSLS GGVFRSNLLT
     QDNGILTFSN LSPGQYYFKP MMKEFRFEPS SQMIEVQEGQ NLRITITGFR TAYSCYGTVS
     SLNGEPEQGV AVEAVGQKDC SIYGEDTVTD EEGKFRLRGL LPGCMYHVQL KAEGNDHIER
     ALPHHRVIEV GNNDVDDVNI IVFRQINQFD LSGNVITSSE YLSTLWVKLY KSESLDNPIQ
     TVSLGQSLFF HFPPLLRDGE NYVVLLDTTL PRSQYDYVLP QVSFTAVGYH KHITLVFSPT
     RKLPEQDIAQ GSYIALPLTL LLLLAGYNHD KLIPLLLQLT SRLQGVRALG QAASDSSGPE
     DMKRQTKKQK TRRT
//
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   -----------------------------------------------------------------------
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   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.
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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   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;
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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   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   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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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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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   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;
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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   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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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   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.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   CSKI1_MOUSE             Reviewed;        1431 AA.
AC   Q6P9K8; Q6ZPU2; Q8BWU2; Q8BX99; Q9CXH0;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Caskin-1;
DE   AltName: Full=CASK-interacting protein 1;
GN   Name=Caskin1; Synonyms=Kiaa1306;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; 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 667-1431 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J; TISSUE=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] OF 14-1431 (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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-1431 (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 THR-1067; SER-1069; SER-1259
RP   AND SER-1363, 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-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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-650; THR-779; SER-791;
RP   SER-1259 AND SER-1363, 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 link the scaffolding protein CASK to downstream
CC       intracellular effectors (By similarity).
CC   -!- SUBUNIT: Binds the CaM kinase domain of CASK. Forms a ternary
CC       complex with CASK and LIN7A, LIN7B or LIN7C. Competes with APBA1
CC       that forms a similar complex with CASK and LIN7 proteins. The
CC       tripartite complex CASKIN1/CASK/LIN7(A/B/C) binds the cytoplasmic
CC       tail of NRXN1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q6P9K8-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q6P9K8-2; Sequence=VSP_013123;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q6P9K8-3; Sequence=VSP_013124;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q6P9K8-4; Sequence=VSP_013121, VSP_013122;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 6 ANK repeats.
CC   -!- SIMILARITY: Contains 2 SAM (sterile alpha motif) domains.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; AK014376; BAB29308.1; -; mRNA.
DR   EMBL; AK048449; BAC33340.1; -; mRNA.
DR   EMBL; AK049987; BAC34019.1; -; mRNA.
DR   EMBL; AK129327; BAC98137.1; -; mRNA.
DR   EMBL; BC060720; AAH60720.1; -; mRNA.
DR   IPI; IPI00411109; -.
DR   IPI; IPI00553626; -.
DR   IPI; IPI00553792; -.
DR   IPI; IPI00755229; -.
DR   RefSeq; NP_082213.2; NM_027937.2.
DR   UniGene; Mm.480045; -.
DR   ProteinModelPortal; Q6P9K8; -.
DR   SMR; Q6P9K8; 4-265, 479-538, 548-604.
DR   STRING; Q6P9K8; -.
DR   PhosphoSite; Q6P9K8; -.
DR   PRIDE; Q6P9K8; -.
DR   Ensembl; ENSMUST00000024958; ENSMUSP00000024958; ENSMUSG00000033597.
DR   Ensembl; ENSMUST00000088474; ENSMUSP00000085824; ENSMUSG00000033597.
DR   Ensembl; ENSMUST00000115347; ENSMUSP00000111004; ENSMUSG00000033597.
DR   GeneID; 268932; -.
DR   KEGG; mmu:268932; -.
DR   UCSC; uc008awm.1; mouse.
DR   UCSC; uc008awo.1; mouse.
DR   UCSC; uc008awp.1; mouse.
DR   CTD; 268932; -.
DR   MGI; MGI:2442952; Caskin1.
DR   eggNOG; roNOG14504; -.
DR   GeneTree; ENSGT00530000063104; -.
DR   HOGENOM; HBG717177; -.
DR   HOVERGEN; HBG051133; -.
DR   InParanoid; Q6P9K8; -.
DR   OMA; PEVKRAH; -.
DR   OrthoDB; EOG4JT04T; -.
DR   NextBio; 392583; -.
DR   ArrayExpress; Q6P9K8; -.
DR   Bgee; Q6P9K8; -.
DR   CleanEx; MM_CASKIN1; -.
DR   Genevestigator; Q6P9K8; -.
DR   GermOnline; ENSMUSG00000033597; 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; 4.
DR   Pfam; PF00536; SAM_1; 2.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00248; ANK; 6.
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; 6.
DR   PROSITE; PS50105; SAM_DOMAIN; 2.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ANK repeat; Cytoplasm; Phosphoprotein; Repeat;
KW   SH3 domain.
FT   CHAIN         1   1431       Caskin-1.
FT                                /FTId=PRO_0000066981.
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      476    539       SAM 1.
FT   DOMAIN      545    609       SAM 2.
FT   REGION      375    471       CASK-binding (By similarity).
FT   COMPBIAS    761    878       Pro-rich.
FT   COMPBIAS   1154   1356       Pro-rich.
FT   MOD_RES     253    253       Phosphotyrosine.
FT   MOD_RES     336    336       Phosphotyrosine (By similarity).
FT   MOD_RES     650    650       Phosphoserine.
FT   MOD_RES     779    779       Phosphothreonine.
FT   MOD_RES     791    791       Phosphoserine.
FT   MOD_RES    1067   1067       Phosphothreonine.
FT   MOD_RES    1069   1069       Phosphoserine.
FT   MOD_RES    1259   1259       Phosphoserine.
FT   MOD_RES    1363   1363       Phosphoserine.
FT   VAR_SEQ     351    365       SRTGSEPSPPQGGGS -> KSTPLWREASRGHSA (in
FT                                isoform 4).
FT                                /FTId=VSP_013121.
FT   VAR_SEQ     366   1431       Missing (in isoform 4).
FT                                /FTId=VSP_013122.
FT   VAR_SEQ     477    547       Missing (in isoform 2).
FT                                /FTId=VSP_013123.
FT   VAR_SEQ    1284   1342       Missing (in isoform 3).
FT                                /FTId=VSP_013124.
FT   CONFLICT    274    274       K -> E (in Ref. 1; BAB29308).
FT   CONFLICT    969    969       A -> S (in Ref. 1; BAC34019).
FT   CONFLICT   1235   1235       S -> A (in Ref. 3; BAC98137).
SQ   SEQUENCE   1431 AA;  150495 MW;  F89BFB1B2B8926EF 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 SASEGKSAEA
     VSQWLATFQL QLYAPNFTSA GYDLPTISRM TPEDLTAIGV TKPGHRKKIT AEISGLNIPD
     WLPEHKPANL AVWLSMIGLA QYYKVLVDNG YENIDFITDI TWEDLQEIGI TKLGHQKKLM
     LAVRKLAELQ KAEYSKYEGG PLRRKTPQSL EMMAIESPPP SEPAAAECQS PKMTTFQDSE
     LSGELQAALS GPAEAGAAAV EKSSNHLPPT PRTTSRESSL SGRARHISSS QELLGDGPPG
     PGSPMSRSQE YLLDEGMAPG TPPKEVRSSR HGHSVKRASV PPVPGKPRQV LPSGASHFTP
     PQTPTKAQPG SPQALGGPHG PATAKVKPTP QLLPPTDRPM SPRSLPQSPT HRGFAYVLPQ
     PVEGEVGPPA PGPAPPPVPA AVPTLCLPPE TDVEPGRPKK RAHSLNRYAA SDSEPERDEL
     LVPAAAGPYA TVQRRVGRSH SVRAPAGTDK NVNRSQSFAV RPRKKGPPPP PPKRSSSAMA
     SANLADEPAP DVEAEDGRLG VRAQRRRASD LAGSVDTGSA GSVKSIAAML ELSSIGGGGR
     AIRRPPEGHP TPRPASPEPG RVATVLASVK HKEAIGPDGE VVNRRRTLSG PVTGLLATAR
     RGSGEPAEQS HFMEDGTARQ RLRGPAKGEA SAEGPPLARV EASATLKRRI RAKQSQQENV
     KFILTESDTV KRRPKAKEPD TGPEPPPPLS VYQNGTATVR RRPTSEQAGP PELPPPPPPA
     EPPPADLMQL PPLPLPDGNA RKPVKPPVSP KPILSQPVSK IQGSPTPASK KVPLPGPGSP
     EVKRAHGTPP PVSPKPPPPP TAPKPAKALA GLQSSSATPS PVPSPARQPP AALIKPASSP
     PSQSASPVKP PSPGTPALHV PAKPPRAAAS VVSGPPVASD CASPGDSARQ KLEETSACLA
     AALQAVEEKI RQEDGQGPRP SSIEEKSTGS ILEDIGSMFD DLADQLDAML 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   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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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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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   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   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;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   PAPD7_MOUSE             Reviewed;         542 AA.
AC   Q6PB75;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=DNA polymerase sigma;
DE            EC=2.7.7.7;
DE   AltName: Full=PAP-associated domain-containing protein 7;
GN   Name=Papd7; Synonyms=Pols;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; 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: DNA polymerase, probably involved in DNA repair. May
CC       play a role in sister chromatid cohesion. Does not play a role in
CC       replication-dependent histone mRNA degradation (By similarity).
CC   -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
CC       diphosphate + DNA(n+1).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC   -!- SIMILARITY: Contains 1 PAP-associated domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC059846; AAH59846.1; -; mRNA.
DR   IPI; IPI00387593; -.
DR   RefSeq; NP_941002.2; NM_198600.2.
DR   UniGene; Mm.315959; -.
DR   ProteinModelPortal; Q6PB75; -.
DR   SMR; Q6PB75; 1-287.
DR   STRING; Q6PB75; -.
DR   PhosphoSite; Q6PB75; -.
DR   PRIDE; Q6PB75; -.
DR   Ensembl; ENSMUST00000044081; ENSMUSP00000040757; ENSMUSG00000034575.
DR   GeneID; 210106; -.
DR   KEGG; mmu:210106; -.
DR   UCSC; uc007rch.1; mouse.
DR   CTD; 210106; -.
DR   MGI; MGI:2682295; Papd7.
DR   GeneTree; ENSGT00400000022055; -.
DR   HOGENOM; HBG714944; -.
DR   HOVERGEN; HBG053636; -.
DR   InParanoid; Q6PB75; -.
DR   OrthoDB; EOG4N04DQ; -.
DR   PhylomeDB; Q6PB75; -.
DR   BRENDA; 2.7.7.7; 244.
DR   NextBio; 372866; -.
DR   ArrayExpress; Q6PB75; -.
DR   Bgee; Q6PB75; -.
DR   CleanEx; MM_POLS; -.
DR   Genevestigator; Q6PB75; -.
DR   GermOnline; ENSMUSG00000034575; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   InterPro; IPR002934; Nucleotidyltransferase.
DR   InterPro; IPR002058; PAP_assoc.
DR   Pfam; PF01909; NTP_transf_2; 1.
DR   Pfam; PF03828; PAP_assoc; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; DNA synthesis; DNA-binding;
KW   DNA-directed DNA polymerase; Mitosis; Nucleotidyltransferase; Nucleus;
KW   Transferase.
FT   CHAIN         1    542       DNA polymerase sigma.
FT                                /FTId=PRO_0000120309.
FT   DOMAIN      178    238       PAP-associated.
FT   COMPBIAS    332    372       Ser-rich.
FT   ACT_SITE     49     49       By similarity.
SQ   SEQUENCE   542 AA;  59997 MW;  6B9FB7D11F89CB28 CRC64;
     MSPCPEEAAM RREVVKRIET VVKDLWPTAD VQIFGSFSTG LYLPTSDIDL VVFGKWERPP
     LQLLEQALRK HNVAEPCSIK VLDKATVPII KLTDQETEVK VDISFNMETG VRAAEFIKNY
     MKKYSLLPYL ILVLKQFLLQ RDLNEVFTGG ISSYSLILMA ISFLQLHPRI DARRADENLG
     MLLVEFFELY GRNFNYLKTG IRIKEGGAYI AKEEIMKAMT SGYRPSMLCI EDPLLPGNDV
     GRSSYGAMQV KQVFDYAYIV LSHAVSPLAR SYPNRDSEST LGRIIKVTQE VIDYRRRIKE
     KWGSRILPSP DLDNRIKIKE RITTCNGEQM QSREPSSPYT QRLTLSLSSP QLLSSGSSAS
     SVSSLSGSDI DSDTPPCTTP SVYQFSLQAP TTLMASLPTA LPMPSSKPQP AASRTLIMTT
     NNQTRVTIPP PTLGVAPVPC RQAGVDGTTS LKAVHSVTSP AIPSASPNPL SSPHLYHKQH
     NGMKLSMKGS HNHTQGGGYS SVGSGAVRPP VGNRGHHQYN RTGWRRKKHA HTRDSLPVSL
     SR
//
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   -----------------------------------------------------------------------
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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   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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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   ERC2_MOUSE              Reviewed;         957 AA.
AC   Q6PH08; Q80U20; Q8CCP1;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 2.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=ERC protein 2;
DE   AltName: Full=CAZ-associated structural protein 1;
DE            Short=CAST1;
GN   Name=Erc2; Synonyms=Cast1, D14Ertd171e, Kiaa0378;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; 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=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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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   PARTIAL 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   [4]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   MEDLINE=22153387; PubMed=12163476; DOI=10.1083/jcb.200202083;
RA   Ohtsuka T., Takao-Rikitsu E., Inoue E., Inoue M., Takeuchi M.,
RA   Matsubara K., Deguchi-Tawarada M., Satoh K., Morimoto K.,
RA   Nakanishi H., Takai Y.;
RT   "Cast: a novel protein of the cytomatrix at the active zone of
RT   synapses that forms a ternary complex with RIM1 and Munc13-1.";
RL   J. Cell Biol. 158:577-590(2002).
RN   [5]
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).
CC   -!- FUNCTION: 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 together with
CC       BSN. May recruit liprin-alpha proteins to the CAZ.
CC   -!- SUBUNIT: Interacts with BSN, ERC1, PPFIA1, PPFIA2, PPFIA3 and
CC       PPFIA4. Interacts through its C-terminus with the PDZ domain of
CC       RIMS1. Part of a complex consisting of ERC2, RIMS1 and UNC13A.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell junction, synapse. Cell
CC       junction, synapse, synaptosome. Cytoplasm, cytoskeleton.
CC       Note=Localized to the active zone of presynaptic density.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q6PH08-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PH08-2; Sequence=VSP_012306, VSP_011467;
CC         Note=Incomplete sequence;
CC       Name=3;
CC         IsoId=Q6PH08-3; Sequence=VSP_011469, VSP_011470;
CC       Name=4;
CC         IsoId=Q6PH08-4; Sequence=VSP_011466, VSP_011468, VSP_011471;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed throughout the central nervous
CC       system, including hippocampus, cortex, cerebellum and olfactory
CC       bulb.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC056760; AAH56760.1; -; mRNA.
DR   EMBL; AK032385; BAC27848.1; -; mRNA.
DR   EMBL; AK122265; BAC65547.1; -; mRNA.
DR   IPI; IPI00228623; -.
DR   IPI; IPI00420931; -.
DR   IPI; IPI00460558; -.
DR   IPI; IPI00460559; -.
DR   RefSeq; NP_808482.2; NM_177814.4.
DR   UniGene; Mm.318004; -.
DR   ProteinModelPortal; Q6PH08; -.
DR   SMR; Q6PH08; 138-170.
DR   STRING; Q6PH08; -.
DR   PhosphoSite; Q6PH08; -.
DR   PRIDE; Q6PH08; -.
DR   Ensembl; ENSMUST00000079438; ENSMUSP00000078408; ENSMUSG00000040640.
DR   Ensembl; ENSMUST00000090302; ENSMUSP00000087773; ENSMUSG00000040640.
DR   Ensembl; ENSMUST00000100776; ENSMUSP00000098339; ENSMUSG00000040640.
DR   Ensembl; ENSMUST00000112283; ENSMUSP00000107902; ENSMUSG00000040640.
DR   GeneID; 238988; -.
DR   KEGG; mmu:238988; -.
DR   UCSC; uc007sty.1; mouse.
DR   UCSC; uc007sua.1; mouse.
DR   CTD; 238988; -.
DR   MGI; MGI:1098749; Erc2.
DR   GeneTree; ENSGT00390000015969; -.
DR   HOVERGEN; HBG051496; -.
DR   OMA; MYNPAHN; -.
DR   OrthoDB; EOG4FTW00; -.
DR   ArrayExpress; Q6PH08; -.
DR   Bgee; Q6PH08; -.
DR   CleanEx; MM_ERC2; -.
DR   Genevestigator; Q6PH08; -.
DR   GermOnline; ENSMUSG00000040640; 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:0030426; C:growth cone; ISS:UniProtKB.
DR   GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
DR   GO; GO:0019717; C:synaptosome; IEA:UniProtKB-SubCell.
DR   InterPro; IPR019323; CAZ_cplx_RIM-bd_prot.
DR   Pfam; PF10174; Cast; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Phosphoprotein; Synapse; Synaptosome.
FT   CHAIN         1    957       ERC protein 2.
FT                                /FTId=PRO_0000087003.
FT   COILED      140    917       Potential.
FT   COMPBIAS     35     41       Poly-Gly.
FT   COMPBIAS    129    133       Poly-His.
FT   COMPBIAS    879    882       Poly-Lys.
FT   COMPBIAS    920    932       Poly-His.
FT   MOD_RES      14     14       Phosphoserine.
FT   MOD_RES     187    187       Phosphoserine (By similarity).
FT   VAR_SEQ       1    325       Missing (in isoform 2).
FT                                /FTId=VSP_012306.
FT   VAR_SEQ     219    219       Q -> QLLDARRTK (in isoform 4).
FT                                /FTId=VSP_011466.
FT   VAR_SEQ     326    358       NERTRRMAEAESQVSHLEVILDQKEKENIHLRE -> LPKC
FT                                RGCTEMALNRSVQTCFCSKMPCEQQICSH (in isoform
FT                                2).
FT                                /FTId=VSP_011467.
FT   VAR_SEQ     493    515       DALRLRLEEKESFLNKKTKQLQD -> RHLLRYWRAGALSH
FT                                IQCCSWETS (in isoform 4).
FT                                /FTId=VSP_011468.
FT   VAR_SEQ     516    957       Missing (in isoform 4).
FT                                /FTId=VSP_011471.
FT   VAR_SEQ     752    755       Missing (in isoform 3).
FT                                /FTId=VSP_011469.
FT   VAR_SEQ     950    957       DDEEGIWA -> LSEGLDKRIAQHCSSILIIYCSLALLTIH
FT                                QRRPAVAAGLKGRGVFAFTFLLNSVLLD (in isoform
FT                                3).
FT                                /FTId=VSP_011470.
SQ   SEQUENCE   957 AA;  110639 MW;  9476977763320323 CRC64;
     MYGSARTISN LEGSPSRSPR LPRSPRLGHR RTSSGGGGGT GKTLSMENIQ SLNAAYATSG
     PMYLSDHEGV ASTTYPKGTM TLGRATNRAV YGGRVTAMGS SPNIASAGLS HTDVLSYTDQ
     HGGLSGSSHH HHHQVPSMLR QVRDSTMLDL QAQLKELQRE NDLLRKELDI KDSKLGSSMN
     SIKTFWSPEL KKERVLRKEE AARMSVLKEQ MRVSHEENQH LQLTIQALQD ELRTQRDLNH
     LLQQESGNRG AEHFTIELTE ENFRRLQAEH DRQAKELFLL RKTLEEMELR IETQKQTLNA
     RDESIKKLLE MLQSKGLPSK SLEDDNERTR RMAEAESQVS HLEVILDQKE KENIHLREEL
     HRRSQLQPEP AKTKALQTVI EMKDTKIASL ERNIRDLEDE VQMLKANGVL NTEDREEEIK
     QIEVYKSHSK FMKTKIDQLK QELSKKESEL LALQTKLETL SNQNSDCKQH IEVLKESLTA
     KEQRAAILQT EVDALRLRLE EKESFLNKKT KQLQDLTEEK GTLAGEIRDM KDMLEVKERK
     INVLQKKIEN LQEQLRDKDK QLTNLKDRVK SLQTDSSNTD TALATLEEAL SEKERIIERL
     KEQRERDDRE RLEEIESFRK ENKDLKEKVN ALQAELTEKE SSLIDLKEHA SSLASAGLKR
     DSKLKSLEIA IEQKKEECNK LEAQLKKAHN 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   NFRKB_MOUSE             Reviewed;        1296 AA.
AC   Q6PIJ4; Q8BWV5; Q8K0X6;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Nuclear factor related to kappa-B-binding protein;
DE   AltName: Full=DNA-binding protein R kappa-B;
GN   Name=Nfrkb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; 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=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, 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 504-1296.
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: Binds to the DNA consensus sequence 5'-GGGGAATCTCC-3'.
CC       Modulates the deubiquitinase activity of UCHL5 (By similarity).
CC   -!- SUBUNIT: Component of the chromatin-remodeling INO80 complex, at
CC       least composed of ACTL6A, ACTR5, ACTR8, RVBL1, RVBL2, INO80,
CC       INO80B, INO80C, INO80D and INO80E. Interacts with UCHL5 (By
CC       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 NFRKB family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC33927.1; Type=Erroneous initiation;
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DR   EMBL; BC029701; AAH29701.1; -; mRNA.
DR   EMBL; BC033595; AAH33595.1; -; mRNA.
DR   EMBL; AK049804; BAC33927.1; ALT_INIT; mRNA.
DR   IPI; IPI00274469; -.
DR   RefSeq; NP_766354.2; NM_172766.3.
DR   UniGene; Mm.238146; -.
DR   ProteinModelPortal; Q6PIJ4; -.
DR   PhosphoSite; Q6PIJ4; -.
DR   PRIDE; Q6PIJ4; -.
DR   Ensembl; ENSMUST00000086167; ENSMUSP00000083341; ENSMUSG00000042185.
DR   GeneID; 235134; -.
DR   KEGG; mmu:235134; -.
DR   UCSC; uc009orr.1; mouse.
DR   CTD; 235134; -.
DR   MGI; MGI:2442410; Nfrkb.
DR   GeneTree; ENSGT00390000016213; -.
DR   HOGENOM; HBG402942; -.
DR   HOVERGEN; HBG082022; -.
DR   InParanoid; Q6PIJ4; -.
DR   OMA; HVTSNPV; -.
DR   OrthoDB; EOG444KJZ; -.
DR   NextBio; 382524; -.
DR   ArrayExpress; Q6PIJ4; -.
DR   Bgee; Q6PIJ4; -.
DR   CleanEx; MM_NFRKB; -.
DR   Genevestigator; Q6PIJ4; -.
DR   GermOnline; ENSMUSG00000042185; Mus musculus.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Acetylation; DNA-binding; Nucleus; Phosphoprotein.
FT   CHAIN         1   1296       Nuclear factor related to kappa-B-binding
FT                                protein.
FT                                /FTId=PRO_0000227808.
FT   COMPBIAS    309    327       Lys-rich.
FT   COMPBIAS    664    671       Poly-Ala.
FT   COMPBIAS    683    796       Ser-rich.
FT   COMPBIAS    714    736       Pro-rich.
FT   COMPBIAS   1242   1268       Gln-rich.
FT   MOD_RES     176    176       Phosphoserine (By similarity).
FT   MOD_RES     178    178       Phosphoserine (By similarity).
FT   MOD_RES     226    226       Phosphoserine (By similarity).
FT   MOD_RES     228    228       Phosphoserine (By similarity).
FT   MOD_RES     298    298       Phosphoserine (By similarity).
FT   MOD_RES     351    351       Phosphoserine (By similarity).
FT   MOD_RES     376    376       Phosphoserine (By similarity).
FT   MOD_RES     796    796       Phosphoserine (By similarity).
FT   MOD_RES    1196   1196       Phosphoserine (By similarity).
FT   MOD_RES    1199   1199       Phosphothreonine (By similarity).
FT   MOD_RES    1234   1234       N6-acetyllysine (By similarity).
FT   MOD_RES    1288   1288       Phosphoserine (By similarity).
SQ   SEQUENCE   1296 AA;  138764 MW;  ED6A42FE704DED1B CRC64;
     MDSLDHMLTD PLELGPCGDG HSTGIMEDCL LGGTRVSLPE DLLEDPEIFF DVVSLSTWQE
     VLSDSQREHL QQFLPRFPAD SVEQQRELIL ALFSGENFRF GNPLHIAQKL FRDGHFNPEV
     VKYRQLCFKS QYKRYLNSQQ QYFHRLLKQI LASRSDLLEM ARRSGPALPF PHKHHSPSRS
     PEEREWRTQQ RYLKVLREVK EECGDTALSS DEEDLSSWLP SSPARSPSPA VPLRVVPTLS
     TTDMKTADKI ELGDSDLKLM LKKHHEKRKH QPDHPDLLTG DLTLSDIMTR VNAGRKGSLA
     ALYDLAVLKK KVKEKEEKKK KKIKLIKSEA EDLAEPLSST EGVPTLSQAP SPLAISSIKE
     EPLEDIKPCL GINEISSSFF SLLLEILLLE SQASLPMLED RVLDWQSSPA SSLNSWFSAA
     PNWAELVLPA LQYLAGESRA VPSSFSPFVE FKEKTQQWKL LGQSQDNEKE LAALFHLWLE
     TKDQAFCKEN EDSSDAMTPV PRVRTDYVVR PSTGEEKRVF QEQERYRYSQ PHKAFTFRMH
     GFESVVGPVK GVFDKETSLN KAREHSLLRS DRPAYVTILS LVRDAAARLP NGEGTRAEIC
     ELLKDSQFLA PDVTSTQVNT VVSGALDRLH YEKDPCVKYD IGRKLWIYLH RDRSEEEFER
     IHQAQAAAAK ARKALQQKPK PPSKVKSSNK EGSTKGLSGP SEQSQMSLSD SSMPPTPVTP
     VTPTTPALPT PISPPPVSAV NRSGSSTVSE PAQSSSGVLL VSSPTMPQLG TMLSPASIQT
     PPSSQATARV VSHSSSAGLP QVRVVAQPSL PAVSQQSVGP AQPLPQMPAG PQIRVPVTAT
     QTKVVPQAVM ATVPVKGQTA AASVQRPGPG QTGLTVTNLP AAVSPVSKTA MSSPGNSAPS
     ASTTAVIQNV TGQNIIKQVS ITGQLGVKPQ TGSSIPLTAT NFRIQGKDVL RLPPSSITTD
     AKGQTVLRIT PDMMATLAKS QVTTVKLTQD LFGAGSGTAG KGISATLHVT SNPVHAADSP
     AKAPSASVPS SAPAGTTVVK VTPDLKPTET ANSAFRLMPA LGVSVADQKG KNTVASSEAK
     PAATIRIVQG LGVMPPKAGQ TITVAAHAKQ GASVAGGSGT VHSSTVSLPS INAAVSKTVA
     VASGATSTPI SIGTGAPTVR QVPVNTTVVS TSQSGKLPTR ITVPLSVISQ PMKGKSVVTA
     PIIKGNLGAN LSGLGRNIIL TTMPAGTKLI AGNKPVSFLT AQQLQQLQQQ GQATQVRIQT
     VPASHLQQGT ASGSSKAVST VVVTTAPSPK QAPEQQ
//
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.
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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   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   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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   CTL1_MOUSE              Reviewed;         653 AA.
AC   Q6X893; Q6X894; Q8R0Y4; Q91Z29;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Choline transporter-like protein 1;
DE   AltName: Full=Solute carrier family 44 member 1;
DE   AltName: CD_antigen=CD92;
GN   Name=Slc44a1; Synonyms=Cd92, Cdw92, Ctl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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   SUBCELLULAR LOCATION, AND FUNCTION.
RC   TISSUE=Fibroblast;
RX   PubMed=15474312; DOI=10.1016/j.gene.2004.07.042;
RA   Yuan Z., Wagner L., Poloumienko A., Bakovic M.;
RT   "Identification and expression of a mouse muscle-specific CTL1 gene.";
RL   Gene 341:305-312(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 390-653 (ISOFORM 1).
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   FUNCTION, TOPOLOGY, AND SUBCELLULAR LOCATION.
RX   PubMed=19357133; DOI=10.1096/fj.08-121491;
RA   Michel V., Bakovic M.;
RT   "The solute carrier 44A1 is a mitochondrial protein and mediates
RT   choline transport.";
RL   FASEB J. 23:2749-2758(2009).
CC   -!- FUNCTION: Choline transporter. May be involved in membrane
CC       synthesis and myelin production.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Mitochondrion outer membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=A;
CC         IsoId=Q6X893-1; Sequence=Displayed;
CC       Name=2; Synonyms=B;
CC         IsoId=Q6X893-2; Sequence=VSP_015428;
CC   -!- TISSUE SPECIFICITY: Specifically abundant in skeletal muscle (at
CC       protein level).
CC   -!- SIMILARITY: Belongs to the CTL (choline transporter-like) family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH25941.1; 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; AY249865; AAP81042.1; -; mRNA.
DR   EMBL; AY249866; AAP81043.1; -; mRNA.
DR   EMBL; BC010258; AAH10258.1; -; mRNA.
DR   EMBL; BC025941; AAH25941.1; ALT_INIT; mRNA.
DR   IPI; IPI00421237; -.
DR   IPI; IPI00648678; -.
DR   UniGene; Mm.270088; -.
DR   STRING; Q6X893; -.
DR   TCDB; 2.A.92.1.1; choline transporter-like (CTL) family.
DR   PhosphoSite; Q6X893; -.
DR   PRIDE; Q6X893; -.
DR   Ensembl; ENSMUST00000102911; ENSMUSP00000099975; ENSMUSG00000028412.
DR   UCSC; uc008swz.1; mouse.
DR   MGI; MGI:2140592; Slc44a1.
DR   GeneTree; ENSGT00550000074521; -.
DR   HOVERGEN; HBG080361; -.
DR   OrthoDB; EOG4W9J3G; -.
DR   NextBio; 354424; -.
DR   ArrayExpress; Q6X893; -.
DR   Bgee; Q6X893; -.
DR   CleanEx; MM_SLC44A1; -.
DR   Genevestigator; Q6X893; -.
DR   GO; GO:0016021; C:integral to 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:0015220; F:choline transmembrane transporter activity; IDA:MGI.
DR   InterPro; IPR007603; Choline_transptr-like.
DR   PANTHER; PTHR12385; DUF580; 1.
DR   Pfam; PF04515; DUF580; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    653       Choline transporter-like protein 1.
FT                                /FTId=PRO_0000191713.
FT   TOPO_DOM      1     29       Cytoplasmic (Potential).
FT   TRANSMEM     30     50       Helical; (Potential).
FT   TOPO_DOM     51    211       Mitochondrial intermembrane (Potential).
FT   TRANSMEM    212    232       Helical; (Potential).
FT   TOPO_DOM    233    237       Cytoplasmic (Potential).
FT   TRANSMEM    238    258       Helical; (Potential).
FT   TOPO_DOM    259    287       Mitochondrial intermembrane (Potential).
FT   TRANSMEM    288    308       Helical; (Potential).
FT   TOPO_DOM    309    314       Cytoplasmic (Potential).
FT   TRANSMEM    315    335       Helical; (Potential).
FT   TOPO_DOM    336    337       Mitochondrial intermembrane (Potential).
FT   TRANSMEM    338    358       Helical; (Potential).
FT   TOPO_DOM    359    379       Cytoplasmic (Potential).
FT   TRANSMEM    380    400       Helical; (Potential).
FT   TOPO_DOM    401    536       Mitochondrial intermembrane (Potential).
FT   TRANSMEM    537    557       Helical; (Potential).
FT   TOPO_DOM    558    565       Cytoplasmic (Potential).
FT   TRANSMEM    566    586       Helical; (Potential).
FT   TOPO_DOM    587    653       Mitochondrial intermembrane (Potential).
FT   COMPBIAS    473    491       Cys-rich.
FT   VAR_SEQ     650    653       LRKR -> VGSEEEAAALHDFPFHFFSVCVFTDCTSSGEAL
FT                                VVCITQDMLLFLFACLPITWMAEVLSQLRLPSVKVS (in
FT                                isoform 2).
FT                                /FTId=VSP_015428.
FT   CONFLICT    426    426       L -> P (in Ref. 2; AAH25941).
FT   CONFLICT    439    439       F -> L (in Ref. 2; AAH25941).
FT   CONFLICT    510    510       L -> F (in Ref. 2; AAH25941).
SQ   SEQUENCE   653 AA;  73083 MW;  3857DA8BE428EFF5 CRC64;
     MGCCSSASAA QSSKREWKPL EDRSCTDIPW LLLFVLFCIG MGFICGFSVA TGAAARLVSG
     YDSYGNICGQ RNAKLEAIPN SGLDHTHRKY VFFLDPCNLD LINRKIKSIA LCVAACPRQE
     LKTLSDVQKF AEINGSALCS YNIKPSEYTL TSKSSGFCPK LPVPASAPIP FFHRCAPVNI
     SCYAKFAEAL ITFVSDNSVL HRLISGVMTS KEIILGLCLL SLVLSMILMV IIRYISRVLV
     WILTVLVILG SLGGTGVLWW LYAKQRRSPK EAVIPEQLQI AEDNLRALLI YAISATVFTV
     ILFLIMLVMR KRVALTIALF HVAGKVFIHL PLLVFQPFWT FFALVLFWAY WIMTLLFLGT
     TGSAVQNEQG FVEYKISGPL QYMWWYHVVG LIWISEFILA CQQMTVAGAV VTYYFTRDKR
     NLPFTLILAS VNRLIRYHFG TVAKGSFIIT LVKIPRMVLM YIHSQLKGKE NACARCMLKS
     CICCLWCLEK CLSYLNQNAY TATAINSTNL CTSAKDAFVI LVENALRVAA INTVGDFMLF
     LGKVLIVCST GLAGIMLLNY QQDYTVWVLP LIIVCLFAFL VAHCFLSIYE MVVDVLFLCF
     AIDTKYNDGS PGREFYMDKV LMEFVENSRK AMKEAGKGGA ADARELKPML RKR
//
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.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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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   PF21A_MOUSE             Reviewed;         659 AA.
AC   Q6ZPK0; Q6XVG0; Q80Z33; Q8CAZ4; Q8VEC8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=PHD finger protein 21A;
DE   AltName: Full=BHC80a;
DE   AltName: Full=BRAF35-HDAC complex protein BHC80;
DE            Short=mBHC80;
GN   Name=Phf21a; Synonyms=Bhc80, Kiaa1696, Pftf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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; 6; 7; 8 AND
RP   9), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=15325272; DOI=10.1016/j.bbrc.2004.07.163;
RA   Iwase S., Januma A., Miyamoto K., Shono N., Honda A., Yanagisawa J.,
RA   Baba T.;
RT   "Characterization of BHC80 in BRAF-HDAC complex, involved in neuron-
RT   specific gene repression.";
RL   Biochem. Biophys. Res. Commun. 322:601-608(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] (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 MRNA] (ISOFORM 4).
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 119-303 (ISOFORM 3).
RC   STRAIN=C57BL/6;
RA   Herrera L., Ottolenghi C., Forabosco A., Schlessinger D.;
RT   "Mouse ovary and testis gene cohorts and RNA and protein developmental
RT   markers from microarray expression profiling.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the BHC complex, a corepressor complex that
CC       represses transcription of neuron-specific genes in non-neuronal
CC       cells. The BHC complex is recruited at RE1/NRSE sites by REST and
CC       acts by deacetylating and demethylating specific sites on
CC       histones, thereby acting as a chromatin modifier. In the BHC
CC       complex, it may act as a scaffold. Inhibits KDM1A-mediated
CC       demethylation of 'Lys-4' of histone H3 in vitro, suggesting a role
CC       in demethylation regulation (By similarity).
CC   -!- SUBUNIT: 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. In the complex, it interacts directly with
CC       HDAC1, HDAC2, HMG20B/BRAF35, KDM1A and RCOR1/CoREST (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=9;
CC       Name=1;
CC         IsoId=Q6ZPK0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZPK0-2; Sequence=VSP_017451, VSP_017453;
CC       Name=3; Synonyms=BHC80-6(AIF2+5);
CC         IsoId=Q6ZPK0-3; Sequence=VSP_017452;
CC       Name=4;
CC         IsoId=Q6ZPK0-4; Sequence=VSP_017450, VSP_017453, VSP_017454;
CC       Name=5; Synonyms=BHC80-1(AIF1+3);
CC         IsoId=Q6ZPK0-5; Sequence=VSP_017450, VSP_017454;
CC       Name=6; Synonyms=BHC80-4(AIF2+3);
CC         IsoId=Q6ZPK0-6; Sequence=VSP_017452, VSP_017454;
CC       Name=7; Synonyms=BHC80-2(AIF1+4);
CC         IsoId=Q6ZPK0-7; Sequence=VSP_017450, VSP_017455;
CC       Name=8; Synonyms=BHC80-5(AIF2+4);
CC         IsoId=Q6ZPK0-8; Sequence=VSP_017452, VSP_017455;
CC       Name=9; Synonyms=BHC80-3(AIF1+5);
CC         IsoId=Q6ZPK0-9; Sequence=VSP_017450;
CC   -!- TISSUE SPECIFICITY: Expressed in the brain and testis. Weakly or
CC       not expressed in other tissues tested. Localized throughout the
CC       central nervous system (CNS) in brain, including the cerebellum,
CC       hippocampus, and cortex. Notably present in neuronal cells of
CC       granular cell layer and dentate gyrus in cerebellum and
CC       hippocampus, respectively. In the seminiferous tubules, the
CC       signals it is present strongly in spermatocytes, and weakly in
CC       spermatogonia and round spermatids. In some cases, it is also
CC       observed solely in spermatocytes (at protein level).
CC   -!- SIMILARITY: Contains 1 A.T hook DNA-binding domain.
CC   -!- SIMILARITY: Contains 1 PHD-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98234.1; Type=Erroneous initiation;
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DR   EMBL; AB105178; BAC65327.1; -; mRNA.
DR   EMBL; AK129424; BAC98234.1; ALT_INIT; Transcribed_RNA.
DR   EMBL; AK037174; BAC29735.1; -; mRNA.
DR   EMBL; BC019181; AAH19181.1; -; mRNA.
DR   EMBL; AY206982; AAP43962.1; -; mRNA.
DR   IPI; IPI00124469; -.
DR   IPI; IPI00228265; -.
DR   IPI; IPI00453806; -.
DR   IPI; IPI00742280; -.
DR   IPI; IPI00742299; -.
DR   IPI; IPI00742330; -.
DR   IPI; IPI00742344; -.
DR   IPI; IPI00742352; -.
DR   IPI; IPI00742439; -.
DR   RefSeq; NP_001103161.1; NM_001109691.1.
DR   RefSeq; NP_620094.2; NM_138755.2.
DR   UniGene; Mm.330408; -.
DR   UniGene; Mm.450689; -.
DR   ProteinModelPortal; Q6ZPK0; -.
DR   SMR; Q6ZPK0; 466-523.
DR   STRING; Q6ZPK0; -.
DR   PhosphoSite; Q6ZPK0; -.
DR   PRIDE; Q6ZPK0; -.
DR   Ensembl; ENSMUST00000068702; ENSMUSP00000070649; ENSMUSG00000058318.
DR   Ensembl; ENSMUST00000111290; ENSMUSP00000106921; ENSMUSG00000058318.
DR   GeneID; 192285; -.
DR   KEGG; mmu:192285; -.
DR   UCSC; uc008kxh.1; mouse.
DR   UCSC; uc008kxi.1; mouse.
DR   CTD; 192285; -.
DR   MGI; MGI:2384756; Phf21a.
DR   GeneTree; ENSGT00530000063984; -.
DR   HOVERGEN; HBG080293; -.
DR   NextBio; 371282; -.
DR   Bgee; Q6ZPK0; -.
DR   CleanEx; MM_PHF21A; -.
DR   Genevestigator; Q6ZPK0; -.
DR   GermOnline; ENSMUSG00000058318; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
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; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; 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:0001967; P:suckling behavior; IMP:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR017956; AT_hook_DNA-bd_motif.
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; 1.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00384; AT_hook; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00184; RING; 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   Alternative splicing; Chromatin regulator; Coiled coil; Metal-binding;
KW   Nucleus; Phosphoprotein; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    659       PHD finger protein 21A.
FT                                /FTId=PRO_0000226768.
FT   DNA_BIND    405    417       A.T hook (By similarity).
FT   ZN_FING     468    515       PHD-type.
FT   COILED      538    582       Potential.
FT   COMPBIAS      4    116       Gln-rich.
FT   MOD_RES     424    424       Phosphothreonine (By similarity).
FT   MOD_RES     427    427       Phosphoserine (By similarity).
FT   MOD_RES     435    435       Phosphoserine (By similarity).
FT   VAR_SEQ     128    212       Missing (in isoform 4, isoform 5, isoform
FT                                7 and isoform 9).
FT                                /FTId=VSP_017450.
FT   VAR_SEQ     129    212       Missing (in isoform 2).
FT                                /FTId=VSP_017451.
FT   VAR_SEQ     129    129       Missing (in isoform 3, isoform 6 and
FT                                isoform 8).
FT                                /FTId=VSP_017452.
FT   VAR_SEQ     341    352       LNPTQKQRKNKQ -> TVKSHPEAEEKQAESRTVTPPAAPK
FT                                PKREENPQKLAFMVSL (in isoform 2 and
FT                                isoform 4).
FT                                /FTId=VSP_017453.
FT   VAR_SEQ     409    463       GRPPKYNAVLGFGALTPTSPPSSHPDSPENEKTETTFTFPA
FT                                PVQPVSLPSPTSTD -> ANEEHWPK (in isoform 4,
FT                                isoform 5 and isoform 6).
FT                                /FTId=VSP_017454.
FT   VAR_SEQ     409    452       GRPPKYNAVLGFGALTPTSPPSSHPDSPENEKTETTFTFPA
FT                                PVQ -> ANEEHWPK (in isoform 7 and isoform
FT                                8).
FT                                /FTId=VSP_017455.
FT   CONFLICT    325    325       A -> P (in Ref. 1; BAC65327 and 3;
FT                                BAC29735).
SQ   SEQUENCE   659 AA;  72521 MW;  E0EECD3F02CCFF78 CRC64;
     MELQTLQEAL KVEIQVHQKL VAQMKQDPQN ADLKKQLHEL QAKITALSEK QKRVVEQLRK
     NLIVKQEQPD KFQIQPLSQS ENKLQTAQQQ PLQPLQQQQP QQPQQQQQQQ QQHAQQSAAA
     PPSLTASQKT VTTASMITTK TLPLVLKAAT ATMPASVVGQ RPTIAMVTAI NSQKAVLSTD
     VQNTPVNLQT SSKVTGPGAE AVQIVAKNTV TLQVQATPPQ PIKVPQFIPP PRLTPRPNFL
     PQVRPKPVAQ NNIPIAPAPP PMLAAPQLIQ RPVMLTKFTP TTLPTSQNSI HPVRVVNGQT
     ATIAKTFPMA QLTSIVIATP GTRLAGPQTV QLSKPSLEKQ LNPTQKQRKN KQGLVTHDHL
     EEIQSKRQER KRRTTANPVY SGAVFEPERK KSAVTYLNST MHPGTRKRGR PPKYNAVLGF
     GALTPTSPPS SHPDSPENEK TETTFTFPAP VQPVSLPSPT STDGDIHEDF CSVCRKSGQL
     LMCDTCSRVY HLDCLEPPLK TIPKGMWICP RCQDQMLKKE EAIPWPGTLA IVHSYIAYKA
     AKEEEKQKLL KWSSDLKQER EQLEQKVKEL SSSISKCMEM KSSILARQKE MRSSLDKVKR
     LIRLVHGVDL CRPVDSEATA GALSNGPDCT PPANAASTPA PSPSSQSCTA NCNQGEETK
//
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   KDM3B_MOUSE             Reviewed;        1562 AA.
AC   Q6ZPY7; Q2VPQ5; Q5U5V7; Q6P9K3; Q8CCE2; Q8K2A5; Q9CU57;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Lysine-specific demethylase 3B;
DE            EC=1.14.11.-;
DE   AltName: Full=JmjC domain-containing histone demethylation protein 2B;
DE   AltName: Full=Jumonji domain-containing protein 1B;
GN   Name=Kdm3b; Synonyms=Jhdm2b, Jmjd1b, Kiaa1082;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; 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] OF 574-1562 (ISOFORM 1).
RC   STRAIN=C57BL/6, and Czech II; 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1119-1562.
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., 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 demethylase that specifically demethylates 'Lys-
CC       9' of histone H3, thereby playing a central role in histone code.
CC       Demethylation of Lys residue generates formaldehyde and succinate
CC       May have tumor suppressor activity (By similarity).
CC   -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6ZPY7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZPY7-2; Sequence=VSP_018301, VSP_018302;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate
CC       the association with nuclear receptors (By similarity).
CC   -!- SIMILARITY: Belongs to the JHDM2 histone demethylase family.
CC   -!- SIMILARITY: Contains 1 JmjC domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH38376.1; Type=Frameshift; Positions=1555;
CC       Sequence=BAC98091.1; Type=Erroneous initiation;
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK129281; BAC98091.1; ALT_INIT; mRNA.
DR   EMBL; BC031981; AAH31981.1; -; mRNA.
DR   EMBL; BC038376; AAH38376.1; ALT_FRAME; mRNA.
DR   EMBL; BC060727; AAH60727.1; -; mRNA.
DR   EMBL; BC108415; AAI08416.1; -; mRNA.
DR   EMBL; AK018027; BAB31043.1; -; mRNA.
DR   EMBL; AK033343; BAC28239.1; -; mRNA.
DR   IPI; IPI00664808; -.
DR   IPI; IPI00757477; -.
DR   UniGene; Mm.479894; -.
DR   ProteinModelPortal; Q6ZPY7; -.
DR   STRING; Q6ZPY7; -.
DR   PhosphoSite; Q6ZPY7; -.
DR   PRIDE; Q6ZPY7; -.
DR   Ensembl; ENSMUST00000091949; ENSMUSP00000089570; ENSMUSG00000038773.
DR   Ensembl; ENSMUST00000091950; ENSMUSP00000089571; ENSMUSG00000038773.
DR   UCSC; uc008elp.1; mouse.
DR   UCSC; uc008elq.1; mouse.
DR   MGI; MGI:1923356; Kdm3b.
DR   GeneTree; ENSGT00530000063039; -.
DR   OrthoDB; EOG4W9J32; -.
DR   ArrayExpress; Q6ZPY7; -.
DR   Bgee; Q6ZPY7; -.
DR   CleanEx; MM_JMJD1B; -.
DR   Genevestigator; Q6ZPY7; -.
DR   GermOnline; ENSMUSG00000038773; 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: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:0016568; P:chromatin modification; IEA:UniProtKB-KW.
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; IPR013129; TF_JmjC.
DR   InterPro; IPR003347; TF_JmjC_AAH.
DR   Pfam; PF02373; JmjC; 1.
DR   SMART; SM00558; JmjC; 1.
DR   PROSITE; PS51184; JMJC; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromatin regulator; Dioxygenase; Iron;
KW   Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1   1562       Lysine-specific demethylase 3B.
FT                                /FTId=PRO_0000234374.
FT   DOMAIN     1299   1522       JmjC.
FT   ZN_FING     832    857       C6-type (Potential).
FT   MOTIF      1094   1098       LXXLL motif.
FT   COMPBIAS    255    545       Ser-rich.
FT   METAL      1361   1361       Iron; catalytic (By similarity).
FT   METAL      1363   1363       Iron; catalytic (By similarity).
FT   METAL      1490   1490       Iron; catalytic (By similarity).
FT   MOD_RES     567    567       Phosphoserine (By similarity).
FT   MOD_RES     574    574       Phosphoserine (By similarity).
FT   MOD_RES     599    599       Phosphoserine.
FT   VAR_SEQ    1070   1124       LTPKLFNSLLLGPTASNSKTEGSSLRDLLHSGPGKLPQTPL
FT                                DTGIPFPPVFSSSS -> HVTSDLAHPRRWGCSPSRTLHEH
FT                                RSLQDPGRAHCFSQEAPGLGNVYLVKNRFVVK (in
FT                                isoform 2).
FT                                /FTId=VSP_018301.
FT   VAR_SEQ    1125   1562       Missing (in isoform 2).
FT                                /FTId=VSP_018302.
FT   CONFLICT   1126   1126       V -> G (in Ref. 2; AAH31981).
FT   CONFLICT   1369   1370       NV -> SL (in Ref. 3; BAB31043).
FT   CONFLICT   1545   1545       V -> G (in Ref. 3; BAB31043).
SQ   SEQUENCE   1562 AA;  170875 MW;  4F2D7818104B50BE CRC64;
     MADAAASPVG KRLLLLFADP TASASASAPT AAAVVSGDPG PALRTRAWRA GTVRAMSGAV
     PQDLAIFVEF DGCNWKQHSW VKVHAEDVLA LLLEGSLVWA PRKDPVLLQG TRVPVAQWPA
     LTFTPLVDKL GLGSVVPVEY LVDRELRFLS DANGMHLFQM GTDVQNQILL EHAALRETVN
     ALISDQKLQE IFSRGPYSVQ GHRVKVYQPE GEEVWLCGVV SRQDSVTRLM EVSITETGEV
     KSVDPRLTHV MLMDSSTPQS ENSRNSSLAS SGFGVSLSSL SQPLTFGSGR SQSNGVLATD
     NKPLGFSFSC SSASESQKDS DLSKNLFFQC MSQNVPSTNY LSRVSESVAD DSSSRDSFTQ
     SLESLTSGLC KGRSVLGADT QPGPKAGSSV DRKVPAESMP TLTPAFPRSL LNTRTPENHE
     NLFLQPPKLS REEPSNPFLA FVEKVEHSPF SSFVSQASGS SSSATSVTSK ATASWPESHS
     SAESAPLAKK KPLFITTDSS KLVSGVLGSA LSTGSPSLSA VGNGRSSSPT NSLTQPIEMP
     TLSSSPTEER PTVGPGQQDN PLLKTFSTVF GRHSGSFLSA PAEFAQENKA PFEAVKRFSL
     DERSLACRQD SDSSTNSDLS DLSDSEEQLQ AKSGLKGIPE HLMGKLGPNG ERSAELLLGK
     GKGKQAPKGR PRTAPLKVGQ SVLKDVSKVR KLKQSGEPFL QDGSCINVAP HLHKCRECRL
     ERYRKFKEQE QDDSTVACRF FHFRRLVFTR KGVLRVEGFL SPQQSDPDAM NLWIPSSSLA
     EGIDLETSKY ILANVGDQFC QLVMSEKEAM MMVEPHQKVA WKRAVRGVRE MCDVCETTLF
     NIHWVCRKCG FGVCLDCYRL RKSRPRSETE EMGDEEVFSW LKCAKGQSHE PENLMPTQII
     PGTALYNIGD MVHAARGKWG IKANCPCISR QSKSVLRPAV TNGISQLPSV TPSASSGNET
     TFSSGGGAAA VTNPEPDQVP KGAGTDGRSE EPLKAEGSAS NSNSELKAIR PPCPDTAPPS
     SALHWLADLA TQKAKEETKD AGSLRSVLNK ESHSPFGLDS FNSTAKVSPL TPKLFNSLLL
     GPTASNSKTE GSSLRDLLHS GPGKLPQTPL DTGIPFPPVF SSSSAVAKSK ASLPDFLDHI
     IASVVENKKT SDPSKRSCNL TDTQKEVKEM AMGLNVLDPH TSHSWLCDGR LLCLHDPSNK
     NNWKIFRECW KQGQPVLVSG VHKKLKSELW KPEAFSQEFG DQDVDLVNCR NCAIISDVKV
     RDFWDGFEII CKRLRSEDGQ PMVLKLKDWP PGEDFRDMMP TRFEDLMENL PLPEYTKRDG
     RLNLASRLPS YFVRPDLGPK MYNAYGLITA EDRRVGTTNL HLDVSDAVNV MVYVGIPVGE
     GAHDEEVLKT IDEGDADEVT KQRIHDGKEK PGALWHIYAA KDAEKIRELL RKVGEEQGQE
     NPPDHDPIHD QSWYLDQILR KRLFEEYGVQ GWAIVQFLGD AVFIPAGAPH QVHNLYSCIK
     VAEDFVSPEH VKHCFRLTQE FRHLSNTHTN HEDKLQVKNI IYHAVKDAVG TLKAHESKLA
     RS
//
ID   CNOT1_MOUSE             Reviewed;        2375 AA.
AC   Q6ZQ08; B2RY28; Q3UPB7; Q8BSB4; Q8BXB2; Q8C0H2; Q8K3D8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   08-MAR-2011, entry version 44.
DE   RecName: Full=CCR4-NOT transcription complex subunit 1;
DE   AltName: Full=CCR4-associated factor 1;
GN   Name=Cnot1; Synonyms=Kiaa1007;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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 1-2305 (ISOFORM 3),
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 203-847 (ISOFORM 2),
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 533-1302 (ISOFORM 4), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1819-2375 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Head, 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 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1247-2375 (ISOFORM 1/2).
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 918-2375 (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   [5]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Belongs to the CCR4-NOT complex that functions as
CC       general transcription regulation complex. Acts as a
CC       transcriptional repressor. Represses the ligand-dependent
CC       transcriptional activation by nuclear receptors (By similarity).
CC   -!- SUBUNIT: Subunit of the CCR4-NOT core complex that contains CNOT1,
CC       CNOT2, CNOT3, CNOT4 and CNOT8. Interacts in a ligand-dependent
CC       fashion with ESR1 and RXRA (By similarity).
CC   -!- INTERACTION:
CC       Q8VEG6:Cnot6l; NbExp=1; IntAct=EBI-2104684, EBI-2104661;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q6ZQ08-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZQ08-2; Sequence=VSP_030565, VSP_030566;
CC       Name=3;
CC         IsoId=Q6ZQ08-3; Sequence=VSP_030564;
CC       Name=4;
CC         IsoId=Q6ZQ08-4; Sequence=VSP_030565;
CC   -!- SIMILARITY: Belongs to the CNOT1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27364.1; Type=Erroneous initiation;
CC       Sequence=BAC28830.1; Type=Erroneous initiation;
CC       Sequence=BAE25479.1; Type=Erroneous initiation;
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DR   EMBL; AC113951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC127300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK031357; BAC27364.1; ALT_INIT; mRNA.
DR   EMBL; AK034776; BAC28830.1; ALT_INIT; mRNA.
DR   EMBL; AK048177; BAC33267.1; -; mRNA.
DR   EMBL; AK143651; BAE25479.1; ALT_INIT; mRNA.
DR   EMBL; BC018281; AAH18281.2; -; mRNA.
DR   EMBL; BC158073; AAI58074.1; -; mRNA.
DR   EMBL; AK129258; BAC98068.2; -; Transcribed_RNA.
DR   IPI; IPI00672703; -.
DR   IPI; IPI00673465; -.
DR   IPI; IPI00880243; -.
DR   IPI; IPI00881912; -.
DR   RefSeq; NP_694804.2; NM_153164.2.
DR   RefSeq; NP_835179.1; NM_178078.1.
DR   UniGene; Mm.259220; -.
DR   ProteinModelPortal; Q6ZQ08; -.
DR   IntAct; Q6ZQ08; 1.
DR   STRING; Q6ZQ08; -.
DR   PRIDE; Q6ZQ08; -.
DR   Ensembl; ENSMUST00000068452; ENSMUSP00000063565; ENSMUSG00000036550.
DR   Ensembl; ENSMUST00000098473; ENSMUSP00000096073; ENSMUSG00000036550.
DR   Ensembl; ENSMUST00000109467; ENSMUSP00000105093; ENSMUSG00000036550.
DR   GeneID; 234594; -.
DR   KEGG; mmu:234594; -.
DR   CTD; 234594; -.
DR   MGI; MGI:2442402; Cnot1.
DR   GeneTree; ENSGT00390000014869; -.
DR   HOVERGEN; HBG060834; -.
DR   OrthoDB; EOG495ZQV; -.
DR   NextBio; 382234; -.
DR   ArrayExpress; Q6ZQ08; -.
DR   Bgee; Q6ZQ08; -.
DR   CleanEx; MM_CNOT1; -.
DR   Genevestigator; Q6ZQ08; -.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007196; Not1.
DR   Pfam; PF04054; Not1; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   2375       CCR4-NOT transcription complex subunit 1.
FT                                /FTId=PRO_0000315542.
FT   COMPBIAS   1332   1349       Thr-rich.
FT   MOD_RES    1932   1932       Phosphotyrosine (By similarity).
FT   VAR_SEQ       1   1881       Missing (in isoform 3).
FT                                /FTId=VSP_030564.
FT   VAR_SEQ     777    777       P -> PV (in isoform 2 and isoform 4).
FT                                /FTId=VSP_030565.
FT   VAR_SEQ     821    826       SKMKPS -> T (in isoform 2).
FT                                /FTId=VSP_030566.
FT   CONFLICT   2089   2089       I -> F (in Ref. 3; AAH18281).
FT   CONFLICT   2203   2203       N -> S (in Ref. 2; BAC33267).
FT   CONFLICT   2233   2233       G -> D (in Ref. 2; BAC27364).
SQ   SEQUENCE   2375 AA;  266808 MW;  7771515027BA4B60 CRC64;
     MNLDSLSLAL SQISYLVDNL TKKNYRASQQ EIQHIVNRHG PEADRHLLRC LFSHVDFSGD
     GKSSGKDFHQ TQFLIQECAS LITKPNFIST LSYAIDNPLH YQKSLKPAPH LFAQLSKVLK
     LSKVQEVIFG LALLNSSSPD LRGFAAQFIK QKLPDLLRSY IDADVSGNQE GGFQDIAIEV
     LHLLLSHLLF GQKGAFGVGQ EQIDAFLKTL RRDFPQERCP VVLAPLLYPE KRDILMDRIL
     PDSGGVAKTM MESSLADFMQ EVGYGFCASI EECRNIIMQF GVREVTAAQV ARVLGMMART
     HSGLTDGIPL QSISAPGSGI WSDGKDKSEG AQAHTWNVEV LIDVLKELNP SLNFKEVTYE
     LDHPGFQIRD SKGLHNVVYG IQRGLGMEVF PVDFIYRPWK HAEGQLSFIQ HSLINPEVFC
     FADYPCHTVA TDILKAPPED DNREIATWKS LDLIESLLRL AEVGQYEQVK QLFSFPIKHC
     PDMLVLALLQ INTSWHTLRH ELISTLMPIF LGNHPNSAII LHYAWHGQGQ SPSIRQLIMH
     AMAEWYMRGE QYDQAKLSRI LDVAQDLKAL SMLLNGTPFA FVIDLAALAS RREYLKLDKW
     LTDKIREHGE PFIQACMTFL KRRCPSILGG LAPEKDQPKS AQLPAETLAT MLACLQACAG
     SVSQELSETI LTMVANCSNV MNKARQPPPG VMPKGRPPSA SSLDAISPVQ IDPLAGMASL
     SIGGSAAPHT QSMQGFPPNL GSAFSTPQSP AKAFPPLSTP NQTTAFSGIG GLSSQLPGGL
     GTGSLTGIGT GALGLPAVNN DPFVQRKLGT SGLNQPTFQQ SKMKPSDLSQ VWPEANQHFS
     KEIDDEANSY FQRIYNHPPH PTMSVDEVLE MLQRFKDSTI KREREVFNCM LRNLFEEYRF
     FPQYPDKELH ITACLFGGII EKGLVTYMAL GLALRYVLEA LRKPFGSKMY YFGIAALDRF
     KNRLKDYPQY CQHLASISHF MQFPHHLQEY IEYGQQSRDP PVKMQGSITT PGSIALAQAQ
     AQAQVPAKAP LAGQVNTMVT TSTTTTVAKT VTVTKPTGVS FKKDVPPSIN TTNIDTLLVA
     TDQTERIVEP PENIQEKIAF IFNNLSQSNM TQKVEELKET VKEEFMPWVS QYLVMKRVSI
     EPNFHSLYSN FLDTLKNPEF NKMVLNETYR NIKVLLTSDK AAANFSDRSL LKNLGHWLGM
     ITLAKNKPIL HTDLDVKSLL LEAYVKGQQE LLYVVPFVAK VLESSIRSLV FRPPNPWTMA
     IMNVLAELHQ EHDLKLNLKF EIEVLCKNLA LDINELKPGN LLKDKDRLKN LDEQLSAPKK
     DVKQPEELPA ITTTTTSTTP ATSTTCTATV PPQPQYSYHD INVYSLAGLA PHITLNPTIP
     LFQAHPQLKQ CVRQAIERAV QELVHPVVDR SIKIAMTTCE QIVRKDFALD SEESRMRIAA
     HHMMRNLTAG MAMITCREPL LMSISTNLKN SFASALRTAS PQQREMMDQA AAQLAQDNCE
     LACCFIQKTA VEKAGPEMDK RLATEFELRK HARQEGRRYC DPVVLTYQAE RMPEQIRLKV
     GGVDPKQLAV YEEFARNVPG FLPTNDLSQP TGFLAQPMKQ AWATDDVAQI YDKCITELEQ
     HLHAIPPTLA MNPQAQALRS LLEVVVLSRN SRDAIAALGL LQKAVEGLLD ATSGADADLL
     LRYRECHLLV LKALQDGRAY GSPWCNKQIT RCLIECRDEY KYNVEAVELL IRNHLVNMQQ
     YDLHLAQSME NGLNYMAVAF AMQLVKILLV DERSVAHITE ADLFHTIETL MRINAHSRGN
     APEGLPQLME VVRSNYEAMI DRAHGGPNFM MHSGISQASE YDDPPGLREK AEYLLREWVN
     LYHSAAAGRD STKAFSAFVG QMHQQGILKT DDLITRFFRL CTEMCVEISY RAQAEQQHNP
     AANPTMIRAK CYHNLDAFVR LIALLVKHSG EATNTVTKIN LLNKVLGIVV GVLLQDHDVR
     QSEFQQLPYH RIFIMLLLEL NAPEHVLETI NFQTLTAFCN TFHILRPTKA PGFVYAWLEL
     ISHRIFIARM LAHTPQQKGW PMYAQLLIDL FKYLAPFLRN VELTKPMQIL YKGTLRVLLV
     LLHDFPEFLC DYHYGFCDVI PPNCIQLRNL ILSAFPRNMR LPDPFTPNLK VDMLSEINIA
     PRILTNFTGV MPPQFKKDLD SYLKTRSPVT FLSDLRSNLQ VSNEPGNRYN LQLINALVLY
     VGTQAIAHIH NKGSTPSMST ITHSAHMDIF QNLAVDLDTE GRYLFLNAIA NQLRYPNSHT
     HYFSCTMLYL FAEANTEAIQ EQITRVLLER LIVNRPHPWG LLITFIELIK NPAFKFWNHE
     FVHCAPEIEK LFQSVAQCCM GQKQAQQVME GTGAS
//
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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CC   -----------------------------------------------------------------------
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   Q6ZQ68_MOUSE            Unreviewed;      1255 AA.
AC   Q6ZQ68;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-FEB-2011, entry version 43.
DE   SubName: Full=MKIAA0687 protein;
DE   Flags: Fragment;
GN   Name=Map4k4; Synonyms=mKIAA0687;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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; AK129191; BAC98001.1; -; Transcribed_RNA.
DR   IPI; IPI00460720; -.
DR   UniGene; Mm.19073; -.
DR   ProteinModelPortal; Q6ZQ68; -.
DR   STRING; Q6ZQ68; -.
DR   PRIDE; Q6ZQ68; -.
DR   Ensembl; ENSMUST00000088000; ENSMUSP00000085315; ENSMUSG00000026074.
DR   UCSC; uc007ats.1; mouse.
DR   MGI; MGI:1349394; Map4k4.
DR   GeneTree; ENSGT00600000084021; -.
DR   HOGENOM; HBG715124; -.
DR   HOVERGEN; HBG036506; -.
DR   InParanoid; Q6ZQ68; -.
DR   ArrayExpress; Q6ZQ68; -.
DR   Bgee; Q6ZQ68; -.
DR   Genevestigator; Q6ZQ68; -.
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; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00036; CNH; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   1255 AA;  143585 MW;  1034F4DBEC44E35E CRC64;
     QVYKGRHVKT GQLAAIKVMD VTEDEEEEIK LEINMLKKYS HHRNIATYYG AFIKKSPPGH
     DDQLWLVMEF CGAGSITDLV KNTKGNTLKE DWIAYISREI LRGLAHLHIH HVIHRDIKGQ
     NVLLTENAEV KLVDFGVSAQ LDRTVGRRNT FIGKGPPPLC DMHPMRALFL IPRNPPPRLK
     SKKWSKKFFS FIEGCLVKNY MQRPSTEQLL KHPFIRDQPN ERQVRIQLKD HIDRTRKKRG
     EKDETEYEYS GSEEEEEEVP EQEGEPSSIV NVPGESTLRR DFLRLQQENK ERSEALRRQQ
     LLQEQQLREQ EEYKRQLLAE RQKRIEQQKE QRRRLEEQQR REREARRQQE REQRRREQEE
     KRRLEELERR RKEEEERRRA EEEKRRVERE QEYIRRQLEE EQRHLEILQQ QLLQEQAMLL
     ECRWREMEEH RQAERLQRQL QQEQAYLLSL QHDHRRPHAQ QQPPPPQQQE RSKPSFHAPE
     PKPHYDPADR AREVQWSHLA SLKNNVSPVS RSHSFSDPSP KFAHHHLRSQ DPCPPSRSEG
     LSQSSDSKSE VPEPTQKAWS RSDSDEVPPR VPVRTTSRSP VLSRRDSPLQ GGGQQNSQAG
     QRNSTSSIEP RLLWERVEKL VPRPGSGSSS GSSNSGSQPG SHPGSQSGSG ERFRVRSSSK
     SEGSPSPRQE SAAKKPDDKK EVFRPLKPAG EVDLTALAKE LRAVEDVRPP HKVTDYSSSS
     EESGTTDEEE EDVEQEGADD STSGPEDTRA ASSPNLSNGE TESVKTMIVH DDVESEPAMT
     PSKEGTLIVR QSTVDQKRAS HHESNGFAGR IHLLPDLLQQ SHSSSTSSTS SSPSSSQPTP
     TMSPQTPQDK LTANETQSAS STLQKHKSSS SFTPFIDPRL LQISPSSGTT VTSVVGFSCD
     GLRPEAIRQD PTRKGSVVNV NPTNTRPQSD TPEIRKYKKR FNSEILCAAL WGVNLLVGTE
     SGLMLLDRSG QGKVYPLISR RRFQQMDVLE GLNVLVTISG KKDKLRVYYL SWLRNKILHN
     DPEVEKKQGW TTVGDLEGCV HYKVVKYERI KFLVIALKSS VEVYAWAPKP YHKFMAFKSF
     GELLHKPLLV DLTVEEGQRL KVIYGSCAGF HAVDVDSGSV YDIYLPTHIQ CSIKPHAIII
     LPNTDGMELL VCYEDEGVYV NTYGRITKDV VLQWGEMPTS VAYIRSNQTM GWGEKAIEIR
     SVETGHLDGV FMHKRAQRLK FLCERNDKVF FASVRSGGSS QVYFMTLGRT SLLSW
//
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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CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
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   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   Q6ZQK4_MOUSE            Unreviewed;       458 AA.
AC   Q6ZQK4;
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=MKIAA0044 protein;
DE   Flags: Fragment;
GN   Name=Ppp2r5c; Synonyms=mKIAA0044;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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; AK129042; BAC97852.1; -; mRNA.
DR   IPI; IPI00408059; -.
DR   RefSeq; NP_001128473.1; NM_001135001.1.
DR   UniGene; Mm.240396; -.
DR   UniGene; Mm.458056; -.
DR   ProteinModelPortal; Q6ZQK4; -.
DR   STRING; Q6ZQK4; -.
DR   Ensembl; ENSMUST00000065483; ENSMUSP00000066351; ENSMUSG00000017843.
DR   GeneID; 26931; -.
DR   KEGG; mmu:26931; -.
DR   CTD; 26931; -.
DR   MGI; MGI:1349475; Ppp2r5c.
DR   GeneTree; ENSGT00550000074525; -.
DR   HOGENOM; HBG602178; -.
DR   HOVERGEN; HBG000009; -.
DR   InParanoid; Q6ZQK4; -.
DR   OrthoDB; EOG4RXXZV; -.
DR   ArrayExpress; Q6ZQK4; -.
DR   Bgee; Q6ZQK4; -.
DR   Genevestigator; Q6ZQK4; -.
DR   GO; GO:0005634; C:nucleus; 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; 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;
FT   NON_TER       1      1
SQ   SEQUENCE   458 AA;  53017 MW;  F0A5A632BC484A8C CRC64;
     GSGGGRRQGR RRRPAPAMPN KNKKEKEPPK PVKSGKGPKE GQDTAETEIA SRKNSLTVVQ
     SSTSTKIKVP IPQPVVVPVK KDKRQNSSRF NASNNRELQK LPSLKDVPPA DQEKLFIQKL
     RQCCVLFDFV SDPLSDLKWK EVKRAALSEM VEYITHNRNV ITEPIYPEAV HMFAVNMFRT
     LPPSSNPTGA EFDPEEDEPT LEAAWPHLQL VYEFFLRFLE SPDFQPNIAK KYIDQKFVLQ
     LLELFDSEDP RERDFLKTTL HRIYGKFLGL RAYIRKQINN IFYRFIYETE HHNGIAELLE
     ILGSIINGFA LPLKEEHKIF LLKVLLPLHK VKSLSVYHPQ LAYCVVQFLE KDSTLTEPVV
     MALLKYWPKT HSPKEVMFLN ELEEILDVIE PSEFVKIMEP LFRQLAKCVS SPHFQVAERA
     LYYWNNEYIM SLISDNAAKI LPIMFPSLYR NSKTHWNK
//
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.
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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   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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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   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;
CC   -----------------------------------------------------------------------
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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   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   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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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   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.
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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   CASD1_MOUSE             Reviewed;         797 AA.
AC   Q7TN73; Q1RN01; Q6PD39; Q8VEF5;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=CAS1 domain-containing protein 1;
DE   Flags: Precursor;
GN   Name=Casd1; Synonyms=Cas1, Cast1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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;
RX   MEDLINE=22723761; PubMed=12840045; DOI=10.1101/gr.906803;
RA   Ono R., Shiura H., Aburatani H., Kohda T., Kaneko-Ishino T.,
RA   Ishino F.;
RT   "Identification of a large novel imprinted gene cluster on mouse
RT   proximal chromosome 6.";
RL   Genome Res. 13:1696-1705(2003).
RN   [2]
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).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- DEVELOPMENTAL STAGE: Expressed in neonatal brain and in day 10 and
CC       13 embryo.
CC   -!- SIMILARITY: Belongs to the CASD1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH18542.1; Type=Erroneous initiation;
CC       Sequence=AAH38009.1; Type=Erroneous initiation;
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DR   EMBL; AB091829; BAC77246.1; -; mRNA.
DR   EMBL; BC018542; AAH18542.1; ALT_INIT; mRNA.
DR   EMBL; BC038009; AAH38009.1; ALT_INIT; mRNA.
DR   EMBL; BC058953; AAH58953.1; -; mRNA.
DR   EMBL; BC125377; AAI25378.1; -; mRNA.
DR   EMBL; BC125379; AAI25380.1; -; mRNA.
DR   IPI; IPI00380296; -.
DR   RefSeq; NP_663373.2; NM_145398.2.
DR   UniGene; Mm.270703; -.
DR   ProteinModelPortal; Q7TN73; -.
DR   PRIDE; Q7TN73; -.
DR   Ensembl; ENSMUST00000015333; ENSMUSP00000015333; ENSMUSG00000015189.
DR   GeneID; 213819; -.
DR   KEGG; mmu:213819; -.
DR   UCSC; uc009avo.1; mouse.
DR   CTD; 213819; -.
DR   MGI; MGI:2384865; Casd1.
DR   eggNOG; roNOG14249; -.
DR   GeneTree; ENSGT00390000004037; -.
DR   HOGENOM; HBG315002; -.
DR   HOVERGEN; HBG062482; -.
DR   InParanoid; Q7TN73; -.
DR   OMA; HFGLLLK; -.
DR   OrthoDB; EOG4FJ885; -.
DR   PhylomeDB; Q7TN73; -.
DR   NextBio; 374116; -.
DR   ArrayExpress; Q7TN73; -.
DR   Bgee; Q7TN73; -.
DR   CleanEx; MM_CASD1; -.
DR   Genevestigator; Q7TN73; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR012419; Cas1p.
DR   InterPro; IPR011028; Cyclin-like.
DR   Pfam; PF07779; Cas1p; 1.
DR   SUPFAM; SSF47954; Cyclin_like; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     38       Potential.
FT   CHAIN        39    797       CAS1 domain-containing protein 1.
FT                                /FTId=PRO_0000307231.
FT   TRANSMEM    314    334       Helical; (Potential).
FT   TRANSMEM    364    384       Helical; (Potential).
FT   TRANSMEM    396    416       Helical; (Potential).
FT   TRANSMEM    440    460       Helical; (Potential).
FT   TRANSMEM    462    482       Helical; (Potential).
FT   TRANSMEM    487    507       Helical; (Potential).
FT   TRANSMEM    514    534       Helical; (Potential).
FT   TRANSMEM    547    567       Helical; (Potential).
FT   TRANSMEM    600    620       Helical; (Potential).
FT   TRANSMEM    639    659       Helical; (Potential).
FT   TRANSMEM    672    692       Helical; (Potential).
FT   TRANSMEM    699    719       Helical; (Potential).
FT   TRANSMEM    726    746       Helical; (Potential).
FT   TRANSMEM    771    791       Helical; (Potential).
SQ   SEQUENCE   797 AA;  91603 MW;  9FF23144DDDA8741 CRC64;
     MAALAYNLGK REINHYFSVR SAKVLALVAV LLLAACHLAS RRYRGNDSCE YLLSSGRFLG
     EKVWQPHSCM MHKYKISEAK TCLVDKHIAF IGDSRIRQLF YSFVKIINPQ FKEEGNKHEN
     IPFEDKAASV KVDFLWHPEV NGSMKQCIKV WTEDSVLKPH VIVAGAATWS IKIHNGSEEA
     LAQYKMNITS IAPLLEKLAK TSDVYWVLQD PVYEDLLSEN RKMITNEKID AYNEAAVSIL
     NSSTRTSKSN VKMFSVSKLI AQETIMESLD GLHLPESSRE TSAMILMNVY CNKVVKPVDG
     SCCQPRPPLT LIQKLAACFF TLSIIGYFIF YVIHRNAHRK NKPCTDLESG EEKKNIINTP
     VSSLEILLQS FCKLGLIMAY FYMCDRANLF MKENKFYTHS SFFIPIIYIL VLGVFYNENT
     KETKVLNREQ TDEWKGWMQL VILIYHISGA STFLPVYMHI RVLVAAYLFQ TGYGHFSYFW
     IKGDFGIHRV CQVLFRLNFL VVVLCIVMDR PYQFYYFVPL VTVWFMVIYV TLALWPQITQ
     KKANGNFFWY LGLLLKLGLL LLCIWFLAYS QGAFEKIFSL WPLSKCFELE GSVYEWWFRW
     RLDRYVVFHG VLFAFIYLAL QRRQILSEGK GEPLFSNKIS NFLLFVSVVS FLTYSIWASS
     CKNKAECNEL HPSVSVVQIV AFILIRNIPG YARSIYSSFF AWFGKISLEL FICQYHIWLA
     ADTRGILVLI PGNPTLNIIV STFIFVCVAH EISQITTDLA QVVIPKDNPS LFRRLACTIA
     FFGGVLILSS IQDKSRL
//
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   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   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   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   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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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   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   -----------------------------------------------------------------------
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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   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   -----------------------------------------------------------------------
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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   Q7TS87_MOUSE            Unreviewed;      1971 AA.
AC   Q7TS87;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 52.
DE   SubName: Full=Minichromosome maintenance deficient 3 (S. cerevisiae) associated protein;
DE   SubName: Full=Minichromosome maintenance deficient 3 (S. cerevisiae) associated protein, isoform CRA_b;
GN   Name=Mcm3ap; ORFNames=mCG_3107;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; 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.
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DR   EMBL; BC052452; AAH52452.1; -; mRNA.
DR   EMBL; CH466553; EDL31849.1; -; Genomic_DNA.
DR   IPI; IPI00761873; -.
DR   RefSeq; NP_062307.2; NM_019434.2.
DR   UniGene; Mm.30098; -.
DR   ProteinModelPortal; Q7TS87; -.
DR   STRING; Q7TS87; -.
DR   PRIDE; Q7TS87; -.
DR   Ensembl; ENSMUST00000001178; ENSMUSP00000001178; ENSMUSG00000001150.
DR   GeneID; 54387; -.
DR   KEGG; mmu:54387; -.
DR   UCSC; uc007fup.1; mouse.
DR   CTD; 54387; -.
DR   MGI; MGI:1930089; Mcm3ap.
DR   HOVERGEN; HBG052431; -.
DR   InParanoid; Q7TS87; -.
DR   OMA; NWLKVKF; -.
DR   PhylomeDB; Q7TS87; -.
DR   NextBio; 311220; -.
DR   ArrayExpress; Q7TS87; -.
DR   Bgee; Q7TS87; -.
DR   Genevestigator; Q7TS87; -.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR005062; SAC3/GANP/Nin1/mts3/eIF-3-p25.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF03399; SAC3_GANP; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1971 AA;  217363 MW;  FA9CDB20D1441B02 CRC64;
     MHPVNPFGGQ QPSAFAVSSS TTGTYQTKSP FRFGQPSLFG QNSTPSKSLA FSQVPSFATP
     SGGSHSSSLP AFGLTQTSSV GLFSSLESTP SFAATSSSSV PGNTAFSFKS TSSVGVFPSG
     ATFGPETGEV AGSGFRKTEF KFKPLENAVF KPIPGPESEP EKTQSQISSG FFTFSHPVGS
     GSGGLTPFSF PQVTNSSVTS SSFIFSKPVT SNTPAFASPL SNQNVEEEKR VSTSAFGSSN
     SSFSTFPTAS PGSLGEPFPA NKPSLRQGCE EAISQVEPLP TLMKGLKRKE DQDRSPRRHC
     HEAAEDPDPL SRGDHPPDKR PVRLNRPRGG TLFGRTIQEV FKSNKEAGRL GSKESKESGF
     AEPGESDHAA VPGGSQSTMV PSRLPAVTKE EEESRDEKED SLRGKSVRQS KRREEWIYSL
     GGVSSLELTA IQCKNIPDYL NDRAILEKHF SKIAKVQRVF TRRSKKLAVI HFFDHASAAL
     ARKKGKGLHK DVVIFWHKKK ISPSKKLFPL KEKLGESEAS QGIEDSPFQH SPLSKPIVRP
     AAGSLLSKSS PVKKPSLLKM HQFEADPFDS GSEGSEGLGS CVSSLSTLIG TVADTSEEKY
     RLLDQRDRIM RQARVKRTDL DKARAFVGTC PDMCPEKERY LRETRSQLSV FEVVPGTDQV
     DHAAAVKEYS RSSADQEEPL PHELRPSAVL SRTMDYLVTQ IMDQKEGSLR DWYDFVWNRT
     RGIRKDITQQ HLCDPLTVSL IEKCTRFHIH CAHFMCEEPM SSFDAKINNE NMTKCLQSLK
     EMYQDLRNKG VFCASEAEFQ GYNVLLNLNK GDILREVQQF HPDVRNSPEV NFAVQAFAAL
     NSNNFVRFFK LVQSASYLNA CLLHCYFNQI RKDALRALNV AYTVSTQRST VFPLDGVVRM
     LLFRDSEEAT NFLNYHGLTV ADGCVELNRS AFLEPEGLCK ARKSVFIGRK LTVSVGEVVN
     GGPLPPVPRH TPVCSFNSQN KYVGESLATE LPISTQRAGG DPAGGGRGED CEAEVDVPTL
     AVLPQPPPAS SATPALHVQP LAPAAAPSLL QASTQPEVLL PKPAPVYSDS DLVQVVDELI
     QEALQVDCEE VSSAGAAYVA AALGVSNAAV EDLITAATTG ILRHVAAEEV SMERQRLEEE
     KQRAEEERLK QERELMLTQL SEGLAAELTE LTVTECVWET CSQELQSAVE IDQKVRVARC
     CEAVCAHLVD LFLAEEIFQT AKETLQELQC FCKYLQRWRE AVAARKKFRR QMRAFPAAPC
     CVDVNDRLQA LVPSAECPIT EENLAKGLLD LGHAGKVGVS CTRLRRLRNK TAHQIKVQHF
     HQQLLRNAAW APLDLPSIVS EHLPMKQKRR FWKLVLVLPD VEEQTPESPG RILENWLKVK
     FTGDDSMVGD IGDNAGDIQT LSVFNTLSSK GDQTVSVNVC IKVAHGTLSD SALDAVETQK
     DLLGTSGLML LLPPKVKSEE VAEEELSWLS ALLQLKQLLQ AKPFQPALPL VVLVPSSRGD
     SAGRAVEDGL MLQDLVSAKL ISDYIVVEIP DSVNDLQGTV KVSGAVQWLI SRCPQALDLC
     CQTLVQYVED GISREFSRRF FHDRRERRLA SLPSQEPSTI IELFNSVLQF LASVVSSEQL
     CDISWPVMEF AEVGGSQLLP HLHWNSPEHL AWLKQAVLGF QLPQMDLPPP GAPWLPVCSM
     VIQYTSQIPS SSQTQPVLQS QVENLLCRTY QKWKNKSLSP GQELGPSVAE IPWDDIITLC
     INHKLRDWTP PRLPVTLEAL SEDGQICVYF FKNLLRKYHV PLSWEQARMQ TQRELQLSHG
     RSGMRSIHPP TSTFPTPLLH VHQKGKKKEE SGREGSLSTE DLLRGASAEE LLAQSLSSSL
     LEEKEENKRF EDQLQQWLSQ DSQAFTESTR LPLYLPQTLV SFPDSIKTQT MVKTSTSPQN
     SGTGKQLRFS EASGSSLTEK LKLLERLIQS SRAEEAASEL HLSALLEMVD M
//
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   ELP1_MOUSE              Reviewed;        1333 AA.
AC   Q7TT37; Q3UHY6; Q7TQH1; Q8C6B3; Q8CBI3; Q8CH82; Q8VHU5; Q8VHV9;
AC   Q9CT81;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Elongator complex protein 1;
DE            Short=ELP1;
DE   AltName: Full=IkappaB kinase complex-associated protein;
DE            Short=IKK complex-associated protein;
GN   Name=Ikbkap; Synonyms=Elp1, Ikap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=BALB/c;
RX   MEDLINE=21614679; PubMed=11747609; DOI=10.1089/104454901317094990;
RA   Cuajungco M.P., Leyne M., Mull J., Gill S.P., Gusella J.F.,
RA   Slaugenhaupt S.A.;
RT   "Cloning, characterization, and genomic structure of the mouse Ikbkap
RT   gene.";
RL   DNA Cell Biol. 20:579-586(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/SvJ; TISSUE=Spleen;
RX   MEDLINE=21579790; PubMed=11722848; DOI=10.1016/S0378-1119(01)00737-5;
RA   Coli R., Anderson S.L., Volpi S.A., Rubin B.Y.;
RT   "Genomic organization and chromosomal localization of the mouse IKBKAP
RT   gene.";
RL   Gene 279:81-89(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X CBA;
RA   Shirane M., Hatakeyama S., Nakayama K.;
RT   "Molecular cloning and biochemical analysis of murine IKAP.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [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=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: May act as a scaffold protein that may assemble active
CC       IKK-MAP3K14 complexes (IKKA, IKKB and MAP3K14/NIK) (By
CC       similarity).
CC   -!- FUNCTION: Acts as subunit of the RNA polymerase II elongator
CC       complex, which is a histone acetyltransferase component of the RNA
CC       polymerase II (Pol II) holoenzyme and is involved in
CC       transcriptional elongation. Elongator may play a role in chromatin
CC       remodeling and is involved in acetylation of histones H3 and
CC       probably H4 (By similarity).
CC   -!- SUBUNIT: Interacts preferentially with MAP3K14/NIK followed by
CC       IKK-alpha and IKK-beta. Component of the RNA polymerase II
CC       elongator complex (Elongator), which consists of IKBKAP/ELP1,
CC       STIP1/ELP2, ELP3, ELP4, and two yet unidentified proteins.
CC       Elongator associates with the C-terminal domain (CTD) of Pol II
CC       largest subunit. Interacts with ELP3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain.
CC   -!- DEVELOPMENTAL STAGE: Expressed at embryonic days 7, 11, 15 and 17
CC       with the highest expression at embryonic day 11.
CC   -!- PTM: Phosphorylated (By similarity).
CC   -!- SIMILARITY: Belongs to the ELP1/IKA1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL36025.1; Type=Frameshift; Positions=498;
CC       Sequence=AAO15309.1; Type=Frameshift; Positions=Several;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF367244; AAL36025.1; ALT_FRAME; mRNA.
DR   EMBL; AF387811; AAL40925.1; -; mRNA.
DR   EMBL; AF140786; AAO15309.1; ALT_FRAME; mRNA.
DR   EMBL; AK004402; BAB23291.1; -; mRNA.
DR   EMBL; AK076152; BAC36221.1; -; mRNA.
DR   EMBL; AK035944; BAC29252.1; -; mRNA.
DR   EMBL; AK147153; BAE27720.1; -; mRNA.
DR   EMBL; AL807762; CAM25708.1; -; Genomic_DNA.
DR   EMBL; AL929577; CAM25708.1; JOINED; Genomic_DNA.
DR   EMBL; AL929577; CAM24766.1; -; Genomic_DNA.
DR   EMBL; AL807762; CAM24766.1; JOINED; Genomic_DNA.
DR   EMBL; BC052387; AAH52387.2; -; mRNA.
DR   EMBL; BC054468; AAH54468.1; -; mRNA.
DR   IPI; IPI00380780; -.
DR   RefSeq; NP_080355.2; NM_026079.3.
DR   UniGene; Mm.282743; -.
DR   ProteinModelPortal; Q7TT37; -.
DR   SMR; Q7TT37; 92-128, 197-256, 418-452.
DR   STRING; Q7TT37; -.
DR   PhosphoSite; Q7TT37; -.
DR   PRIDE; Q7TT37; -.
DR   Ensembl; ENSMUST00000030140; ENSMUSP00000030140; ENSMUSG00000028431.
DR   GeneID; 230233; -.
DR   KEGG; mmu:230233; -.
DR   UCSC; uc008sxr.1; mouse.
DR   CTD; 230233; -.
DR   MGI; MGI:1914544; Ikbkap.
DR   GeneTree; ENSGT00390000013344; -.
DR   HOVERGEN; HBG019038; -.
DR   InParanoid; Q7TT37; -.
DR   OMA; ILEXRSS; -.
DR   OrthoDB; EOG4KPT90; -.
DR   PhylomeDB; Q7TT37; -.
DR   NextBio; 379841; -.
DR   ArrayExpress; Q7TT37; -.
DR   Bgee; Q7TT37; -.
DR   Genevestigator; Q7TT37; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0008023; C:transcription elongation factor complex; ISS:UniProtKB.
DR   GO; GO:0008607; F:phosphorylase kinase regulator activity; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR006849; IKI3.
DR   Gene3D; G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 2.
DR   PANTHER; PTHR12747; IKI3; 1.
DR   Pfam; PF04762; IKI3; 1.
DR   PIRSF; PIRSF017233; IKAP; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   1333       Elongator complex protein 1.
FT                                /FTId=PRO_0000283995.
FT   MOD_RES    1172   1172       Phosphoserine (By similarity).
FT   MOD_RES    1175   1175       Phosphoserine (By similarity).
FT   CONFLICT     42     42       T -> P (in Ref. 3; AAO15309).
FT   CONFLICT    120    120       D -> G (in Ref. 4; BAE27720).
FT   CONFLICT    215    216       QT -> HS (in Ref. 3; AAO15309).
FT   CONFLICT    221    221       I -> V (in Ref. 2; AAL40925).
FT   CONFLICT    346    346       I -> V (in Ref. 2; AAL40925 and 3;
FT                                AAO15309).
FT   CONFLICT    582    582       Y -> I (in Ref. 1; AAL36025).
FT   CONFLICT    634    635       ND -> LV (in Ref. 1; AAL36025).
FT   CONFLICT    649    649       D -> A (in Ref. 2; AAL40925).
FT   CONFLICT    663    663       V -> G (in Ref. 1; AAL36025, 2; AAL40925
FT                                and 3; AAO15309).
FT   CONFLICT    693    694       ER -> VW (in Ref. 1; AAL36025).
FT   CONFLICT    773    773       K -> F (in Ref. 1; AAL36025).
FT   CONFLICT   1110   1110       V -> I (in Ref. 1; AAL36025, 2; AAL40925
FT                                and 3; AAO15309).
FT   CONFLICT   1159   1159       A -> G (in Ref. 4; BAB23291).
SQ   SEQUENCE   1333 AA;  149584 MW;  C40E0098DD4DF63C CRC64;
     MRNLKLHRTL EFRDIQAPGK PQCFCLRAEQ GTVLIGSERG LTEVDPVRRE VKTEISLVAE
     GFLPEDGSGC IVGIQDLLDQ ESVCVATASG DVIVCNLSTQ QLECVGSVAS GISVMSWSPD
     QELLLLATAQ QTLIMMTKDF EVIAEEQIHQ DDFGEGKFVT VGWGSKQTQF HGSEGRPTAF
     PVQLPENALP WDDRRPHITW RGDGQYFAVS VVCRQTEARK IRVWNREFAL QSTSESVPGL
     GPALAWKPSG SLIASTQDKP NQQDVVFFEK NGLLHGHFTL PFLKDEVKVN DLLWNADSSV
     LAIWLEDLPK EDSSTLKSYV QLWTVGNYHW YLKQSLPFST TGKNQIVSLL WDPVTPCRLH
     VLCTGWRYLC CDWHWTTDRS SGNSANDLAN VAVIDGNRVL VTVFRQTVVP PPMCTYRLLI
     PHPVNQVIFS AHLGNDLAVL DASNQISVYK CGDKPNMDST VKLGAVGGNG FKVPLTTPHL
     EKRYSIQFGN NEEEEEEEVN ALQLSFLTWV EDDTFLAISY SHSSSQSIIH HLTVTHSEVD
     EEQGQLDVSS SVTVDGVVIG LCCCSKTKSL AVQLADGQVL KYLWESPSLA VEPWKNSEGI
     PVRFVHPCTQ MEVATIGGEE CVLGLTDRCR FFINDTEVAS NITSFAVCDD FLLVTTHSHT
     CQVFSLSGAS LKMLQAALSG SHEASGEILR KVERGSRIVT VVPQDTKLIL QMPRGNLEVV
     HHRALVLAQI RKWLDKLMFK EAFECMRKLR INLNLIHDHN PKVFLENVET FVKQIDSVNH
     INLFFTELRE EDVTKTMYPP PITKSVQVST HPDGKKLDLI CDAMRAAMEA INPRKFCLSI
     LTSHVKKTTP ELEIVLQKVQ ELQGNLPFDP ESVSVEEALK YLLLLVDVNE LFNHSLGTYD
     FNLVLMVAEK SQKDPKEYLP FLNTLKKMET NYQRFTIDKY LKRYEKALGH LSKCGPEYFT
     ECLNLIKDKN LYKEALKLYR PDSPQYQAVS MAYGEHLMQE HLYEPAGLVF ARCGAQEKAL
     EAFLACGSWQ QALCVAAQLQ MSKDKVAGLA RTLAGKLVEQ RKHSEAATVL EQYAQDYEEA
     VLLLLEGSAW EEALRLVYKY DRVDIIETSV KPSILEAQKN YMDFLDSETA TFIRHKNRLQ
     VVRALRRQAP QVHVDHEVAH GPESDLFSET SSIMSGSEMS GRYSHSNSRI SARSSKNRRK
     AERKKHSLKE GSPLEGLALL EALSEVVQSV EKLKDEVRAI LKVLFLFEFE EQAKELQRAF
     ESTLQLMERA VPEIWTPAGQ QSSTTPVLGP SSTANSITAS YQQQKTCVPA LDAGVYMPPK
     MDPRSQWKLS LLE
//
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   -----------------------------------------------------------------------
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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;
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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   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   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   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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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   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;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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   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   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;
CC   -----------------------------------------------------------------------
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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   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;
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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   MADD_MOUSE              Reviewed;        1577 AA.
AC   Q80U28; Q3TQK3; Q6P4I6; Q80W52; Q80WL3; Q80WL4; Q80WL5; Q80WL6;
AC   Q80WL7; Q80WL8; Q80WL9; Q80WM0; Q80WM1; Q80WM2; Q8CBC1;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   30-NOV-2010, entry version 47.
DE   RecName: Full=MAP kinase-activating death domain protein;
DE   AltName: Full=Rab3 GDP/GTP exchange factor;
GN   Name=Madd; Synonyms=Kiaa0358;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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; 4; 5; 6; 7; 8; 9; 10; 11 AND
RP   12).
RC   STRAIN=C57BL/6;
RA   Al-Zoubi A.M., Efimova E.V., Lu S., Prabhakar B.P.;
RT   "Genomic organization and alternative splicing of IG20 isoforms in
RT   mouse tissues.";
RL   Submitted (MAR-2003) 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] (ISOFORM 13), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1011-1577 (ISOFORM 15).
RC   STRAIN=C57BL/6J; 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   [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 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 643-1577 (ISOFORM 14).
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   FUNCTION.
RX   PubMed=14735464; DOI=10.1002/ijc.11660;
RA   Lim K.M., Yeo W.S., Chow V.T.K.;
RT   "Antisense abrogation of DENN expression induces apoptosis of leukemia
RT   cells in vitro, causes tumor regression in vivo and alters the
RT   transcription of genes involved in apoptosis and the cell cycle.";
RL   Int. J. Cancer 109:24-37(2004).
RN   [7]
RP   FUNCTION.
RX   PubMed=15007167; DOI=10.1073/pnas.0307349101;
RA   Del Villar K., Miller C.A.;
RT   "Down-regulation of DENN/MADD, a TNF receptor binding protein,
RT   correlates with neuronal cell death in Alzheimer's disease brain and
RT   hippocampal neurons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:4210-4215(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1058 AND THR-1060, 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 significant role in regulating cell
CC       proliferation, survival and death through alternative mRNA
CC       splicing. Converts GDP-bound inactive form of RAB3A, RAB3C and
CC       RAB3D to the GTP-bound active forms. Component of the TNFRSF1A
CC       signaling complex: MADD links TNFRSF1A with MAP kinase activation.
CC       Plays an important regulatory role in physiological cell death
CC       (TNF-alpha-induced, caspase-mediated apoptosis).
CC   -!- SUBUNIT: Interacts with the death domain of TNFRSF1A through its
CC       own death domain (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=15;
CC       Name=1;
CC         IsoId=Q80U28-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2; Synonyms=IG20;
CC         IsoId=Q80U28-2; Sequence=VSP_052309, VSP_052312, VSP_052313;
CC       Name=3;
CC         IsoId=Q80U28-3; Sequence=VSP_052301, VSP_052309;
CC         Note=No experimental confirmation available;
CC       Name=4; Synonyms=IG20-PASV;
CC         IsoId=Q80U28-4; Sequence=VSP_052302, VSP_052309, VSP_052311,
CC                                  VSP_052312, VSP_052313;
CC       Name=5; Synonyms=IG20-SV4;
CC         IsoId=Q80U28-5; Sequence=VSP_052300, VSP_052301, VSP_052302,
CC                                  VSP_052309, VSP_052311, VSP_052312,
CC                                  VSP_052314;
CC       Name=6; Synonyms=IG20-SV5;
CC         IsoId=Q80U28-6; Sequence=VSP_052300, VSP_052301, VSP_052302,
CC                                  VSP_052308, VSP_052311, VSP_052312,
CC                                  VSP_052314;
CC       Name=7; Synonyms=IG20-SV2;
CC         IsoId=Q80U28-7; Sequence=VSP_052299, VSP_052302, VSP_052309,
CC                                  VSP_052311, VSP_052312, VSP_052313;
CC       Name=8; Synonyms=IG20-SV1;
CC         IsoId=Q80U28-8; Sequence=VSP_052301, VSP_052302, VSP_052309,
CC                                  VSP_052311, VSP_052312, VSP_052313;
CC       Name=9; Synonyms=IG20-SV6;
CC         IsoId=Q80U28-9; Sequence=VSP_052300, VSP_052301, VSP_052302,
CC                                  VSP_052306, VSP_052311, VSP_052312,
CC                                  VSP_052314;
CC       Name=10; Synonyms=IG20-SV7;
CC         IsoId=Q80U28-10; Sequence=VSP_052300, VSP_052301, VSP_052302,
CC                                   VSP_052305, VSP_052311, VSP_052312,
CC                                   VSP_052314;
CC       Name=11; Synonyms=IG20-SV3;
CC         IsoId=Q80U28-11; Sequence=VSP_052299, VSP_052301, VSP_052302,
CC                                   VSP_052309, VSP_052311, VSP_052312,
CC                                   VSP_052313;
CC       Name=12; Synonyms=IG20-SV8;
CC         IsoId=Q80U28-12; Sequence=VSP_052300, VSP_052301, VSP_052302,
CC                                   VSP_052305, VSP_052310;
CC       Name=13;
CC         IsoId=Q80U28-13; Sequence=VSP_052301, VSP_052303, VSP_052304;
CC         Note=No experimental confirmation available;
CC       Name=14;
CC         IsoId=Q80U28-14; Sequence=VSP_052301, VSP_052309, VSP_052315;
CC         Note=No experimental confirmation available;
CC       Name=15;
CC         IsoId=Q80U28-15; Sequence=VSP_052307;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the MADD family.
CC   -!- SIMILARITY: Contains 1 dDENN domain.
CC   -!- SIMILARITY: Contains 1 death domain.
CC   -!- SIMILARITY: Contains 1 DENN domain.
CC   -!- SIMILARITY: Contains 1 uDENN domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65539.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AY263980; AAP22159.1; -; mRNA.
DR   EMBL; AY263981; AAP22160.1; -; mRNA.
DR   EMBL; AY263982; AAP22161.1; -; mRNA.
DR   EMBL; AY263983; AAP22162.1; -; mRNA.
DR   EMBL; AY263984; AAP22163.1; -; mRNA.
DR   EMBL; AY263985; AAP22164.1; -; mRNA.
DR   EMBL; AY263986; AAP22165.1; -; mRNA.
DR   EMBL; AY263987; AAP22166.1; -; mRNA.
DR   EMBL; AY263988; AAP22167.1; -; mRNA.
DR   EMBL; AY263989; AAP22168.1; -; mRNA.
DR   EMBL; AK122257; BAC65539.1; ALT_INIT; mRNA.
DR   EMBL; AK036347; BAC29392.1; -; mRNA.
DR   EMBL; AK163518; BAE37379.1; -; mRNA.
DR   EMBL; AL691450; CAM17578.1; -; Genomic_DNA.
DR   EMBL; BC042212; AAH42212.1; -; mRNA.
DR   EMBL; BC063386; AAH63386.1; -; mRNA.
DR   IPI; IPI00262319; -.
DR   IPI; IPI00471028; -.
DR   IPI; IPI00620097; -.
DR   IPI; IPI00750832; -.
DR   IPI; IPI00756378; -.
DR   IPI; IPI00757009; -.
DR   IPI; IPI00761754; -.
DR   IPI; IPI00807833; -.
DR   IPI; IPI00828295; -.
DR   IPI; IPI00828390; -.
DR   IPI; IPI00828551; -.
DR   IPI; IPI00828556; -.
DR   IPI; IPI00874726; -.
DR   IPI; IPI00875369; -.
DR   IPI; IPI00875878; -.
DR   RefSeq; NP_001171190.1; NM_001177719.1.
DR   RefSeq; NP_001171191.1; NM_001177720.1.
DR   RefSeq; NP_001171192.1; NM_001177721.1.
DR   RefSeq; NP_001171193.1; NM_001177722.1.
DR   RefSeq; NP_001171194.1; NM_001177723.1.
DR   RefSeq; NP_001171195.1; NM_001177724.1.
DR   RefSeq; NP_001171196.1; NM_001177725.1.
DR   RefSeq; NP_001171197.1; NM_001177726.1.
DR   RefSeq; NP_001171198.1; NM_001177727.1.
DR   RefSeq; NP_001171199.1; NM_001177728.1.
DR   RefSeq; NP_001171200.1; NM_001177729.1.
DR   RefSeq; NP_663502.3; NM_145527.4.
DR   UniGene; Mm.36410; -.
DR   STRING; Q80U28; -.
DR   PhosphoSite; Q80U28; -.
DR   PRIDE; Q80U28; -.
DR   Ensembl; ENSMUST00000049326; ENSMUSP00000039131; ENSMUSG00000040687.
DR   Ensembl; ENSMUST00000066473; ENSMUSP00000069350; ENSMUSG00000040687.
DR   Ensembl; ENSMUST00000099723; ENSMUSP00000097311; ENSMUSG00000040687.
DR   Ensembl; ENSMUST00000099725; ENSMUSP00000097313; ENSMUSG00000040687.
DR   Ensembl; ENSMUST00000111367; ENSMUSP00000106998; ENSMUSG00000040687.
DR   Ensembl; ENSMUST00000111370; ENSMUSP00000107001; ENSMUSG00000040687.
DR   Ensembl; ENSMUST00000111381; ENSMUSP00000107012; ENSMUSG00000040687.
DR   GeneID; 228355; -.
DR   KEGG; mmu:228355; -.
DR   UCSC; uc008kuu.1; mouse.
DR   CTD; 228355; -.
DR   MGI; MGI:2444672; Madd.
DR   HOVERGEN; HBG079455; -.
DR   NextBio; 378956; -.
DR   ArrayExpress; Q80U28; -.
DR   Bgee; Q80U28; -.
DR   CleanEx; MM_MADD; -.
DR   Genevestigator; Q80U28; -.
DR   GO; GO:0016021; C:integral to membrane; ISS:UniProtKB.
DR   GO; GO:0017112; F:Rab guanyl-nucleotide exchange factor activity; IMP:UniProtKB.
DR   GO; GO:0000187; P:activation of MAPK activity; IMP:UniProtKB.
DR   GO; GO:0042981; P:regulation of apoptosis; IMP:UniProtKB.
DR   GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
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; PS50017; DEATH_DOMAIN; FALSE_NEG.
DR   PROSITE; PS50211; DENN; 1.
DR   PROSITE; PS50946; UDENN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Guanine-nucleotide releasing factor;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1577       MAP kinase-activating death domain
FT                                protein.
FT                                /FTId=PRO_0000278139.
FT   TRANSMEM    296    316       Helical; (Potential).
FT   TRANSMEM    335    355       Helical; (Potential).
FT   DOMAIN       24     97       UDENN.
FT   DOMAIN      171    401       DENN.
FT   DOMAIN      484    557       dDENN.
FT   DOMAIN     1336   1411       Death.
FT   COMPBIAS   1156   1248       Ser-rich.
FT   MOD_RES     817    817       Phosphoserine (By similarity).
FT   MOD_RES     819    819       Phosphoserine (By similarity).
FT   MOD_RES     920    920       Phosphoserine (By similarity).
FT   MOD_RES    1058   1058       Phosphoserine.
FT   MOD_RES    1060   1060       Phosphothreonine.
FT   MOD_RES    1235   1235       Phosphothreonine (By similarity).
FT   MOD_RES    1266   1266       Phosphoserine (By similarity).
FT   VAR_SEQ     719    744       EAADSTEMGDKATAGISKPLPPVPPS -> VREHLAG (in
FT                                isoform 7 and isoform 11).
FT                                /FTId=VSP_052299.
FT   VAR_SEQ     719    743       Missing (in isoform 5, isoform 6, isoform
FT                                9, isoform 10 and isoform 12).
FT                                /FTId=VSP_052300.
FT   VAR_SEQ     884    903       Missing (in isoform 3, isoform 5, isoform
FT                                6, isoform 8, isoform 9, isoform 10,
FT                                isoform 11, isoform 12, isoform 13 and
FT                                isoform 14).
FT                                /FTId=VSP_052301.
FT   VAR_SEQ    1120   1138       ELWNKHQEVKKQKALEKQR -> G (in isoform 4,
FT                                isoform 5, isoform 6, isoform 7, isoform
FT                                8, isoform 9, isoform 10, isoform 11 and
FT                                isoform 12).
FT                                /FTId=VSP_052302.
FT   VAR_SEQ    1120   1135       ELWNKHQEVKKQKALE -> DLTENLLMFGVSLFTL (in
FT                                isoform 13).
FT                                /FTId=VSP_052303.
FT   VAR_SEQ    1136   1577       Missing (in isoform 13).
FT                                /FTId=VSP_052304.
FT   VAR_SEQ    1172   1198       Missing (in isoform 10 and isoform 12).
FT                                /FTId=VSP_052305.
FT   VAR_SEQ    1183   1200       Missing (in isoform 9).
FT                                /FTId=VSP_052306.
FT   VAR_SEQ    1196   1198       Missing (in isoform 15).
FT                                /FTId=VSP_052307.
FT   VAR_SEQ    1198   1200       Missing (in isoform 6).
FT                                /FTId=VSP_052308.
FT   VAR_SEQ    1199   1199       V -> VV (in isoform 2, isoform 3, isoform
FT                                4, isoform 5, isoform 7, isoform 8,
FT                                isoform 11 and isoform 14).
FT                                /FTId=VSP_052309.
FT   VAR_SEQ    1219   1577       Missing (in isoform 12).
FT                                /FTId=VSP_052310.
FT   VAR_SEQ    1287   1307       Missing (in isoform 4, isoform 5, isoform
FT                                6, isoform 7, isoform 8, isoform 9,
FT                                isoform 10 and isoform 11).
FT                                /FTId=VSP_052311.
FT   VAR_SEQ    1511   1534       CRELYYCVKDSMERAAARQQSIKP -> VLRVCVWAGDWI
FT                                (in isoform 2, isoform 4, isoform 5,
FT                                isoform 6, isoform 7, isoform 8, isoform
FT                                9, isoform 10 and isoform 11).
FT                                /FTId=VSP_052312.
FT   VAR_SEQ    1559   1577       LEGINLKFMHNQFLKLKKW -> PGRDQSQVHAQPGFHRAE
FT                                SH (in isoform 2, isoform 4, isoform 7,
FT                                isoform 8 and isoform 11).
FT                                /FTId=VSP_052313.
FT   VAR_SEQ    1559   1577       LEGINLKFMHNQFLKLKKW -> PGRDQSQVHAQPVPEIKE
FT                                VVSHKYKTPMAHEICYSVLCLFSYVAAVRSSEEDLRTPPRP
FT                                VSS (in isoform 5, isoform 6, isoform 9
FT                                and isoform 10).
FT                                /FTId=VSP_052314.
FT   VAR_SEQ    1571   1577       FLKLKKW -> ERKVFIELNHIKKCNTVRGVFVLEEFVPEI
FT                                KEVVSHKYKTPMAHEICYSVLCLFSYVAAVRSSEEDLRTPP
FT                                RPVSS (in isoform 14).
FT                                /FTId=VSP_052315.
FT   CONFLICT    132    132       T -> A (in Ref. 3; BAC29392, 4; CAM17578
FT                                and 5; AAH63386).
FT   CONFLICT    152    152       I -> V (in Ref. 3; BAC29392, 4; CAM17578
FT                                and 5; AAH63386).
FT   CONFLICT    157    157       W -> R (in Ref. 1; AAP22159/AAP22160/
FT                                AAP22161/AAP22162/AAP22163/AAP22164/
FT                                AAP22165/AAP22166/AAP22167/AAP22168, 3;
FT                                BAC29392, 4; CAM17578 and 5; AAH63386).
FT   CONFLICT   1159   1159       S -> R (in Ref. 3; BAE37379).
SQ   SEQUENCE   1577 AA;  175180 MW;  5D604F8DDD1EF481 CRC64;
     MVQKKFCPRL LDYLVIVGAR HPSSDSVAQT PELLRRYPLE DHPEFPLPPD VVFFCQPEGC
     LSVRQRRMSL RDDTSFVFTL TDKDTGVTRY GICVNFYRSF QKRMPKEKVE GGAGPRGKEG
     AHTSGASEEA ATGSSESGST LQPPSADSTP DINQSPWGKR 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 SQDSEVSTVS
     NSSGETLGAD SDLSSNAGDG PGGEGSAHLA SSRATLSDSE IETNSATSAI FGKAHSLKPK
     EKPAGSPIRS SEDVSQRVYL YEGLLGRDKG SMWDQLEDAA METFSLSKER STLWDQMQFW
     EDAFLDAVML EREGMGMDQG PQEMIDRYLS LGEHDRKRLE DDEDRLLATL LHNLISYMLL
     MKVNKNDIRK KVRRLMGKSH IGLVYSQQVN EVLDQLNSLN GRDLSIRSSG SRHMKKQTFV
     VHAGTDTNGD IFFMEVCDDC VVLRSNIGTV YERWWYEKLI NMTYCPKTKV LCLWRRNGSE
     TQLNKFYTKK CRELYYCVKD SMERAAARQQ SIKPGPELGG EFPVQDMKTG EGGLLQVTLE
     GINLKFMHNQ FLKLKKW
//
ID   RIMB2_MOUSE             Reviewed;        1072 AA.
AC   Q80U40; B9EKT4;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 2.
DT   08-FEB-2011, entry version 68.
DE   RecName: Full=RIMS-binding protein 2;
DE            Short=RIM-BP2;
GN   Name=Rimbp2; Synonyms=Kiaa0318, 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 MRNA] (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).
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 189-1072 (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   PROTEIN SEQUENCE OF 735-749, 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-852, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
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 synaptic transmission as
CC       bifunctional linker that interacts simultaneously with RIMS1,
CC       RIMS2, CACNA1D and CACNA1B (By similarity).
CC   -!- SUBUNIT: Interacts with RIMS1, RIMS2, CACNA1D and CACNA1B, and
CC       potentially with other Ca(2+) channel alpha-1 isoforms (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane (By similarity). Cell
CC       junction, synapse (By similarity). Note=Synaptic plasma membrane
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80U40-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80U40-2; Sequence=VSP_037437;
CC   -!- DOMAIN: The SH3 domains mediate binding to a proline-rich motif in
CC       RIMS1, RIMS2, CACNA1D and CACNA1B (By similarity).
CC   -!- SIMILARITY: Belongs to the RIMBP family.
CC   -!- SIMILARITY: Contains 3 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 3 SH3 domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK044685; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC151100; AAI51101.1; -; mRNA.
DR   EMBL; BC151101; AAI51102.1; -; mRNA.
DR   EMBL; AK122245; BAC65527.2; -; mRNA.
DR   IPI; IPI00831651; -.
DR   IPI; IPI00874334; -.
DR   UniGene; Mm.233996; -.
DR   ProteinModelPortal; Q80U40; -.
DR   SMR; Q80U40; 176-258, 307-607, 859-1039.
DR   STRING; Q80U40; -.
DR   PhosphoSite; Q80U40; -.
DR   PRIDE; Q80U40; -.
DR   Ensembl; ENSMUST00000031370; ENSMUSP00000031370; ENSMUSG00000029420.
DR   UCSC; uc008zsl.1; mouse.
DR   MGI; MGI:2443235; Rimbp2.
DR   eggNOG; roNOG06090; -.
DR   GeneTree; ENSGT00390000017228; -.
DR   HOVERGEN; HBG079131; -.
DR   ArrayExpress; Q80U40; -.
DR   CleanEx; MM_RBP2; -.
DR   CleanEx; MM_RIMBP2; -.
DR   Genevestigator; Q80U40; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane;
KW   Direct protein sequencing; Isopeptide bond; Membrane; Phosphoprotein;
KW   Repeat; SH3 domain; Synapse; Ubl conjugation.
FT   CHAIN         1   1072       RIMS-binding protein 2.
FT                                /FTId=PRO_0000221384.
FT   DOMAIN      181    248       SH3 1.
FT   DOMAIN      311    391       Fibronectin type-III 1.
FT   DOMAIN      405    477       Fibronectin type-III 2.
FT   DOMAIN      501    587       Fibronectin type-III 3.
FT   DOMAIN      868    936       SH3 2.
FT   DOMAIN      972   1039       SH3 3.
FT   MOD_RES     852    852       Phosphoserine.
FT   CROSSLNK    743    743       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK    749    749       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   VAR_SEQ    1065   1072       KKSVHFTP -> VSQPP (in isoform 2).
FT                                /FTId=VSP_037437.
FT   CONFLICT     76     76       Q -> E (in Ref. 2; AAI51101/AAI51102).
FT   CONFLICT    714    714       V -> A (in Ref. 2; AAI51101/AAI51102).
FT   CONFLICT   1065   1065       Missing (in Ref. 1; AK044685).
SQ   SEQUENCE   1072 AA;  118369 MW;  9073B0E66E5F0B69 CRC64;
     MREAAERRQQ LELEHEQALA FLNAKQQEIQ LLQQAQVEAK KEHEGAVQLL ESKVRELEEK
     CRVQSEQFNL LSRDLQKFRQ HTGSIDLLGS SSVALLDVPL APGKPFPQYM NGLATSIHKG
     HEGPTGHYSV IGDYIPLSGD KLESPCVKPS FLLRSSSPRC RFESEMDNDR NSNNSKQSSS
     GKVHLCVARY SYNPFDGPNE NPEAELPLTA GKYLYVYGDM DEDGFYEGEL LDGQRGLVPS
     NFVDFIQDNE SRLAGTLGSE QDQNFLNHSG ISLERDSILH LHSPTQVDSG ITDNGGGTLD
     VNIDDIGEDT VPYPRKITLI KQLAKSVIVG WEPPAVPPGW GTVSSYNVLV DKETRMSLAL
     GRRTKALIEK LNTAACTYRI SVQCVTSRGN SDELQCTLLV GKDVVVAPSQ LRVDNITQIS
     AQLSWLPTNS NYSHIIFLNE EELDIVKAAR YKYQFFNLRP NMAYKVKVLA QPHQMPWQLP
     LEQREKKEAC VEFSTLPAGP PAPPQDVTVH AGATAASVQV SWKPPALTPT GLSNGANVTG
     YGVYAKGQRV AEVIAPTADG TAVELIRLRS LEAKAVSVRT LSVQGESMDS ALAAIPPDLL
     VPPAPHPRTA PPPKPLASDM DTKDQHLGPH VKVDESWEQS RSPGPAHGHM LEPPDMHSAG
     PGRRSPSPSR ILPQPQGAPV STTVAKAMAR EAAQRVAESN RLEKRSLFLE QSSVGQYTNS
     DEEDGYASPE VKRRGTSVDD FLKGSELGKQ PHCCHGDEYH TESSRGSDLS DIMEEDEEEL
     YSEMQLEDGG RRRPSGTSHN ALKILGNSTL MGRADRMEHV SRRYSHSGGG SHRHRPAMAP
     SIDEYTGRDH LSPDFYDESE TDPGAEELPA RIFVALFDYD PLTMSPNPDA AEEELPFKEG
     QIIKVYGDKD ADGFYRGETC ARLGLIPCNM VSEIHADDEE MMDQLLRQGF LPLNTPVEKI
     ERSRRSGRGH SVPTRRMVAL YDYDPRESSP NVDVEAELPF CTGDIITVFG EIDEDGFYYG
     ELNGQKGLVP SNFLEEVPDD VEVHLSDAPP HYSHDPPMRS KAKRKKSVHF TP
//
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   -----------------------------------------------------------------------
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   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;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   NU214_MOUSE             Reviewed;        2085 AA.
AC   Q80U93; A2ATN2;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Nuclear pore complex protein Nup214;
DE   AltName: Full=214 kDa nucleoporin;
DE   AltName: Full=Nucleoporin Nup214;
GN   Name=Nup214; Synonyms=Kiaa0023;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; 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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-930, 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 serve as a docking site in the receptor-mediated
CC       import of substrates across the nuclear pore complex (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer. Interacts with DDX19, NUP88, XPO1 and XPO5 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex (By
CC       similarity). Note=Cytoplasmic filaments (By similarity).
CC   -!- DOMAIN: Contains FG repeats.
CC   -!- PTM: Probably glycosylated as it reacts with wheat germ agglutinin
CC       (WGA) (By similarity).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65471.1; 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; AK122189; BAC65471.1; ALT_INIT; mRNA.
DR   EMBL; AL928893; CAM26045.1; -; Genomic_DNA.
DR   IPI; IPI00229722; -.
DR   RefSeq; NP_758472.2; NM_172268.2.
DR   UniGene; Mm.289686; -.
DR   ProteinModelPortal; Q80U93; -.
DR   SMR; Q80U93; 1-433.
DR   STRING; Q80U93; -.
DR   PhosphoSite; Q80U93; -.
DR   PRIDE; Q80U93; -.
DR   Ensembl; ENSMUST00000065398; ENSMUSP00000066492; ENSMUSG00000001855.
DR   GeneID; 227720; -.
DR   KEGG; mmu:227720; -.
DR   UCSC; uc008jeh.1; mouse.
DR   CTD; 227720; -.
DR   MGI; MGI:1095411; Nup214.
DR   HOGENOM; HBG282886; -.
DR   HOVERGEN; HBG052683; -.
DR   InParanoid; Q80U93; -.
DR   OMA; FGQSPGF; -.
DR   OrthoDB; EOG41G33J; -.
DR   NextBio; 378784; -.
DR   ArrayExpress; Q80U93; -.
DR   Bgee; Q80U93; -.
DR   Genevestigator; Q80U93; -.
DR   GO; GO:0005643; C:nuclear pore; TAS:MGI.
DR   GO; GO:0005487; F:nucleocytoplasmic transporter activity; IMP:MGI.
DR   GO; GO:0006406; P:mRNA export from nucleus; IMP:MGI.
DR   GO; GO:0006606; P:protein import into nucleus; IMP:MGI.
DR   GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
DR   GO; GO:0055085; P:transmembrane transport; IEA:UniProtKB-KW.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
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.
PE   1: Evidence at protein level;
KW   Acetylation; Glycoprotein; mRNA transport; Nuclear pore complex;
KW   Nucleus; Phosphoprotein; Protein transport; Repeat; Translocation;
KW   Transport.
FT   CHAIN         1   2085       Nuclear pore complex protein Nup214.
FT                                /FTId=PRO_0000345014.
FT   DOMAIN      734    762       Leucine-zipper 1.
FT   DOMAIN      855    876       Leucine-zipper 2.
FT   REGION      479   2071       11 X 5 AA approximate repeats.
FT   REGION     1421   2079       18 X 4 AA approximate repeats.
FT   REGION     1439   2080       11 X 3 AA approximate repeats.
FT   COMPBIAS   1221   2085       Pro/Ser/Thr-rich.
FT   MOD_RES      40     40       Phosphoserine (By similarity).
FT   MOD_RES     143    143       N6-acetyllysine (By similarity).
FT   MOD_RES     416    416       Phosphothreonine (By similarity).
FT   MOD_RES     430    430       Phosphoserine (By similarity).
FT   MOD_RES     433    433       Phosphoserine (By similarity).
FT   MOD_RES     437    437       Phosphothreonine (By similarity).
FT   MOD_RES     440    440       Phosphoserine (By similarity).
FT   MOD_RES     639    639       Phosphoserine (By similarity).
FT   MOD_RES     645    645       Phosphoserine (By similarity).
FT   MOD_RES     651    651       Phosphoserine (By similarity).
FT   MOD_RES     660    660       Phosphoserine (By similarity).
FT   MOD_RES     672    672       Phosphoserine (By similarity).
FT   MOD_RES     930    930       Phosphoserine.
FT   MOD_RES     960    960       Phosphoserine (By similarity).
FT   MOD_RES     964    964       Phosphoserine (By similarity).
FT   MOD_RES     975    975       Phosphoserine (By similarity).
FT   MOD_RES     979    979       Phosphoserine (By similarity).
FT   MOD_RES    1142   1142       Phosphoserine (By similarity).
FT   MOD_RES    1162   1162       Phosphothreonine (By similarity).
FT   MOD_RES    1187   1187       Phosphoserine (By similarity).
FT   MOD_RES    1211   1211       Phosphothreonine (By similarity).
FT   MOD_RES    1324   1324       Phosphothreonine (By similarity).
FT   MOD_RES    1345   1345       Phosphoserine (By similarity).
FT   CONFLICT   1973   1973       S -> G (in Ref. 1; BAC65471).
SQ   SEQUENCE   2085 AA;  212979 MW;  C9998CC8BC27EE4A CRC64;
     MGDEMDAMIP EREMKDFQFR ALKKVRIFDS PEELPKERSS VLTISNKYGM LFAGGTNGLN
     VFPTKSLLIQ NKPGDDPNKI VDTIQGLNVP MKFPVHHLAL SCDSLTLSAC MMSSEYGSII
     AFFDVRTFSN QAKPLKRPFT YHKVSNDASG MVNDMKWNPT VPSMVAVCLA DGSISVLQVT
     DVVKVCATLP PSTGVTCVCW SPKGKQLAVG KQNGTVVQYL PTLQEKKVIP CPPFYESDHP
     VRVLDVLWIG TYVFTIVYAG ADGTLETCPD VVMALLPKKE EKHPEIFVNF MEPCYSSCTE
     RQHHYYLSYI EEWDLVLAAS AASTEVSILA RQNDQTNWES WLLEDSSRAE LPVTDKSDDS
     LPMGVAIDYT NEVEVTINEE KTLPPAPVLL LLSTDGVLCP FYMINQNPGV RSLIKTLELI
     STEGERQPKS SGSFPGTPSS PQAPQNLDAP ATASSPLPPV SAAPTSTFPM PSAAGSPSVF
     SFGPSSFKSS ASVTGEPPLY PTGSDSSRAA PGSGTSTFSF APPSKGSLAS TPAVAPVATS
     AAPFTFGFKP TLESTPMSST PNTGMKPSFP PSASSVKVNL NEKFTAVASS APVHSSTSTP
     SVLPFSSSPK PTASGPLSHP TPLPASSSSM PLKSSVSPSP AAGRSTQTAP SSAPSTGQKS
     PRVNPPVPKS GSSQAKALQP PVTEKQRPQW KDSDPVLAGI GEEIAHFQKE LEELKARTAK
     ACLQVGTSEE MKMLRTESDD LHTFLFEIRE TTESLHGDIS TLKTTLLEGF AGVEEAREQH
     GRNHDSGYLH LLYKRPLDPK SEAQLQEIRR LHQYVKFAVQ DVNDVLDLEW DRHLEQKKRQ
     RRLIVPERET LFNTLANNRE IINQQRKRLN QLVDSLQQLR LYNHTAPWSL PSALSTQSNS
     HSFDSDLECL LKTTIESHTK PSPRVPGKLS PAKQAQLRNF LAKRKTPPVR STAPASLSRS
     AFLSQRYYED LDEGSSASSV AQPLEGEDAR PTCTSVAQPL EGEDAQPICK EEEAVVPVPR
     HAPVVRTPSI QPSLLPQSMP FAKPHLIHSS SPAVMSSAVS TSATKVIPQG ADSTMLATKT
     VKHGAPGPSH TVAAPQAAAA AALRRQMASQ APAMSTLTES TLKTVPQVVN VQELRSNPSP
     PSAAMGSAVQ HSAAKTPHAV LTPVANSQAK QGSLINSFKP SGPTAASCQL SSGDKAVGQG
     TAKTESAATS TPSAAGQLNK PFSFASPGTF TFGTITPTPS SSFTATPGAG PPTKEPTQLE
     AFSFGGGGKP FSEAIPGNSP ATGATSAPST SVTAASLEDS APSSSKPAAP PETTVSSASS
     KLETPPSKLG ELLFPSSLAG ETLGSFSGLR VGQAEDSTKP VSKASSTNLA GAQPAKPSGV
     SFPNTSVLGK PVEPAVTSSV SPAPAAPASA LNVSTSSSSA TVFGSVPLTS AGPPGLISFG
     GAALASSKAS FSFGNQQTSS STASSATPTS TSVAPSLPAS FPTLSFGGLL SSPSASSLPV
     SSGKSTEEAA PPAVPDKSDS SEVSATTPSL PVQPQSTQAS LQTSDPVKKE PVLVQTTDSS
     PSRPASSASF VASTESMPVT LGAPDSKIEA VSPASTFAGP GQAAVATAVL PGAGSAATEA
     SGTPTTSTVS SSSPTSATET AVFGTATSGS SVFTQPPAAS SSSAFSQLSS NTATAPSATP
     VFGQVAASIT STAAATPQAS SSGFGSPAFG ASAPGVFGQT AFGQTPAFGQ ATSSPASGFS
     FSQPGFSSVP AFGQSVSSTP ASTSANVFGA TSSTSSPGSF SFGQASTNTG GTLFGQNNPP
     AFGQSPGFGQ GSSVFGGTSA TTSTAAPSGF SFCQASGFGS SNTGSVFGQA ANTGGSVFGQ
     SSTSSGGVFG SGNATRGGGF FSGLGGKPSQ DAANKNPFSS AGGGFGSTAA PNTSNLFGNS
     GAKTFGGFGS SSFGEQKPAG TFSSGGGSVA SQGFGFSTPN KTGGFGAAPV FGSPPTFGGS
     PGFGGVPAFG SAPAFTSPLG STGGKVFGEG TAAASAGGFG FGSSGNTASF GTLASQNAPT
     FGSLSQQTSG FGTPSSGFAG FGSGTGAFTF GSSNSSVQGF GGWRS
//
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;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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;
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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   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   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   UBN2_MOUSE              Reviewed;        1314 AA.
AC   Q80WC1; Q69Z27; Q80ZZ9; Q8BQ40; Q8BRI2;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=Ubinuclein-2;
GN   Name=Ubn2; Synonyms=Kiaa2030;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; 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 169-1313 (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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 130-1313 (ISOFORM 4), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 883-1313 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain, 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 676-1314 (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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., 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=4;
CC       Name=1;
CC         IsoId=Q80WC1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80WC1-2; Sequence=VSP_027026, VSP_027029;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q80WC1-3; Sequence=VSP_027023, VSP_027025, VSP_027027,
CC                                  VSP_027028;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q80WC1-4; Sequence=VSP_027024;
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 ubinuclein family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC31801.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC043095; AAH43095.1; -; mRNA.
DR   EMBL; BC051458; AAH51458.1; -; mRNA.
DR   EMBL; AK044162; BAC31801.1; ALT_INIT; mRNA.
DR   EMBL; AK051609; BAC34690.1; -; mRNA.
DR   EMBL; AK173339; BAD32617.1; -; mRNA.
DR   IPI; IPI00330578; -.
DR   IPI; IPI00342731; -.
DR   IPI; IPI00854896; -.
DR   IPI; IPI00854946; -.
DR   RefSeq; NP_796159.3; NM_177185.4.
DR   UniGene; Mm.302831; -.
DR   UniGene; Mm.445711; -.
DR   ProteinModelPortal; Q80WC1; -.
DR   PhosphoSite; Q80WC1; -.
DR   PRIDE; Q80WC1; -.
DR   Ensembl; ENSMUST00000039127; ENSMUSP00000036188; ENSMUSG00000038538.
DR   GeneID; 320538; -.
DR   KEGG; mmu:320538; -.
DR   UCSC; uc009bke.1; mouse.
DR   CTD; 320538; -.
DR   MGI; MGI:2444236; Ubn2.
DR   eggNOG; roNOG12344; -.
DR   GeneTree; ENSGT00530000063595; -.
DR   HOGENOM; HBG278713; -.
DR   InParanoid; Q80WC1; -.
DR   OMA; VAQSSHS; -.
DR   OrthoDB; EOG4G1MGR; -.
DR   PhylomeDB; Q80WC1; -.
DR   NextBio; 396921; -.
DR   ArrayExpress; Q80WC1; -.
DR   Bgee; Q80WC1; -.
DR   CleanEx; MM_D130059P03RIK; -.
DR   Genevestigator; Q80WC1; -.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Phosphoprotein.
FT   CHAIN         1   1314       Ubinuclein-2.
FT                                /FTId=PRO_0000295726.
FT   COMPBIAS     29    109       Pro-rich.
FT   COMPBIAS    248    331       Lys-rich.
FT   COMPBIAS    853   1192       Ser-rich.
FT   MOD_RES      13     13       Phosphoserine (By similarity).
FT   MOD_RES     418    418       Phosphothreonine (By similarity).
FT   MOD_RES     570    570       Phosphoserine.
FT   MOD_RES    1116   1116       N6-acetyllysine (By similarity).
FT   VAR_SEQ     297    298       SE -> K (in isoform 3).
FT                                /FTId=VSP_027023.
FT   VAR_SEQ     451    451       V -> VVS (in isoform 4).
FT                                /FTId=VSP_027024.
FT   VAR_SEQ     674    674       V -> VKAVLVKTLPVRSFPTML (in isoform 3).
FT                                /FTId=VSP_027025.
FT   VAR_SEQ    1192   1203       STAGASLLANAS -> FYQKPQRLRTKQ (in isoform
FT                                2).
FT                                /FTId=VSP_027026.
FT   VAR_SEQ    1192   1194       STA -> PSS (in isoform 3).
FT                                /FTId=VSP_027027.
FT   VAR_SEQ    1195   1314       Missing (in isoform 3).
FT                                /FTId=VSP_027028.
FT   VAR_SEQ    1204   1314       Missing (in isoform 2).
FT                                /FTId=VSP_027029.
FT   CONFLICT    284    284       P -> S (in Ref. 2; BAC34690).
FT   CONFLICT    867    867       Missing (in Ref. 1; AAH51458).
SQ   SEQUENCE   1314 AA;  141740 MW;  59CE63A74EE149E5 CRC64;
     MAEPRRVAFI SLSPVRRREA DFAGAEREPP RLEPQPYREP ARAEPAPRAD AQPPARDKPL
     PQREVSRAEP PMALQREPPR PEPPPPPLPL QTPPPRESAS RAEPPPRPPK ETVRLELVLK
     DPTDESCVEF SYPELLLCGE QRKKLVHTED PFTDEHKERQ EVEMLAKKFE MKYGGKARKH
     RKDRLQDLID IGFGYDETDP FIDNSEAYDE LVPASLTTKY GGFYINTGTL QFRQASDTEE
     DDFTDNQKHK PPKVPKIKED DIEVKKRKRK EEGEKEKKPR KKVPKQLGVV ALNSHKSEKK
     KKRYKDSLSL AAMIRKFQKE KDALKKESTP KVPVTPSSSS LPKPPCVTTA LGDDIPDLGL
     NSADPDLPIF VSTNEHELFQ EAENALEMLD DFDFDRLLDA TSDGSPLSES GGENGNTTHP
     TFPSQVVPKV VPTLPEGLPV LLEKRIEDLR VAAKLFDEEG RKKFFTQDMN NILLDIELQL
     QELGPVIRSG VYSHLEAFVP CNKETLVKRL KKLHLNVQDD RLREPLQKLK LAVSNVMPEQ
     LFKYQEDCQA RSQAKCAKLQ ADEEREKNGS DDDDDEKPGK RVIGPRKKFH WDDTIRTLLC
     NLVEIKLGCY ELEPNKSQSA EDYLKSFMET EVKPLWPKGW MQARMLFKES RSVHNHLTSA
     PAKKKVIPAS KPKVKECSPK KDPKAPASVV ASGGGPSTSS STSIVASASS SSAPAQETIC
     LDDSLDEDLS FPSASLDLVS EALAVINNGN KGPSVGSRLN VPTTKPRPGL REEKLASIMS
     KLPLATPKKL DSTQTAHSSS LIAGHTGPVP KKPQDLAHTG ISSGLIAGSS IQNPKVSLEP
     LPARLLQQGL QRSSQIHASS SSQTHVSSSQ AQAAASSHAL GTSEAQDASS LTQVTKVHQH
     SAVQQNYVSP LQATISKSQT NPVVKLSNNP QLSCSSQLLK TSDKPLMYRL PLSTPSPGNG
     SQGPHPLVSR TAPSTTTSSN YLAKAMVSQI STQGFKSPFS MAASPKLAAS PKPATSPKPL
     PSPKPSVSPK PSLSAKPSIS TKQISKSNPA PKPAVCPSSS SPNTLVAQSS HSTSNNPVHK
     QPSGMNISRQ SPTLNLLPSN RTSGLPTTKT LQAPSKLTNS SSTGTAGKNS LSGIPMNVPA
     SRGSNLNSSG ANRTSLSGGT GSGTQGATKP LSTPHRPTSA SGSSVVTASV QSTAGASLLA
     NASPLTLMTS PLSVTNQTVT PFGMLGGLVP VTMPFQFPLE LLGFGTDTAG VTATSGSTSA
     ALHHSLTQNL LKSLQPGAQH AAALPHSPLP AHLQQAFNDG GQSKGDTKLP RKPQ
//
ID   AGFG2_MOUSE             Reviewed;         479 AA.
AC   Q80WC7; Q8BKS5; Q99J67;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Arf-GAP domain and FG repeats-containing protein 2;
DE   AltName: Full=HIV-1 Rev-binding protein-like protein;
DE   AltName: Full=Rev/Rex activation domain-binding protein related;
DE            Short=RAB-R;
GN   Name=Agfg2; Synonyms=Hrbl, Rabr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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 Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, 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 247-479 (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   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).
CC   -!- SUBUNIT: Interacts with EPS15R.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80WC7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80WC7-2; Sequence=VSP_010669, VSP_010670;
CC   -!- DOMAIN: Contains FG repeats and 4 N-P-F repeats.
CC   -!- SIMILARITY: Contains 1 Arf-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; BC003330; AAH03330.1; -; mRNA.
DR   EMBL; BC046788; AAH46788.1; -; mRNA.
DR   EMBL; AK050881; BAC34441.1; -; mRNA.
DR   IPI; IPI00114911; -.
DR   IPI; IPI00761792; -.
DR   RefSeq; NP_663541.1; NM_145566.1.
DR   RefSeq; NP_835456.1; NM_178162.2.
DR   UniGene; Mm.260869; -.
DR   ProteinModelPortal; Q80WC7; -.
DR   SMR; Q80WC7; 16-155.
DR   STRING; Q80WC7; -.
DR   PhosphoSite; Q80WC7; -.
DR   PRIDE; Q80WC7; -.
DR   Ensembl; ENSMUST00000031736; ENSMUSP00000031736; ENSMUSG00000029722.
DR   GeneID; 231801; -.
DR   KEGG; mmu:231801; -.
DR   UCSC; uc009adl.1; mouse.
DR   UCSC; uc009ado.1; mouse.
DR   CTD; 231801; -.
DR   MGI; MGI:2443267; Agfg2.
DR   GeneTree; ENSGT00560000077249; -.
DR   HOVERGEN; HBG006551; -.
DR   OrthoDB; EOG4S1T7B; -.
DR   NextBio; 380751; -.
DR   ArrayExpress; Q80WC7; -.
DR   Bgee; Q80WC7; -.
DR   Genevestigator; Q80WC7; -.
DR   GermOnline; ENSMUSG00000029722; 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: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   Acetylation; Alternative splicing; Metal-binding; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    479       Arf-GAP domain and FG repeats-containing
FT                                protein 2.
FT                                /FTId=PRO_0000204829.
FT   DOMAIN       27    153       Arf-GAP.
FT   ZN_FING      47     70       C4-type.
FT   MOD_RES     174    174       N6-acetyllysine (By similarity).
FT   VAR_SEQ     253    289       VGQTPAHGGFANFDAFSSSPSSSTFGSLPPSVQAPFQ ->
FT                                GKYYPGAGTRLRRICITAKTSLVHRGLTFLCGWGQGA (in
FT                                isoform 2).
FT                                /FTId=VSP_010669.
FT   VAR_SEQ     290    479       Missing (in isoform 2).
FT                                /FTId=VSP_010670.
SQ   SEQUENCE   479 AA;  48968 MW;  BE299F70C28D6457 CRC64;
     MVMAAKKGPG PGGGVGGSKA EAEAASEVWC RRVRELGGCS QAGNRHCFEC AQRGVTYVDI
     TVGSFVCTTC SGLLRGLNPP HRVKSISMTT FTEPEVLFLQ SRGNEVCRKI WLGLFDARTS
     LIPDSRDPQK VKEFLQEKYE KKRWYVPPEQ VKGPSYSKGS VSATPVQGSV PEGKPIRTLL
     GDPVPSLSDP ASTSSQPGSQ SQARSSSQAR SSQPPSHSST KKASTDLLAD IGGDPFAAPQ
     VVPAFASFPG FGVGQTPAHG GFANFDAFSS SPSSSTFGSL PPSVQAPFQA QPTPAGSGQM
     SAFGVAPLAA ASQPNNLADV GGLLGPRMAA GGLPGSVFGM PSQVPALQSA VPGVSGSGGL
     PFGAYTNPFA TPAQAQLPST NPFQPNGLAS GPGFGMSSVR PGLLQPVPPS GAFASPFSAP
     VFPTQAGLAD QQNGSSFGDL GTSKLGQRPL SQPAGISTNP FMTGSSAFAS KPPTTNPFL
//
ID   HPLN4_MOUSE             Reviewed;         400 AA.
AC   Q80WM4; Q05AB1; Q80XX2;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Hyaluronan and proteoglycan link protein 4;
DE   AltName: Full=Brain link protein 2;
DE   Flags: Precursor;
GN   Name=Hapln4; Synonyms=Bral2, Lpr4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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=22662284; PubMed=12663660; DOI=10.1074/jbc.M213100200;
RA   Spicer A.P., Joo A., Bowling R.A. Jr.;
RT   "A hyaluronan binding link protein gene family whose members are
RT   physically linked adjacent to chondroitin sulfate proteoglycan core
RT   protein genes: the missing links.";
RL   J. Biol. Chem. 278:21083-21091(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=14550776; DOI=10.1016/S1044-7431(03)00133-7;
RA   Bekku Y., Su W.-D., Hirakawa S., Faessler R., Ohtsuka A., Kang J.S.,
RA   Sanders J., Murakami T., Ninomiya Y., Oohashi T.;
RT   "Molecular cloning of Bral2, a novel brain-specific link protein, and
RT   immunohistochemical colocalization with brevican in perineuronal
RT   nets.";
RL   Mol. Cell. Neurosci. 24:148-159(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RA   Czipri M., Nesterovitch A.B., Glant T.T.;
RT   "Discoordinate expression of link proteins and skeletal tissue
RT   proteoglycans (aggrecan and versican) in different organs from early
RT   embryonic to adult age of mice.";
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [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   -!- FUNCTION: Binds to hyaluronic acid and may be involved in
CC       formation of the extracellular matrix.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in brain where it is
CC       found mainly throughout the midbrain and hindbrain in a
CC       perineuronal net pattern.
CC   -!- DEVELOPMENTAL STAGE: Expression begins at embryonic day 20 and
CC       increases thereafter. Expression continues into adulthood.
CC   -!- SIMILARITY: Belongs to the HAPLN family.
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 2 Link domains.
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DR   EMBL; AY262758; AAP22050.1; -; mRNA.
DR   EMBL; AB107882; BAC79076.1; -; mRNA.
DR   EMBL; AY269789; AAP12625.1; -; mRNA.
DR   EMBL; AK034300; BAC28664.1; -; mRNA.
DR   EMBL; BC125339; AAI25340.1; -; mRNA.
DR   EMBL; BC125341; AAI25342.1; -; mRNA.
DR   IPI; IPI00229184; -.
DR   RefSeq; NP_808568.1; NM_177900.4.
DR   UniGene; Mm.152048; -.
DR   ProteinModelPortal; Q80WM4; -.
DR   SMR; Q80WM4; 47-270, 273-366.
DR   PhosphoSite; Q80WM4; -.
DR   PRIDE; Q80WM4; -.
DR   Ensembl; ENSMUST00000007738; ENSMUSP00000007738; ENSMUSG00000007594.
DR   GeneID; 330790; -.
DR   KEGG; mmu:330790; -.
DR   UCSC; uc009lyr.1; mouse.
DR   CTD; 330790; -.
DR   MGI; MGI:2679531; Hapln4.
DR   GeneTree; ENSGT00550000074236; -.
DR   HOGENOM; HBG402950; -.
DR   HOVERGEN; HBG051922; -.
DR   InParanoid; Q80WM4; -.
DR   OMA; CGGRRPG; -.
DR   OrthoDB; EOG4G7BZJ; -.
DR   NextBio; 399552; -.
DR   ArrayExpress; Q80WM4; -.
DR   Bgee; Q80WM4; -.
DR   CleanEx; MM_HAPLN4; -.
DR   Genevestigator; Q80WM4; -.
DR   GermOnline; ENSMUSG00000007594; Mus musculus.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005540; F:hyaluronic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   InterPro; IPR016186; C-type_lectin-like.
DR   InterPro; IPR016187; C-type_lectin_fold.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR000538; Link.
DR   Gene3D; G3DSA:3.10.100.10; C-type_lectin-like; 2.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF07686; V-set; 1.
DR   Pfam; PF00193; Xlink; 2.
DR   PRINTS; PR01265; LINKMODULE.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00445; LINK; 2.
DR   SUPFAM; SSF56436; C-type_lectin_fold; 2.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS01241; LINK_1; 1.
DR   PROSITE; PS50963; LINK_2; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Extracellular matrix; Glycoprotein; Hyaluronic acid;
KW   Immunoglobulin domain; Proteoglycan; Repeat; Secreted; Signal.
FT   SIGNAL        1     30       Potential.
FT   CHAIN        31    400       Hyaluronan and proteoglycan link protein
FT                                4.
FT                                /FTId=PRO_0000013193.
FT   DOMAIN       47    155       Ig-like C2-type.
FT   DOMAIN      164    266       Link 1.
FT   DOMAIN      271    363       Link 2.
FT   CARBOHYD    133    133       N-linked (GlcNAc...) (Potential).
FT   DISULFID     69    144       By similarity.
FT   DISULFID    186    264       By similarity.
FT   DISULFID    210    231       By similarity.
FT   DISULFID    291    361       By similarity.
FT   DISULFID    316    337       By similarity.
FT   CONFLICT     76     76       A -> D (in Ref. 1; AAP22050).
SQ   SEQUENCE   400 AA;  42809 MW;  6656BF0714698429 CRC64;
     MACAPGALGH RALWAVAWGL LLLVPVLAGA QRGRKKVVHV LEGESGSVVV QTAPGQVVSH
     RGGTIVLPCR YHYEAAAHGH DGVRLKWTKV VDPLAFADVF VALGPQHRAF GPYRGRAELQ
     NDGPGDASLV LRNVTLQDYG RYECEVTNEL EDDVGMVKLD LEGVVFPYHP RGGRYKMTFV
     EAQRACAEQD GILASAEQLH AAWRDGLDWC NAGWLRDGSV QYPVSHAREP CGGTGSTGAG
     GGTNGGVRNY GYRHNAEERY DAFCFTSNLP GRVFFLKPLR PVALAGAVRA CAARGATVAK
     VGQLFAAWKL QLLDRCTAGW LADGSARYPI VNPRTRCGGP RPGVRSLGFP DASRRLFGVY
     CYRAPGAPDP APGGWGWGWA GGGGWAGGSR DPAAWTPLRV
//
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).
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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   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;
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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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   T106B_MOUSE             Reviewed;         275 AA.
AC   Q80X71; Q9D737;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Transmembrane protein 106B;
GN   Name=Tmem106b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; 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=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: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the TMEM106 family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK009646; BAB26411.1; -; mRNA.
DR   EMBL; BC050246; AAH50246.1; -; mRNA.
DR   IPI; IPI00330680; -.
DR   RefSeq; NP_082268.2; NM_027992.3.
DR   UniGene; Mm.27742; -.
DR   ProteinModelPortal; Q80X71; -.
DR   PhosphoSite; Q80X71; -.
DR   PRIDE; Q80X71; -.
DR   Ensembl; ENSMUST00000031556; ENSMUSP00000031556; ENSMUSG00000029571.
DR   GeneID; 71900; -.
DR   KEGG; mmu:71900; -.
DR   UCSC; uc009ayk.1; mouse.
DR   CTD; 71900; -.
DR   MGI; MGI:1919150; Tmem106b.
DR   eggNOG; roNOG05660; -.
DR   GeneTree; ENSGT00390000013076; -.
DR   HOGENOM; HBG715151; -.
DR   HOVERGEN; HBG055025; -.
DR   InParanoid; Q80X71; -.
DR   OMA; FDFCTLI; -.
DR   OrthoDB; EOG4640D1; -.
DR   NextBio; 334884; -.
DR   ArrayExpress; Q80X71; -.
DR   Bgee; Q80X71; -.
DR   CleanEx; MM_TMEM106B; -.
DR   Genevestigator; Q80X71; -.
DR   GermOnline; ENSMUSG00000029571; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR009790; DUF1356_TMEM106.
DR   Pfam; PF07092; DUF1356; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    275       Transmembrane protein 106B.
FT                                /FTId=PRO_0000242651.
FT   TRANSMEM     98    118       Helical; (Potential).
FT   MOD_RES      34     34       Phosphoserine (By similarity).
FT   MOD_RES      51     51       Phosphotyrosine (By similarity).
FT   CONFLICT    219    219       S -> Y (in Ref. 1; BAB26411).
SQ   SEQUENCE   275 AA;  31172 MW;  4075221F1280EC4A CRC64;
     MGKSLSHLPL HSNKEDGYDG VTSTDNMRNG LVSSEVHNED GRNGDVSQFP YVEFTGRDSV
     TCPTCQGTGR IPRGQENQLV ALIPYSDQRL RPRRTKLYVM ASVFVCLLLS GLAVFFLFPR
     SIEVKYIGVK SAYVSYDAEK RTIYLNITNT LNITNNNYYS VEVENITAQV QFSKTVIGKA
     RLNNITNIGP LDMKQIDYTV PTVIAEEMSY MYDFCTLLSI KVHNIVLMMQ VTVTTAYFGH
     SEQISQERYQ YVDCGRNTTY QLAQSEYLNV LQPQQ
//
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   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   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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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   ZN598_MOUSE             Reviewed;         908 AA.
AC   Q80YR4; Q6KAT0; Q8R3S1;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Zinc finger protein 598;
GN   Name=Znf598; Synonyms=Zfp598;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; 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=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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 68-908 (ISOFORM 3).
RC   STRAIN=Czech II; 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).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q80YR4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80YR4-2; Sequence=VSP_020667;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q80YR4-3; Sequence=VSP_020666;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD21377.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK131127; BAD21377.1; ALT_INIT; mRNA.
DR   EMBL; BC024690; AAH24690.1; -; mRNA.
DR   EMBL; BC050859; AAH50859.1; -; mRNA.
DR   IPI; IPI00153808; -.
DR   IPI; IPI00788350; -.
DR   IPI; IPI00788432; -.
DR   RefSeq; NP_898972.1; NM_183149.1.
DR   UniGene; Mm.219581; -.
DR   ProteinModelPortal; Q80YR4; -.
DR   SMR; Q80YR4; 21-72, 126-269.
DR   PhosphoSite; Q80YR4; -.
DR   PRIDE; Q80YR4; -.
DR   Ensembl; ENSMUST00000047179; ENSMUSP00000038367; ENSMUSG00000041130.
DR   Ensembl; ENSMUST00000088395; ENSMUSP00000085737; ENSMUSG00000041130.
DR   GeneID; 213753; -.
DR   KEGG; mmu:213753; -.
DR   UCSC; uc008axn.1; mouse.
DR   UCSC; uc008axo.1; mouse.
DR   UCSC; uc008axp.1; mouse.
DR   CTD; 213753; -.
DR   MGI; MGI:2670965; Zfp598.
DR   eggNOG; roNOG06542; -.
DR   GeneTree; ENSGT00390000014178; -.
DR   HOGENOM; HBG505725; -.
DR   HOVERGEN; HBG055813; -.
DR   InParanoid; Q80YR4; -.
DR   OMA; HELFCCK; -.
DR   OrthoDB; EOG444KK1; -.
DR   PhylomeDB; Q80YR4; -.
DR   NextBio; 374085; -.
DR   ArrayExpress; Q80YR4; -.
DR   Bgee; Q80YR4; -.
DR   CleanEx; MM_ZFP598; -.
DR   Genevestigator; Q80YR4; -.
DR   GermOnline; ENSMUSG00000041130; Mus musculus.
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   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   SMART; SM00355; ZnF_C2H2; 5.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 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; Metal-binding; Phosphoprotein; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    908       Zinc finger protein 598.
FT                                /FTId=PRO_0000250569.
FT   ZN_FING      27     67       RING-type.
FT   ZN_FING     185    208       C2H2-type.
FT   COMPBIAS    645    729       Pro-rich.
FT   COMPBIAS    730    741       Thr-rich.
FT   MOD_RES     304    304       Phosphotyrosine (By similarity).
FT   MOD_RES     433    433       Phosphoserine (By similarity).
FT   VAR_SEQ     333    335       Missing (in isoform 3).
FT                                /FTId=VSP_020666.
FT   VAR_SEQ     626    653       Missing (in isoform 2).
FT                                /FTId=VSP_020667.
FT   CONFLICT    600    600       L -> M (in Ref. 2; AAH24690).
SQ   SEQUENCE   908 AA;  99192 MW;  528DE75B72EDE40B CRC64;
     MAAAAGAEGR RAALEAVAAP ERGGGSCVLC CGDLEATALG RCDHPVCYRC STKMRVLCEQ
     RYCAVCREEL RQVVFGKKLP AFALIPIHQL QHEKKYDIYF ADGKVFALYR QLLQHECPRC
     PHLPPFSLFG DLEQHMRKQH ELFCCKLCLK HLKIFTYERK WYSRKDLARH RMQGDPDDTS
     HRGHPLCKFC DERYLDNDEL LKHLRRDHYF CHFCDSDGAQ DYYSDYAYLR EHFREKHFLC
     EEGRCSTEQF THAFRTEIDL KAHKTACHSR SRAEARQNRQ IDLQFSFAPR HSRRSEGVVS
     GEDYEEVDRY NRQGRAGRAS GRGAQQNRRG SWRYKREEED REVAAAIRAS VAAQQQEETQ
     RVEDREEGSR PKKEEAAARV PEEPRGHRRL PRAQGEGSGS KEASANGPVS QEAFPATGPG
     PVVALSNTLP PPSPELKEED FPSLCASTSS CCTAVTPGSV GLALAYPGPP RGKNTFQEED
     FPALVSSAPK PSSAPSSLIS AWNSGCSKKG NLPTPGSQAV VGGSQPPRKA GKGSRGGRKG
     GPAPVDEEDS GGLTVQGLRS VPTTVAVSSL LAPATNQSSA KVGKKKKVGS EKPGATSSPL
     LPPDHTPKPS GAEQVLEAPL SKAEVPVTIV VNGHSEGSAL VRSAPKEPPG LPRPLGPLPC
     PIPQEDFPAL GGPCPPRMPP PPGFSTVVLL KGTPPPPPPP PGLVPPISKP PPGFSSLLPS
     SHSACAPSPT TTTTTTTTTK TPGLAPTPQA YLVPENFRER NLQLIQSIKD FLQSDEACFS
     KFKSHSGEFR QGMISAAQYY KSCRDLLGES FQKIFSELLA LLPDTAKQQE LLSAHTDFCS
     REKPPNSRSK RNKKNVWQTS TQQLGLDCCV CPTCQQVLAH GDVSSHQALH AARDDDFPSL
     QAIARIIT
//
ID   SHAN2_MOUSE             Reviewed;        1476 AA.
AC   Q80Z38; Q3UTK4; Q5DU07;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-FEB-2011, entry version 56.
DE   RecName: Full=SH3 and multiple ankyrin repeat domains protein 2;
DE            Short=Shank2;
DE   AltName: Full=Cortactin-binding protein 1;
DE            Short=CortBP1;
GN   Name=Shank2; Synonyms=Cortbp1, Kiaa1022;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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 GRID2.
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-350 (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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 345-1476 (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   TISSUE SPECIFICITY.
RX   MEDLINE=98414600; PubMed=9742101;
RA   Du Y., Weed S.A., Xiong W.-C., Marshall T.D., Parsons J.T.;
RT   "Identification of a novel cortactin SH3 domain-binding protein and
RT   its localization to growth cones of cultured neurons.";
RL   Mol. Cell. Biol. 18:5838-5851(1998).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-586; THR-730; THR-903
RP   AND SER-1338, 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   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-1292, 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 THR-1340, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
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-1334 AND SER-1338, 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: 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 (By similarity).
CC   -!- SUBUNIT: Interacts with CCTN/cortactin SH3 domain, DLGAP1/GKAP and
CC       alpha-latrotoxin receptor 1. Is part of a complex with DLG4/PSD-95
CC       and DLGAP1/GKAP. Interacts with DNM2 and BAIAP2. Interacts with
CC       SLC9A3, PLCB3 and CFTR. Interacts with DBNL (By similarity).
CC       Interacts with GRID2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell junction, synapse. Cell
CC       junction, synapse, postsynaptic cell membrane, postsynaptic
CC       density. Cell projection, growth cone (By similarity).
CC       Note=Cytoplasm, postsynaptic density of neuronal cells.
CC       Colocalizes with cortactin in growth cones in differentiating
CC       hippocampal neurons (By similarity). Present in the dendritic
CC       spines of cerebellar Purkinje cells.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80Z38-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80Z38-2; Sequence=VSP_020040;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain.
CC   -!- DOMAIN: The PDZ domain is required for interaction with GRID2,
CC       PLCB3, SLC9A3 and CFTR.
CC   -!- SIMILARITY: Belongs to the SHANK family.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) 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; AB099695; BAC58120.1; -; mRNA.
DR   EMBL; AK139360; BAE23976.1; -; mRNA.
DR   EMBL; AK220363; BAD90424.1; -; mRNA.
DR   IPI; IPI00349908; -.
DR   IPI; IPI00757097; -.
DR   RefSeq; NP_001074839.2; NM_001081370.2.
DR   RefSeq; NP_001106844.2; NM_001113373.2.
DR   UniGene; Mm.323725; -.
DR   ProteinModelPortal; Q80Z38; -.
DR   SMR; Q80Z38; 149-233, 240-343, 1410-1473.
DR   STRING; Q80Z38; -.
DR   PhosphoSite; Q80Z38; -.
DR   PRIDE; Q80Z38; -.
DR   Ensembl; ENSMUST00000084391; ENSMUSP00000081426; ENSMUSG00000037541.
DR   GeneID; 210274; -.
DR   KEGG; mmu:210274; -.
DR   UCSC; uc009kqf.1; mouse.
DR   CTD; 210274; -.
DR   MGI; MGI:2671987; Shank2.
DR   eggNOG; roNOG06402; -.
DR   GeneTree; ENSGT00510000046474; -.
DR   HOVERGEN; HBG054027; -.
DR   NextBio; 372912; -.
DR   ArrayExpress; Q80Z38; -.
DR   Bgee; Q80Z38; -.
DR   CleanEx; MM_SHANK2; -.
DR   Genevestigator; Q80Z38; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030426; C:growth cone; 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:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW   Cytoplasm; Glycoprotein; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; SH3 domain; SH3-binding; Synapse.
FT   CHAIN         1   1476       SH3 and multiple ankyrin repeat domains
FT                                protein 2.
FT                                /FTId=PRO_0000247760.
FT   DOMAIN      147    206       SH3.
FT   DOMAIN      247    341       PDZ.
FT   DOMAIN     1413   1476       SAM.
FT   MOTIF      1169   1175       SH3-binding (Potential).
FT   COMPBIAS     24     27       Poly-Arg.
FT   COMPBIAS    355    358       Poly-Pro.
FT   COMPBIAS    513    560       Pro-rich.
FT   COMPBIAS   1017   1020       Poly-Pro.
FT   COMPBIAS   1169   1211       Pro-rich.
FT   COMPBIAS   1348   1353       Poly-Pro.
FT   MOD_RES     586    586       Phosphoserine.
FT   MOD_RES     730    730       Phosphothreonine.
FT   MOD_RES     903    903       Phosphothreonine.
FT   MOD_RES    1334   1334       Phosphoserine.
FT   MOD_RES    1338   1338       Phosphoserine.
FT   MOD_RES    1340   1340       Phosphothreonine.
FT   CARBOHYD   1292   1292       O-linked (GlcNAc...).
FT   VAR_SEQ     380    383       Missing (in isoform 2).
FT                                /FTId=VSP_020040.
SQ   SEQUENCE   1476 AA;  158979 MW;  FDD71D40CC8B16E5 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 GLSLVDKASV RKKKDKPEEI VPASKPSRTA ENVAIESRVA
     TIKQRPTSRC FPAASDVNSV YERQGIAVMT PTVPGSPKGP FLGLPRGTMR RQKSIDSRIF
     LSGITEEERQ FLAPPMLKFT RSLSMPDTSE DIPPPPQSVP PSPPPPSPTT YNCPRSPTPR
     VYGTIKPAFN QNPVVAKVPP ATRSDTVATM MREKGMFYRR ELDRFSLDSE DVYSRSPAPQ
     AAFRTKRGQM PENPYSEVGK IASKAVYVPA KPARRKGVLV KQSNVEDSPE KTCSIPIPTI
     IVKEPSTSSS GKSSQGSSME IDPQATEPGQ LRPDDSLTVS SPFAAAIAGA VRDREKRLEA
     RRNSPAFLST DLGDEDVGLG PPAPRMQASK FPEEGGFGDE DETEQPLLPT PGAAPRELEN
     HFLGGGEAGA QGEAGGPLSS TSKAKGPESG PAAPLKSSSP AGPENYVHPL TGRLLDPSSP
     LALALSARDR AMQESQQGHK GEAPKADLNK PLYIDTKMRP SVESGFPPVT RQNTRGPLRR
     QETENKYETD LGKDRRADDK KNMLINIVDT AQQKSAGLLM VHTVDVPMAG PPLEEEEDRE
     DGDTKPDHSP STVPEGVPKT EGALQISAAP EPAVAPGRTI VAAGSVEEAV ILPFRIPPPP
     LASVDLDEDF LFTEPLPPPL EFANSFDIPD DRAASVPALA DLVKQKKNDT PQPPTLNSSQ
     PANSTDSKKP AGISNCLPSS FLPPPESFDA VTDSGIEEVD SRSSSDHHLE TTSTISTVSS
     ISTLSSEGGE SMDTCTVYAD GQAFVVDKPP VPPKPKMKPI VHKSNALYQD TLPEEDTDGF
     VIPPPAPPPP PGSAQAGVAK VIQPRTSKLW GDVPEVKSPI LSGPKANVIS ELNSILQQMN
     RGKSVKPGEG LELPVGAKSA NLAPRSPEVM STVSGTRSTT VTFTVRPGTS QPITLQSRPP
     DYESRTSGPR RAPSPVVSPT ELSKEILPTP PPPSATAASP SPTLSDVFSL PSQSPAGDLF
     GLNPAGRSRS PSPSILQQPI SNKPFTTKPV HLWTKPDVAD WLESLNLGEH KETFMDNEID
     GSHLPNLQKE DLIDLGVTRV GHRMNIERAL KQLLDR
//
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.
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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   Q80ZX0_MOUSE            Unreviewed;      1251 AA.
AC   Q80ZX0;
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=Sec24 related gene family, member B (S. cerevisiae);
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The 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; BC046776; AAH46776.1; -; mRNA.
DR   IPI; IPI00331016; -.
DR   RefSeq; NP_997092.1; NM_207209.2.
DR   UniGene; Mm.192303; -.
DR   HSSP; P40482; 1PD1.
DR   ProteinModelPortal; Q80ZX0; -.
DR   SMR; Q80ZX0; 503-1251.
DR   STRING; Q80ZX0; -.
DR   PhosphoSite; Q80ZX0; -.
DR   PRIDE; Q80ZX0; -.
DR   Ensembl; ENSMUST00000001079; ENSMUSP00000001079; ENSMUSG00000001052.
DR   GeneID; 99683; -.
DR   KEGG; mmu:99683; -.
DR   UCSC; uc008rit.1; mouse.
DR   CTD; 99683; -.
DR   MGI; MGI:2139764; Sec24b.
DR   GeneTree; ENSGT00590000082962; -.
DR   HOGENOM; HBG746961; -.
DR   HOVERGEN; HBG054850; -.
DR   InParanoid; Q80ZX0; -.
DR   OMA; QGFPSTC; -.
DR   PhylomeDB; Q80ZX0; -.
DR   NextBio; 354069; -.
DR   ArrayExpress; Q80ZX0; -.
DR   Bgee; Q80ZX0; -.
DR   Genevestigator; Q80ZX0; -.
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.
SQ   SEQUENCE   1251 AA;  135551 MW;  4E36C4C0C0F79D25 CRC64;
     MSAPAGSPHP AAGARMPPKL GGAVSGLAPP QQNGPAQSPM QVPSGYGLPH QNYMVPSGHY
     SQGPGKMTSL PLDSQCDSYY SRPYTVPTQN SGTPSSANQP GAQQMYGRGP SAPHMGGSMP
     GSFQGIPASA SHSYSSASQP YSSLGNRYSS PTTYSANASV ASQGYPSTCS HYPISTVSNV
     VYPNVSYPSL PASEPYGQMF TSQSAPPPAR PVKESYSGPS TALTYPSRPP PPPSQHQQQQ
     QQQQQQQQQQ QSHSGYSSLP WSGPALPPAQ DSLIRNQMGS LATANSHPTN NENVQPPKSS
     SVVSTVLPGP SSTRMPPAPS HPVGPVPSAP PPPEQMQTKG MQYGDYGNNQ ASSTATPLSS
     ASDDEEEQEE DEEAGVDSSS TTSSASPLPN SYDALEGGSY PDMHSSSASS PVPDHALEPS
     PTLAQALSAA PTPPAAQPAK VAKPFGYGYP ALQPAYQNAA PPPMPAAHPS GPAYTGYPQH
     YPGVNQLSSG LGGLSLQSSP QPESLRPVNL TQEKNILPPT PIWAPVPNLS AELSKLNCSP
     DSFRCTLTSI PQTQALLNKA KLPLGLLLHP FRDLTQLPVI TSNTIVRCRS CRTYINPFVS
     FIDQRRWKCN LCYRVNDVPE EFLYNPLTRS YGEPHKRPEV QNSTVEFIAS SDYMLRPPQP
     AVYLFVLDVS HNAVEAGYLT VLCQSLLENL DKLPGDSRTR IGFMTFDSTI HFYNLQEGLS
     QPQMLIVSDI DDVFLPTPDS LLVNLYESKE LIKDLLNALP SMFINTRETH SALGPALQAA
     FKLMSPTGGR VSVFQTQLPS LGAGLLQSRE DPNQRSSTKV VHHLGPATDF YKKLALDCSG
     QQTAVDLFLL SSQYSDLASL ACMSKYSAGC IFYYPSFHST HNPSQAEKLQ KDLKRYLTRK
     IGFEAVMRIR CTKGLSMHTF HGNFFVRSTD LLSLANINPD AGFAVQLSIE ESLTDTALVC
     FQTALLYTSS KGERRIRVHT LCLPVVSSLA DVYAGVDVQA AVCLLANMAV DRSVSSSLSD
     ARDALVNAVV DPLSAYSSAV ASVPRSTLTA PSSLKLLPLY VLALLKQKAF RTGTSTRLDD
     RVYAMCQMKS QPLVHLMKMI HPNLYRIDRL TDEGAIHVND RVVPQPPLQK LSAEKLTREG
     AFLMDCGSVF YIWVGKGCDS NFIENVLGYP DFASIPQKMT HLPELDTLPS ERTRSFVTWL
     RDSRPLSPVL HLVKDESPAK TDFFQHLLED RTEAALSYYE FLIHIQQQVC K
//
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.
CC   -----------------------------------------------------------------------
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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   Q8BFW6_MOUSE            Unreviewed;       529 AA.
AC   Q8BFW6;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   SubName: Full=Ectonucleoside triphosphate diphosphohydrolase 3;
DE   SubName: Full=Nucleoside triphosphate diphosphohydrolase-3;
DE            EC=3.6.1.5;
GN   Name=Entpd3; ORFNames=mCG_22707;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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, and Oviduct;
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, and Oviduct;
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, and Oviduct;
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, and Oviduct;
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, and Oviduct;
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, and Oviduct;
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, and Oviduct;
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   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.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Crawford P.A., Kirley T.L.;
RT   "Sequencing of mouse brain NTPDase3.";
RL   Submitted (AUG-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).
RN   [13]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CD-1; TISSUE=Spleen;
RX   PubMed=15130768; DOI=10.1016/j.bcp.2004.02.012;
RA   Lavoie E.G., Kukulski F., Levesque S.A., Lecka J., Sevigny J.;
RT   "Cloning and characterization of mouse nucleoside triphosphate
RT   diphosphohydrolase-3.";
RL   Biochem. Pharmacol. 67:1917-1926(2004).
RN   [14]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CD-1; TISSUE=Spleen;
RA   Kukulski F., Levesque S.A., Lavoie E.G., Lecka J., Bigonnesse F.,
RA   Knowles A.F., Robson S.C., Kirley T.L., Sevigny J.;
RT   "Comparative hydrolysis of P2 receptor agonists by NTPDases 1, 2, 3
RT   and 8.";
RL   Purinergic Signal 1:193-204(2005).
RN   [15]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CD-1; TISSUE=Spleen;
RX   PubMed=17727821; DOI=10.1016/j.bcp.2007.07.033;
RA   Munkonda M.N., Kauffenstein G., Kukulski F., Levesque S.A.,
RA   Legendre C., Pelletier J., Lavoie E.G., Lecka J., Sevigny J.;
RT   "Inhibition of human and mouse plasma membrane bound NTPDases by P2
RT   receptor antagonists.";
RL   Biochem. Pharmacol. 74:1524-1534(2007).
RN   [16]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Oviduct;
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 GDA1/CD39 NTPase family.
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DR   EMBL; BC079871; AAH79871.1; -; mRNA.
DR   EMBL; AY376710; AAQ86585.1; -; mRNA.
DR   EMBL; AY714060; AAU13839.1; -; mRNA.
DR   EMBL; AK046218; BAC32641.1; -; mRNA.
DR   EMBL; AK087561; BAC39928.1; -; mRNA.
DR   EMBL; CH466587; EDL09171.1; -; Genomic_DNA.
DR   IPI; IPI00221493; -.
DR   RefSeq; NP_848791.2; NM_178676.4.
DR   UniGene; Mm.76648; -.
DR   ProteinModelPortal; Q8BFW6; -.
DR   SMR; Q8BFW6; 53-479.
DR   STRING; Q8BFW6; -.
DR   PRIDE; Q8BFW6; -.
DR   Ensembl; ENSMUST00000047687; ENSMUSP00000036830; ENSMUSG00000041608.
DR   GeneID; 215446; -.
DR   KEGG; mmu:215446; -.
DR   UCSC; uc009scq.1; mouse.
DR   CTD; 215446; -.
DR   MGI; MGI:1321386; Entpd3.
DR   HOGENOM; HBG402995; -.
DR   HOVERGEN; HBG018982; -.
DR   InParanoid; Q8BFW6; -.
DR   PhylomeDB; Q8BFW6; -.
DR   BRENDA; 3.6.1.5; 244.
DR   NextBio; 374730; -.
DR   ArrayExpress; Q8BFW6; -.
DR   Bgee; Q8BFW6; -.
DR   Genevestigator; Q8BFW6; -.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0017110; F:nucleoside-diphosphatase activity; IDA:MGI.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IDA:MGI.
DR   GO; GO:0009134; P:nucleoside diphosphate catabolic process; IDA:MGI.
DR   GO; GO:0009143; P:nucleoside triphosphate catabolic process; IDA:MGI.
DR   InterPro; IPR000407; GDA1_CD39_NTPase.
DR   PANTHER; PTHR11782; GDA1_CD39_NTPase; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
DR   PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase.
SQ   SEQUENCE   529 AA;  58984 MW;  E34F5EF187484F2C CRC64;
     MFTVMTRQPC EQAGFRALSR TPAIVTLVVL LVSIVVLVTL TLIQIRHPQV LPPGLKYGVV
     LDAGSSRTTV YVYQWPAEKE NNTGVVSQTF RCSVKGSGIS SYENNPQDAP KAFEDCILKV
     KEQVPEHLHG STRIYLGATA GMRLLRLQNE TAAREVLESI QSYFKSQPFD FRGAQIISGQ
     EEGVYGWITA NYIMGNFLEK NLWHMWVHPH GVDTTGALDL GGASTQISFV AGEKMEPNAS
     DTVQVSLYGY TYTLYTHSFQ CYGQNEAEKK FLAMLLQSPS TEANISNPCY PQGYSTAFTL
     GHVFGSLCTE KQRPESYNSS KSVTFMGTGD PRLCREKVAS VFDFNACQEQ DACSFDGIYQ
     PKVQGPFVAF AGFYYTASAL NLSGSFSLTS FNDSSWDFCR HTWSELPALL SRFDETYARS
     YCFSAHYIYH LLVNGYKFTE ETWPQIRFEK EVGNSSIAWS LGYMLSLTNQ IPAGSPLIHL
     PIQPPVFMGV LAFFTAIALL CLAFLLYLCS SFRTKERSEN AFDQAVDSD
//
ID   LPP_MOUSE               Reviewed;         613 AA.
AC   Q8BFW7; Q5U407; Q8BHI1; Q8BKI0; Q8BKN2; Q8BLF4; Q8BLG3; Q8C101;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Lipoma-preferred partner homolog;
GN   Name=Lpp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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/6J, and NOD;
RC   TISSUE=Aorta, Embryo, Eye, Head, Ovary, Spinal ganglion, Testis,
RC   Thymus, 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=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   [3]
RP   NEOPLASTIC TRANSFORMATION.
RX   PubMed=9696033; DOI=10.1038/sj.onc.1201952;
RA   Fedele M., Berlingieri M.T., Scala S., Chiariotti L., Viglietto G.,
RA   Rippel V., Bullerdiek J., Santoro M., Fusco A.;
RT   "Truncated and chimeric HMGI-C genes induce neoplastic transformation
RT   of NIH3T3 murine fibroblasts.";
RL   Oncogene 17:413-418(1998).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-302, 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-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 play a structural role at sites of cell adhesion in
CC       maintaining cell shape and motility. In addition to these
CC       structural functions, it may also be implicated in signaling
CC       events and activation of gene transcription. May be involved in
CC       signal transduction from cell adhesion sites to the nucleus
CC       allowing successful integration of signals arising from soluble
CC       factors and cell-cell adhesion sites. Also suggested to serve as a
CC       scaffold protein upon which distinct protein complexes are
CC       assembled in the cytoplasm and in the nucleus (By similarity).
CC   -!- SUBUNIT: Interacts with VASP, with PDZ domains of SCRIB and with
CC       ACTN1/alpha-actinin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity). Cell junction (By similarity). Note=Found in the
CC       nucleus, in the cytoplasm and at cell adhesion sites (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q8BFW7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BFW7-2; Sequence=VSP_016353, VSP_016354;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8BFW7-3; Sequence=VSP_016351, VSP_016353, VSP_016354;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q8BFW7-4; Sequence=VSP_016350, VSP_016352;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q8BFW7-5; Sequence=VSP_016355, VSP_016356;
CC         Note=No experimental confirmation available;
CC   -!- MISCELLANEOUS: Fusion protein carrying the DNA-binding domains of
CC       HMGA2/HMGIC and the LIM domain of LPP causes malignant
CC       transformation of NIH3T3 cells.
CC   -!- SIMILARITY: Belongs to the zyxin/ajuba family.
CC   -!- SIMILARITY: Contains 3 LIM zinc-binding domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK029335; BAC26401.1; -; mRNA.
DR   EMBL; AK029567; BAC26516.1; -; mRNA.
DR   EMBL; AK040643; BAC30654.1; -; mRNA.
DR   EMBL; AK045288; BAC32298.1; -; mRNA.
DR   EMBL; AK045341; BAC32316.1; -; mRNA.
DR   EMBL; AK051345; BAC34608.1; -; mRNA.
DR   EMBL; AK051937; BAC34815.1; -; mRNA.
DR   EMBL; AK054550; BAC35821.1; -; mRNA.
DR   EMBL; AK076989; BAC36552.1; -; mRNA.
DR   EMBL; AK169780; BAE41362.1; -; mRNA.
DR   EMBL; BC085321; AAH85321.1; -; mRNA.
DR   IPI; IPI00221494; -.
DR   IPI; IPI00656172; -.
DR   IPI; IPI00656185; -.
DR   IPI; IPI00656290; -.
DR   IPI; IPI00656313; -.
DR   RefSeq; NP_001139424.1; NM_001145952.1.
DR   RefSeq; NP_001139426.1; NM_001145954.1.
DR   RefSeq; NP_848780.3; NM_178665.5.
DR   UniGene; Mm.209385; -.
DR   UniGene; Mm.450045; -.
DR   ProteinModelPortal; Q8BFW7; -.
DR   SMR; Q8BFW7; 415-605.
DR   MINT; MINT-4111189; -.
DR   PhosphoSite; Q8BFW7; -.
DR   PRIDE; Q8BFW7; -.
DR   Ensembl; ENSMUST00000038053; ENSMUSP00000036304; ENSMUSG00000033306.
DR   Ensembl; ENSMUST00000115314; ENSMUSP00000110969; ENSMUSG00000033306.
DR   GeneID; 210126; -.
DR   KEGG; mmu:210126; -.
DR   UCSC; uc007yub.1; mouse.
DR   UCSC; uc007yuc.1; mouse.
DR   UCSC; uc007yud.1; mouse.
DR   UCSC; uc007yue.1; mouse.
DR   UCSC; uc007yuh.1; mouse.
DR   CTD; 210126; -.
DR   MGI; MGI:2441849; Lpp.
DR   eggNOG; roNOG08309; -.
DR   GeneTree; ENSGT00600000084017; -.
DR   HOVERGEN; HBG093602; -.
DR   InParanoid; Q8BFW7; -.
DR   OMA; DYAYIPP; -.
DR   OrthoDB; EOG4XKV6J; -.
DR   PhylomeDB; Q8BFW7; -.
DR   NextBio; 372874; -.
DR   ArrayExpress; Q8BFW7; -.
DR   Bgee; Q8BFW7; -.
DR   Genevestigator; Q8BFW7; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   Activator; Alternative splicing; Cell adhesion; Cell junction;
KW   Cytoplasm; LIM domain; Metal-binding; Nucleus; Phosphoprotein; Repeat;
KW   Zinc.
FT   CHAIN         1    613       Lipoma-preferred partner homolog.
FT                                /FTId=PRO_0000075833.
FT   DOMAIN      415    474       LIM zinc-binding 1.
FT   DOMAIN      475    535       LIM zinc-binding 2.
FT   DOMAIN      536    604       LIM zinc-binding 3.
FT   COMPBIAS     41    390       Pro-rich.
FT   MOD_RES     117    117       Phosphoserine (By similarity).
FT   MOD_RES     127    127       Phosphoserine (By similarity).
FT   MOD_RES     245    245       Phosphotyrosine.
FT   MOD_RES     298    298       Phosphotyrosine (By similarity).
FT   MOD_RES     301    301       Phosphotyrosine (By similarity).
FT   MOD_RES     302    302       Phosphotyrosine.
FT   MOD_RES     318    318       Phosphotyrosine (By similarity).
FT   MOD_RES     398    398       Phosphothreonine (By similarity).
FT   VAR_SEQ       1    125       Missing (in isoform 4).
FT                                /FTId=VSP_016350.
FT   VAR_SEQ     102    102       Missing (in isoform 3).
FT                                /FTId=VSP_016351.
FT   VAR_SEQ     126    144       TSILADLECSSPYKPRPPQ -> MELLGKVGACLKRSTGTL
FT                                K (in isoform 4).
FT                                /FTId=VSP_016352.
FT   VAR_SEQ     145    152       GSASSIAS -> VGTSHSAA (in isoform 2 and
FT                                isoform 3).
FT                                /FTId=VSP_016353.
FT   VAR_SEQ     153    613       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_016354.
FT   VAR_SEQ     373    378       GGYPGP -> VRNLLT (in isoform 5).
FT                                /FTId=VSP_016355.
FT   VAR_SEQ     379    613       Missing (in isoform 5).
FT                                /FTId=VSP_016356.
FT   CONFLICT     29     29       F -> V (in Ref. 1; BAC32298).
FT   CONFLICT     81     81       I -> T (in Ref. 1; BAC34815).
FT   CONFLICT     83     83       P -> S (in Ref. 2; AAH85321).
FT   CONFLICT    133    133       E -> D (in Ref. 1; BAC26401).
FT   CONFLICT    395    395       E -> A (in Ref. 1; BAC34608).
FT   CONFLICT    567    567       C -> R (in Ref. 2; AAH85321).
SQ   SEQUENCE   613 AA;  65891 MW;  E34BE2EF2A3B7126 CRC64;
     MSHPSWLPPK STGEPLGHVP ARMETTHSFG NPSISVSTQQ PPKKYAPVVA PKPKYNPYKQ
     PGGEGDLLPP PPPPLEDPGT IPPGPGHFPP PPPLDEGAFK VQQGNPGGKT LEERRSSLDA
     EIDSLTSILA DLECSSPYKP RPPQGSASSI ASPPVSTPVT GHKRMVIPQQ PPLTATKKSA
     TKPQPAPQAA PIPVTPIGTL KPQPQPVPAS YTTASTSSRP TFNVQVKSAQ PSPHYMAGPS
     SGQIYGPGPR GYNNQPVPVS GQCPPPPTCV GTDYAYIPPS GHPPESGYGY TSNQGRYYEP
     YYAAGPSYGG RSEGDTAYGQ QVQPNTWKRE AAYAPPASGN QNHPGMYPVS GPKKTYITDP
     VSAPCAPPLQ PKGGYPGPMG PPSIPPSFRP EDELEHLTKK MLYDMENPPA DDYFGRCARC
     GENVVGEGTG CTAMDQVFHV DCFTCIVCDV KLRGQPFYAV EKKAYCEPCY INTLEQCSVC
     SKPIMERILR ATGKAYHPHC FTCVMCHRSL DGIPFTVDAC GLIHCIEDFH KKFAPRCSVC
     KEPIMPAPGQ EETVRIVALD RDFHVHCYRC EDCGGLLSEG DNQGCYPLDG HILCKTCNSA
     RIRVLTAKAS TDL
//
ID   P4HTM_MOUSE             Reviewed;         503 AA.
AC   Q8BG58; Q8CAF1; Q9D499;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Transmembrane prolyl 4-hydroxylase;
DE            Short=P4H-TM;
DE            EC=1.14.11.-;
DE   AltName: Full=Hypoxia-inducible factor prolyl hydroxylase 4;
DE            Short=HIF-PH4;
DE            Short=HIF-prolyl hydroxylase 4;
DE            Short=HPH-4;
GN   Name=P4htm; Synonyms=Ph4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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 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: Catalyzes the post-translational formation of 4-
CC       hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins.
CC       Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a
CC       cellular oxygen sensor and, under normoxic conditions, may target
CC       HIF through the hydroxylation for proteasomal degradation via the
CC       von Hippel-Lindau ubiquitination complex (By similarity).
CC   -!- CATALYTIC ACTIVITY: An HIF alpha chain L-proline + 2-oxoglutarate
CC       + O(2) = An HIF alpha chain trans-4-hydroxy-L-proline + succinate
CC       + CO(2).
CC   -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity).
CC   -!- COFACTOR: Ascorbate (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       type II membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BG58-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BG58-2; Sequence=VSP_007575, VSP_007576;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Glycosylated (By similarity).
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
CC   -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB30379.2; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part;
CC       Sequence=BAC30172.1; Type=Frameshift; Positions=9;
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DR   EMBL; AK046783; BAC32866.1; -; mRNA.
DR   EMBL; AK047714; BAC33135.1; -; mRNA.
DR   EMBL; AK016685; BAB30379.2; ALT_SEQ; mRNA.
DR   EMBL; AK038927; BAC30172.1; ALT_SEQ; mRNA.
DR   IPI; IPI00221483; -.
DR   IPI; IPI00620061; -.
DR   RefSeq; NP_083220.3; NM_028944.3.
DR   UniGene; Mm.226534; -.
DR   ProteinModelPortal; Q8BG58; -.
DR   SMR; Q8BG58; 134-465.
DR   STRING; Q8BG58; -.
DR   PRIDE; Q8BG58; -.
DR   Ensembl; ENSMUST00000006853; ENSMUSP00000006853; ENSMUSG00000006675.
DR   GeneID; 74443; -.
DR   KEGG; mmu:74443; -.
DR   UCSC; uc009rqk.1; mouse.
DR   UCSC; uc009rqm.1; mouse.
DR   CTD; 74443; -.
DR   MGI; MGI:1921693; P4htm.
DR   GeneTree; ENSGT00390000014570; -.
DR   HOGENOM; HBG445603; -.
DR   InParanoid; Q8BG58; -.
DR   OMA; QQGTAVF; -.
DR   OrthoDB; EOG4K3KW8; -.
DR   NextBio; 340775; -.
DR   ArrayExpress; Q8BG58; -.
DR   Bgee; Q8BG58; -.
DR   CleanEx; MM_4933406E20RIK; -.
DR   Genevestigator; Q8BG58; -.
DR   GermOnline; ENSMUSG00000006675; 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:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; 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:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR005123; Oxoglutarate/Fe-dep_oxygenase.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; FALSE_NEG.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Calcium; Dioxygenase; Endoplasmic reticulum;
KW   Glycoprotein; Iron; Membrane; Metal-binding; Oxidoreductase; Repeat;
KW   Signal-anchor; Transmembrane; Transmembrane helix; Vitamin C; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    503       Transmembrane prolyl 4-hydroxylase.
FT                                /FTId=PRO_0000206669.
FT   TOPO_DOM      1     61       Cytoplasmic (Potential).
FT   TRANSMEM     62     82       Helical; Signal-anchor for type II
FT                                membrane protein; (Potential).
FT   TOPO_DOM     83    503       Lumenal (Potential).
FT   DOMAIN      186    221       EF-hand 1.
FT   DOMAIN      225    260       EF-hand 2.
FT   DOMAIN      310    461       Fe2OG dioxygenase.
FT   CA_BIND     199    211       1 (Potential).
FT   CA_BIND     238    250       2 (Potential).
FT   METAL       329    329       Iron (By similarity).
FT   METAL       331    331       Iron (By similarity).
FT   METAL       375    375       Iron (By similarity).
FT   BINDING     452    452       2-oxoglutarate (Potential).
FT   CARBOHYD    349    349       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    369    369       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    383    383       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     212    225       LAQTRLGNGRWMTP -> RTPPAMWVGTGEN (in
FT                                isoform 2).
FT                                /FTId=VSP_007575.
FT   VAR_SEQ     226    503       Missing (in isoform 2).
FT                                /FTId=VSP_007576.
SQ   SEQUENCE   503 AA;  57049 MW;  C220CA0840F1BAFF CRC64;
     MAAAVATVQR PEAETVEEAS NLQWPLPPEH RPSGAATRPG DSEDAPVRPL CKPRGICSRA
     YFLVLMVFVH LYLGNVLALL LFVHYSNGDE STDPGPQRRE QSPQPVPTLG PLTRLEGIKV
     GYERKVQVVA GRDHFIRTLS LKPLLFEIPG FLSDEECRLI IHLAQMKGLQ RSQILPTEEY
     EEAMSAMQVS QLDLFQLLDQ NHDGRLQLRE VLAQTRLGNG RWMTPENIQE MYSAIKADPD
     GDGVLSLQEF SNMDLRDFHK YMRSHKAESN ELVRNSHHTW LHQGEGAHHV MRAIRQRVLR
     LTRLSPEIVE FSEPLQVVRY GEGGHYHAHV DSGPVYPETI CSHTKLVANE SVPFETSCRY
     MTVLFYLNNV TGGGETVFPV ADNRTYDEMS LIQDDVDLRD TRRHCDKGNL RVKPQQGTAV
     FWYNYLPDGQ GWVGEVDDYS LHGGCLVTRG TKWIANNWIN VDPSRARQAL FQQEMARLAR
     EGGMDSQPEW ALDRAYSDAR VEL
//
ID   FBX46_MOUSE             Reviewed;         603 AA.
AC   Q8BG80;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=F-box only protein 46;
DE   AltName: Full=F-box only protein 34-like;
GN   Name=Fbxo46; Synonyms=Fbx46, Fbxo34l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; 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=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: Substrate-recognition component of the SCF (SKP1-CUL1-F-
CC       box protein)-type E3 ubiquitin ligase complex (By similarity).
CC   -!- SUBUNIT: Interacts with SKP1A and CUL1 (By similarity).
CC   -!- SIMILARITY: Contains 1 F-box domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK030147; BAC26809.1; -; mRNA.
DR   EMBL; AK030220; BAC26851.1; -; mRNA.
DR   EMBL; BC049813; AAH49813.1; -; mRNA.
DR   IPI; IPI00221511; -.
DR   RefSeq; NP_780739.1; NM_175530.3.
DR   UniGene; Mm.230830; -.
DR   ProteinModelPortal; Q8BG80; -.
DR   PhosphoSite; Q8BG80; -.
DR   PRIDE; Q8BG80; -.
DR   Ensembl; ENSMUST00000053109; ENSMUSP00000055692; ENSMUSG00000050428.
DR   GeneID; 243867; -.
DR   KEGG; mmu:243867; -.
DR   UCSC; uc009fkt.1; mouse.
DR   CTD; 243867; -.
DR   MGI; MGI:2444918; Fbxo46.
DR   eggNOG; maNOG18542; -.
DR   GeneTree; ENSGT00530000064222; -.
DR   HOGENOM; HBG506013; -.
DR   HOVERGEN; HBG051583; -.
DR   InParanoid; Q8BG80; -.
DR   OMA; LWCPRPF; -.
DR   OrthoDB; EOG461440; -.
DR   PhylomeDB; Q8BG80; -.
DR   NextBio; 385980; -.
DR   ArrayExpress; Q8BG80; -.
DR   Bgee; Q8BG80; -.
DR   CleanEx; MM_FBXO46; -.
DR   Genevestigator; Q8BG80; -.
DR   GermOnline; ENSMUSG00000050428; Mus musculus.
DR   InterPro; IPR001810; F-box_dom_cyclin-like.
DR   InterPro; IPR022364; F-box_dom_Skp2-like.
DR   SMART; SM00256; FBOX; 1.
DR   SUPFAM; SSF81383; F-box_dom_Skp2-like; 1.
DR   PROSITE; PS50181; FBOX; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Ubl conjugation pathway.
FT   CHAIN         1    603       F-box only protein 46.
FT                                /FTId=PRO_0000119951.
FT   DOMAIN      470    522       F-box.
FT   MOD_RES     225    225       Phosphoserine (By similarity).
FT   MOD_RES     347    347       Phosphothreonine (By similarity).
SQ   SEQUENCE   603 AA;  65294 MW;  B8B6AF154D1BAD5E CRC64;
     MDRGSLLPFQ LWCPRPFSKY SQNQPRPPST ALKPPVCPDT SSGTEPDHRP AHLESTPPAV
     AAEAPTSQPA PLLSTAASGD EGRVLLDTWY VIKPGNTKEK VAFFVAHQCG GSSRASSMKV
     KGHWGSDSSK AKRRRRCLEP TKAPPDQGGR EGTPATEVTP TSSGDDVDLV SVAEMVALVE
     QRAALALQSY PRPSTPAPVV FVSADQGGPA KGLGSERRSG GGDCSRVAEA VAHFEAQRDS
     PPTKGLRKEE RPGPGPGEVR IAFRISNVRE PHSPDGNLPN GGGGRPGCAY PGSPGPGTRA
     KDKITCDLYQ LISPSRDALP SNVEFLLARA DEASEGETPA PTRPEDTPPA PPPPPARDCG
     ASGFHVDVVV TGVVDACIFF GKDGTKNVKE ETVCLTVSPE EPPPPGQLFF LQSRGPEGPP
     EPPPADIPST VPGPDDSEGT TDTSLCRLYR HVSHDFLEIR FKIQRLLEPR QYMLLLPEHV
     LVKIFSFLPT RALAALKCTC HHFKGIIEAF GVRATDSRWS RDPLYRDDPC KQCRKRYEKG
     DVSLCRWHPK PYHHDLPYGR SYWMCCRRAD RETPGCRLGL HDNNWVLPCN GVGGGRAGRE
     EGR
//
ID   TET3_MOUSE              Reviewed;        1668 AA.
AC   Q8BG87; Q4VAD3; Q8C8N8; Q8CI60;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 3.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Methylcytosine dioxygenase TET3;
DE            EC=1.14.11.n2;
GN   Name=Tet3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; 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=Adipose tissue, 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 757-1553 (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, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP   HIS-950 AND ASP-952.
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: Catalyzes the conversion of methylcytosine (5mC) to 5-
CC       hydroxymethylcytosine (hmC).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BG87-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BG87-2; Sequence=VSP_034193, VSP_034194;
CC   -!- TISSUE SPECIFICITY: Not expressed in embryonic stem cells (ES
CC       cells).
CC   -!- SIMILARITY: Belongs to the TET family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH96437.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=AAH96437.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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DR   EMBL; AK044758; BAC32068.1; -; mRNA.
DR   EMBL; AK046543; BAC32779.1; -; mRNA.
DR   EMBL; AK046552; BAC32784.1; -; mRNA.
DR   EMBL; AK046553; BAC32785.1; -; mRNA.
DR   EMBL; AC090648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC159713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC096437; AAH96437.1; ALT_SEQ; mRNA.
DR   IPI; IPI00457624; -.
DR   IPI; IPI00881991; -.
DR   RefSeq; NP_898961.2; NM_183138.2.
DR   UniGene; Mm.211030; -.
DR   UniGene; Mm.480457; -.
DR   Ensembl; ENSMUST00000056191; ENSMUSP00000049948; ENSMUSG00000072977.
DR   GeneID; 194388; -.
DR   KEGG; mmu:194388; -.
DR   UCSC; uc009cnl.1; mouse.
DR   CTD; 194388; -.
DR   MGI; MGI:2444739; B430006D22Rik.
DR   eggNOG; maNOG22176; -.
DR   GeneTree; ENSGT00510000046514; -.
DR   HOVERGEN; HBG079550; -.
DR   InParanoid; Q8BG87; -.
DR   OMA; PPDKPPK; -.
DR   OrthoDB; EOG46Q6RP; -.
DR   ArrayExpress; Q8BG87; -.
DR   Bgee; Q8BG87; -.
DR   Genevestigator; Q8BG87; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Alternative splicing; Dioxygenase; Iron; Metal-binding;
KW   Oxidoreductase.
FT   CHAIN         1   1668       Methylcytosine dioxygenase TET3.
FT                                /FTId=PRO_0000340228.
FT   METAL       950    950       Iron; catalytic (Probable).
FT   METAL       952    952       Iron; catalytic (Probable).
FT   METAL      1546   1546       Iron; catalytic (By similarity).
FT   BINDING    1561   1561       2-oxoglutarate (By similarity).
FT   VAR_SEQ     705    719       EQIVEKDEGPYYTHL -> GRWEWSRAFFLSVEH (in
FT                                isoform 2).
FT                                /FTId=VSP_034193.
FT   VAR_SEQ     720   1668       Missing (in isoform 2).
FT                                /FTId=VSP_034194.
FT   MUTAGEN     950    950       H->Y: Loss of enzyme activity; when
FT                                associated with A-952.
FT   MUTAGEN     952    952       D->A: Loss of enzyme activity; when
FT                                associated with Y-950.
FT   CONFLICT    962    962       V -> A (in Ref. 3; AAH96437).
SQ   SEQUENCE   1668 AA;  180378 MW;  73DD97090F917199 CRC64;
     MDSGPVYHGD SRQLSTSGAP VNGAREPAGP GLLGAAGPWR VDQKPDWEAA SGPTHAARLE
     DAHDLVAFSA VAEAVSSYGA LSTRLYETFN REMSREAGSN GRGPRPESCS EGSEDLDTLQ
     TALALARHGM KPPNCTCDGP ECPDFLEWLE GKIKSMAMEG GQGRPRLPGA LPPSEAGLPA
     PSTRPPLLSS EVPQVPPLEG LPLSQSALSI AKEKNISLQT AIAIEALTQL SSALPQPSHS
     TSQASCPLPE ALSPSAPFRS PQSYLRAPSW PVVPPEEHPS FAPDSPAFPP ATPRPEFSEA
     WGTDTPPATP RNSWPVPRPS PDPMAELEQL LGSASDYIQS VFKRPEALPT KPKVKVEAPS
     SSPAPVPSPI SQREAPLLSS EPDTHQKAQT ALQQHLHHKR NLFLEQAQDA SFPTSTEPQA
     PGWWAPPGSP APRPPDKPPK EKKKKPPTPA GGPVGAEKTT PGIKTSVRKP IQIKKSRSRD
     MQPLFLPVRQ IVLEGLKPQA SEGQAPLPAQ LSVPPPASQG AASQSCATPL TPEPSLALFA
     PSPSGDSLLP PTQEMRSPSP MVALQSGSTG GPLPPADDKL EELIRQFEAE FGDSFGLPGP
     PSVPIQEPEN QSTCLPAPES PFATRSPKKI KIESSGAVTV LSTTCFHSEE GGQEATPTKA
     ENPLTPTLSG FLESPLKYLD TPTKSLLDTP AKKAQSEFPT CDCVEQIVEK DEGPYYTHLG
     SGPTVASIRE LMEDRYGEKG KAIRIEKVIY TGKEGKSSRG CPIAKWVIRR HTLEEKLLCL
     VRHRAGHHCQ NAVIVILILA WEGIPRSLGD TLYQELTDTL RKYGNPTSRR CGLNDDRTCA
     CQGKDPNTCG ASFSFGCSWS MYFNGCKYAR SKTPRKFRLT GDNPKEEEVL RNSFQDLATE
     VAPLYKRLAP QAYQNQVTNE DVAIDCRLGL KEGRPFSGVT ACMDFCAHAH KDQHNLYNGC
     TVVCTLTKED NRCVGQIPED EQLHVLPLYK MASTDEFGSE ENQNAKVSSG AIQVLTAFPR
     EVRRLPEPAK SCRQRQLEAR KAAAEKKKLQ KEKLSTPEKI KQEALELAGV TTDPGLSLKG
     GLSQQSLKPS LKVEPQNHFS SFKYSGNAVV ESYSVLGSCR PSDPYSMSSV YSYHSRYAQP
     GLASVNGFHS KYTLPSFGYY GFPSSNPVFP SQFLGPSAWG HGGSGGSFEK KPDLHALHNS
     LNPAYGGAEF AELPGQAVAT DNHHPIPHHQ QPAYPGPKEY LLPKVPQLHP ASRDPSPFAQ
     SSSCYNRSIK QEPIDPLTQA ESIPRDSAKM SRTPLPEASQ NGGPSHLWGQ YSGGPSMSPK
     RTNSVGGNWG VFPPGESPTI VPDKLNSFGA SCLTPSHFPE SQWGLFTGEG QQSAPHAGAR
     LRGKPWSPCK FGNGTSALTG PSLTEKPWGM GTGDFNPALK GGPGFQDKLW NPVKVEEGRI
     PTPGANPLDK AWQAFGMPLS SNEKLFGALK SEEKLWDPFS LEEGTAEEPP SKGVVKEEKS
     GPTVEEDEEE LWSDSEHNFL DENIGGVAVA PAHCSILIEC ARRELHATTP LKKPNRCHPT
     RISLVFYQHK NLNQPNHGLA LWEAKMKQLA ERARQRQEEA ARLGLGQQEA KLYGKKRKWG
     GAMVAEPQHK EKKGAIPTRQ ALAMPTDSAV TVSSYAYTKV TGPYSRWI
//
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.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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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   F168A_MOUSE             Reviewed;         244 AA.
AC   Q8BGZ2; Q3UVC2; Q80U50; Q8BGN7;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Protein FAM168A;
GN   Name=Fam168a; Synonyms=Kiaa0280;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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, Head, 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] (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 79-244.
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=Q8BGZ2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BGZ2-2; Sequence=VSP_010096;
CC   -!- SIMILARITY: Belongs to the FAM168 protein family.
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DR   EMBL; AK043083; BAC31453.1; -; mRNA.
DR   EMBL; AK047153; BAC32972.1; -; mRNA.
DR   EMBL; AK048559; BAC33374.1; -; mRNA.
DR   EMBL; AK051453; BAC34646.1; -; mRNA.
DR   EMBL; AK137424; BAE23348.1; -; mRNA.
DR   EMBL; BC076580; AAH76580.1; -; mRNA.
DR   EMBL; AK122235; BAC65517.1; -; mRNA.
DR   IPI; IPI00261542; -.
DR   IPI; IPI00283461; -.
DR   RefSeq; NP_848879.1; NM_178764.3.
DR   UniGene; Mm.260362; -.
DR   ProteinModelPortal; Q8BGZ2; -.
DR   PhosphoSite; Q8BGZ2; -.
DR   PRIDE; Q8BGZ2; -.
DR   Ensembl; ENSMUST00000049053; ENSMUSP00000038233; ENSMUSG00000029461.
DR   Ensembl; ENSMUST00000084914; ENSMUSP00000081977; ENSMUSG00000029461.
DR   Ensembl; ENSMUST00000107042; ENSMUSP00000102657; ENSMUSG00000029461.
DR   GeneID; 319604; -.
DR   KEGG; mmu:319604; -.
DR   UCSC; uc009inq.1; mouse.
DR   UCSC; uc009inr.1; mouse.
DR   CTD; 319604; -.
DR   MGI; MGI:2442372; Fam168a.
DR   GeneTree; ENSGT00390000005140; -.
DR   HOGENOM; HBG444825; -.
DR   HOVERGEN; HBG052179; -.
DR   InParanoid; Q8BGZ2; -.
DR   OMA; PATLLMK; -.
DR   OrthoDB; EOG43FGXW; -.
DR   PhylomeDB; Q8BGZ2; -.
DR   ArrayExpress; Q8BGZ2; -.
DR   Bgee; Q8BGZ2; -.
DR   Genevestigator; Q8BGZ2; -.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Phosphoprotein.
FT   CHAIN         1    244       Protein FAM168A.
FT                                /FTId=PRO_0000050743.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES       6      6       Phosphoserine (By similarity).
FT   VAR_SEQ      51     59       Missing (in isoform 2).
FT                                /FTId=VSP_010096.
FT   CONFLICT     79     83       GTFHL -> RHLPP (in Ref. 3; BAC65517).
SQ   SEQUENCE   244 AA;  26184 MW;  60E3E9621665D30C CRC64;
     MNPVYSPVQP GAPYGNPKNM AYTGYPTAYP AAAPAYNPSL YPTNSPSYAP EFQFLHSAYA
     TLLMKQAWPQ NSSSCGTEGT FHLPVDTGTE NRTYQASSAA FRYTAGTPYK VPPTQSNTAP
     PPYSPSPNPY QTAMYPIRSA YPQQNLYAQG AYYTQPVYAA QPHVIHHTTV VQPNSIPSAI
     YPAPVAAPRT NGVAMGMVAG TTMAMSAGTL LTTPQHTAIG AHPVSMPTYR AQGTPAYSYV
     PPHW
//
ID   KBTB3_MOUSE             Reviewed;         607 AA.
AC   Q8BHI4; Q8BNJ8;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Kelch repeat and BTB domain-containing protein 3;
DE   AltName: Full=BTB and kelch domain-containing protein 3;
GN   Name=Kbtbd3; Synonyms=Bklhd3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; 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 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   -!- SIMILARITY: Contains 1 BACK (BTB/Kelch associated) domain.
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC   -!- SIMILARITY: Contains 5 Kelch repeats.
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DR   EMBL; AK034334; BAC28678.1; -; mRNA.
DR   EMBL; AK078744; BAC37374.1; -; mRNA.
DR   EMBL; AK083497; BAC38935.1; -; mRNA.
DR   EMBL; BC027392; AAH27392.1; -; mRNA.
DR   IPI; IPI00308276; -.
DR   RefSeq; NP_001158046.1; NM_001164574.1.
DR   RefSeq; NP_081238.2; NM_026962.3.
DR   UniGene; Mm.25946; -.
DR   ProteinModelPortal; Q8BHI4; -.
DR   SMR; Q8BHI4; 22-278, 304-449.
DR   PRIDE; Q8BHI4; -.
DR   Ensembl; ENSMUST00000049648; ENSMUSP00000050183; ENSMUSG00000025893.
DR   GeneID; 69149; -.
DR   KEGG; mmu:69149; -.
DR   UCSC; uc009obj.1; mouse.
DR   CTD; 69149; -.
DR   MGI; MGI:1916399; Kbtbd3.
DR   HOGENOM; HBG444377; -.
DR   HOVERGEN; HBG052212; -.
DR   InParanoid; Q8BHI4; -.
DR   OMA; ESRQKHL; -.
DR   OrthoDB; EOG42BX83; -.
DR   PhylomeDB; Q8BHI4; -.
DR   NextBio; 457714; -.
DR   ArrayExpress; Q8BHI4; -.
DR   Bgee; Q8BHI4; -.
DR   CleanEx; MM_KBTBD3; -.
DR   Genevestigator; Q8BHI4; -.
DR   GermOnline; ENSMUSG00000025893; Mus musculus.
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; 2.
DR   PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR   SMART; SM00875; BACK; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00612; Kelch; 3.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   2: Evidence at transcript level;
KW   Kelch repeat; Repeat.
FT   CHAIN         1    607       Kelch repeat and BTB domain-containing
FT                                protein 3.
FT                                /FTId=PRO_0000119079.
FT   DOMAIN       48    115       BTB.
FT   DOMAIN      150    252       BACK.
FT   REPEAT      291    337       Kelch 1.
FT   REPEAT      339    390       Kelch 2.
FT   REPEAT      400    450       Kelch 3.
FT   REPEAT      452    502       Kelch 4.
FT   REPEAT      548    595       Kelch 5.
FT   CONFLICT    440    440       I -> M (in Ref. 1; BAC38935).
SQ   SEQUENCE   607 AA;  69551 MW;  1AE2DAE6875244CD CRC64;
     MDNSYNLNEQ SSWNGISSEK KKNYLASEDH GQKILSVLQS FREQNVFYDF KIIMKEEIIP
     CHRCVLAACS DFFRAMFEVN MKERDDGSVT ITNLSSKAVK AFLDYAYTGK TRITDDNVEM
     FFQLSSFLQV SFLSKACSDF LIKSISLVNC LHLLSLSDSY GSAQLFSHTL YFVQHHFHLL
     YKSSDFLEMN FGVLQKCLES DELNVPEEEM VLKAVLTWIK YNLESRQKHL PHLITKVRLH
     QLSEDTLQDY LLNEEYLLKS TNCFDIIVDA IKCVQGSSGL FPDARPSTTE KYIFIHKTEE
     NGENQYTFCY NIKTDSWKIL PQSHLIDLPG SSLSSYGEKI FLTGGCKGKC CRRIRLHIAQ
     SYHDATDQTW CYCPAKNEFF CVSAMKTPRT MHTSVMALNR LFVIGGKTRG SQDIKSLLDV
     ESYNPLSREW TSVSPLPRGI YYPEASACQN IIYVLGSEVE IADAFNPSLD CFFKYNATTD
     QWSELVAEFG QFFHATLIKA VPVNCTLYIC DLSTYKVYSF CPDTCVWKGE GSFECAGFNA
     GAIGIEDKIY ILGGDYAPDE ITDEVQVYHS SRSEWEEVSP MPRALTEFYC QVIQFNKYRD
     PWYSNHF
//
ID   GBRA5_MOUSE             Reviewed;         463 AA.
AC   Q8BHJ7;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit alpha-5;
DE   AltName: Full=GABA(A) receptor subunit alpha-5;
DE   Flags: Precursor;
GN   Name=Gabra5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; 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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(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 (By similarity).
CC   -!- SUBUNIT: Generally pentameric. There are five types of GABA(A)
CC       receptor chains: alpha, beta, gamma, delta, and rho (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein (By similarity). Cell
CC       membrane; Multi-pass membrane protein (By similarity).
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       GABRA5 sub-subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK038476; BAC30012.1; -; mRNA.
DR   EMBL; AK083185; BAC38799.1; -; mRNA.
DR   EMBL; BC062112; AAH62112.1; -; mRNA.
DR   IPI; IPI00221880; -.
DR   RefSeq; NP_795916.1; NM_176942.4.
DR   UniGene; Mm.273114; -.
DR   ProteinModelPortal; Q8BHJ7; -.
DR   SMR; Q8BHJ7; 286-346.
DR   MINT; MINT-1789015; -.
DR   STRING; Q8BHJ7; -.
DR   PhosphoSite; Q8BHJ7; -.
DR   PRIDE; Q8BHJ7; -.
DR   Ensembl; ENSMUST00000068456; ENSMUSP00000063276; ENSMUSG00000055078.
DR   GeneID; 110886; -.
DR   KEGG; mmu:110886; -.
DR   UCSC; uc009heb.1; mouse.
DR   CTD; 110886; -.
DR   MGI; MGI:95617; Gabra5.
DR   HOGENOM; HBG506497; -.
DR   HOVERGEN; HBG051707; -.
DR   InParanoid; Q8BHJ7; -.
DR   OMA; WTNGTTK; -.
DR   OrthoDB; EOG4X0MSC; -.
DR   PhylomeDB; Q8BHJ7; -.
DR   NextBio; 364867; -.
DR   ArrayExpress; Q8BHJ7; -.
DR   Bgee; Q8BHJ7; -.
DR   Genevestigator; Q8BHJ7; -.
DR   GermOnline; ENSMUSG00000055078; 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:0008306; P:associative learning; IMP:MGI.
DR   GO; GO:0001662; P:behavioral fear response; IMP: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; IPR005435; GABBAa5_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; PR01618; GABAARALPHA5.
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   Isopeptide bond; Ligand-gated ion channel; Membrane;
KW   Postsynaptic cell membrane; Receptor; Signal; Synapse; Transmembrane;
KW   Transmembrane helix; Transport; Ubl conjugation.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26    463       Gamma-aminobutyric acid receptor subunit
FT                                alpha-5.
FT                                /FTId=PRO_0000000445.
FT   TOPO_DOM     26    259       Extracellular (Potential).
FT   TRANSMEM    260    281       Helical; (Potential).
FT   TRANSMEM    286    307       Helical; (Potential).
FT   TRANSMEM    319    341       Helical; (Potential).
FT   TOPO_DOM    342    428       Cytoplasmic (Potential).
FT   TRANSMEM    429    450       Helical; (Potential).
FT   CARBOHYD     45     45       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    145    145       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    207    207       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    236    236       N-linked (GlcNAc...) (Potential).
FT   DISULFID    173    187       By similarity.
FT   CROSSLNK    355    355       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
SQ   SEQUENCE   463 AA;  52274 MW;  12C677403D326378 CRC64;
     MDNGMLSRFI MTQTLLVFCI SMTLSSHFGF SQMPTSSVQD ETNDNITIFT RILDGLLDGY
     DNRLRPGLGE RITQVRTDIY VTSFGPVSDT EMEYTIDVFF RQSWKDERLR FKGPMQRLPL
     NNLLASKIWT PDTFFHNGKK SIAHNMTTPN KLLRLEDDGT LLYTMRLTIS AECPMQLEDF
     PMDAHACPLK FGSYAYPNSE VVYVWTNGST KSVVVAEDGS RLNQYHLMGQ TVGTENISTS
     TGEYTIMTAH FHLKRKIGYF VIQTYLPCIM TVILSQVSFW LNRESVPART VFGVTTVLTM
     TTLSISARNS LPKVAYATAM DWFIAVCYAF VFSALIEFAT VNYFTKRGWA WDGKKALEAA
     KIKKKERELI LNKSTNAFTT GKLTHPPNIP KEQPPAGTAN APTVSIKASE EKTAESKKTY
     NSISKIDKMS RIVFPILFGT FNLVYWATYL NREPVIKGAT SPK
//
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   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;
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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   SP130_MOUSE             Reviewed;        1057 AA.
AC   Q8BIH0; Q6NZP5; Q6P553; Q8BID9; Q9CSU1;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Histone deacetylase complex subunit SAP130;
DE   AltName: Full=130 kDa Sin3-associated polypeptide;
DE   AltName: Full=Sin3-associated polypeptide p130;
GN   Name=Sap130;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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=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   [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-683, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., 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 transcriptional repressor. 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: Component of a mSin3A corepressor complex that contains
CC       SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BIH0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BIH0-2; Sequence=VSP_024357;
CC       Name=3;
CC         IsoId=Q8BIH0-3; Sequence=VSP_024358, VSP_024359;
CC   -!- DOMAIN: The N-terminus may interact with a transcriptional
CC       coactivator (By similarity).
CC   -!- DOMAIN: The C-terminus may interact with HDAC-dependent and HDAC-
CC       independent corepressors (By similarity).
CC   -!- PTM: Acetylated (By similarity).
CC   -!- SIMILARITY: Belongs to the SAP130 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH66030.1; Type=Erroneous initiation;
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DR   EMBL; AK011978; BAB27953.1; -; mRNA.
DR   EMBL; AK053675; BAC35469.1; -; mRNA.
DR   EMBL; AK084078; BAC39113.1; -; mRNA.
DR   EMBL; BC063075; AAH63075.1; -; mRNA.
DR   EMBL; BC066030; AAH66030.1; ALT_INIT; mRNA.
DR   IPI; IPI00454138; -.
DR   IPI; IPI00844747; -.
DR   IPI; IPI00844759; -.
DR   RefSeq; NP_766553.1; NM_172965.2.
DR   UniGene; Mm.194538; -.
DR   PhosphoSite; Q8BIH0; -.
DR   PRIDE; Q8BIH0; -.
DR   Ensembl; ENSMUST00000025109; ENSMUSP00000025109; ENSMUSG00000024260.
DR   GeneID; 269003; -.
DR   KEGG; mmu:269003; -.
DR   UCSC; uc008eic.1; mouse.
DR   CTD; 269003; -.
DR   MGI; MGI:1919782; Sap130.
DR   eggNOG; roNOG14142; -.
DR   GeneTree; ENSGT00440000037733; -.
DR   HOGENOM; HBG445901; -.
DR   HOVERGEN; HBG106600; -.
DR   InParanoid; Q8BIH0; -.
DR   OMA; MTVPSHS; -.
DR   OrthoDB; EOG49W2GD; -.
DR   NextBio; 392636; -.
DR   ArrayExpress; Q8BIH0; -.
DR   Bgee; Q8BIH0; -.
DR   CleanEx; MM_SAP130; -.
DR   Genevestigator; Q8BIH0; -.
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.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Nucleus; Phosphoprotein; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN         1   1057       Histone deacetylase complex subunit
FT                                SAP130.
FT                                /FTId=PRO_0000283737.
FT   REGION      845   1057       Interactions with SIN3A and HDAC1 (By
FT                                similarity).
FT   COMPBIAS     56    143       Pro-rich.
FT   COMPBIAS    208    212       Poly-Ala.
FT   COMPBIAS    718    845       Pro-rich.
FT   MOD_RES     329    329       Phosphothreonine (By similarity).
FT   MOD_RES     416    416       Phosphoserine (By similarity).
FT   MOD_RES     428    428       Phosphoserine (By similarity).
FT   MOD_RES     429    429       Phosphoserine (By similarity).
FT   MOD_RES     683    683       Phosphoserine.
FT   MOD_RES     884    884       Phosphoserine (By similarity).
FT   VAR_SEQ       1    178       Missing (in isoform 2).
FT                                /FTId=VSP_024357.
FT   VAR_SEQ     340    348       KTIFSTGTP -> VRTVTPPEG (in isoform 3).
FT                                /FTId=VSP_024358.
FT   VAR_SEQ     349   1057       Missing (in isoform 3).
FT                                /FTId=VSP_024359.
FT   CONFLICT    594    594       Missing (in Ref. 1; BAC35469).
SQ   SEQUENCE   1057 AA;  111228 MW;  9D963F4CD53B971A CRC64;
     MSSQQFPRLG TPSPGLSQPP SQIASSGSAG LINQVATVND EAGRDADVGT REHVGPSSSL
     PPREEKQEPV VVRPYPQVQM LPAHHAVASA TPVAVTAPPA HLTPAVPLSF SEGLMKPPPK
     PTMPSRPIAP APPSTMSLPP KVPGQVTVTM ESSIPQASAI PVATISGQQG HPSNLHHIMT
     TNVQMSIIRS NAPGPPLHIG ASHLPRGAAA AAVMSSSKVT TVLRPTSQLP NAATAQPAVQ
     HLIHQPIQSR PPVTTSSTIP PAVVATVSAT RAQSPVITTT AAHAADSTLS RPTLSIQHPP
     SAAISIQRPA QSRDVTTRIT LPSHPALGTP KQQLHTMAQK TIFSTGTPVA AATVAPILAT
     NTLPSTTTAG SVSHTQAPTS TIVTMTMPSH SSHATAVTTS NIPVAKVVPQ QITHTSPRIQ
     PDYPPERSSL IPISGHRASP NPVAMETRND NRPSVPVQFQ YFLPTYPPSA YPLAAHTYTP
     ITSSVSTIRQ YPVSAQAPNS TITAQTGVGV ASTVHLNPMQ LMTVDASHAR HIQGIQPAPI
     STQGIQPAPI GTSGIQPAPI GTPGIHSAAP INTQGLQPAA MANQQPQPEG KTSAVVLADG
     ATIVANPISN PFSAAPAATT VVQTHSQSAS TNTPAQGSSP RPSILRKKPA TDGMAVRKTL
     LPPQPPDVAT PRVESSMRSA SGSPRPAGAK PKSEVHVSIA TPVTVSLETI SNQNAEQPTV
     AVPPTAQQPP PTIPSMIAAA SPPSQPAIAL STIPGAVPVT PPITTIAATP TLSAPVGGTP
     STVLGPPVPE IKVKEEAEPV DITRPVSTVP PLATNTVSPS LALLASNLSM PPSDLPPGAS
     PRKKPRKQQH VISTEEGDMM ETNSTDDEKS AAKSLLVKAE KRKSPPKEYI DEEGVRYVPV
     RPRPPITLLR HYRNPWKAAY HHFQRYSDVR VKEEKKAMLQ EIANQKGVSC RAQGWKVHLC
     AAQLLQLTNL EHDVYERLTN LQEGIIPKKK AATDDDLHRI NELIQGNMQR CKLVMDQISE
     ARDSMLKVLD HKDRVLKLLN KNGTVKKVSK LKRKEKV
//
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   -----------------------------------------------------------------------
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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   ZNT6_MOUSE              Reviewed;         460 AA.
AC   Q8BJM5; Q3UB35; Q6NVE0; Q8K4H6; Q8R4Z2; Q99JQ3;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Zinc transporter 6;
DE            Short=ZnT-6;
DE   AltName: Full=Solute carrier family 30 member 6;
GN   Name=Slc30a6; Synonyms=Znt6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=C57BL/6J;
RX   MEDLINE=22113027; PubMed=11997387; DOI=10.1074/jbc.M200462200;
RA   Huang L., Kirschke C.P., Gitschier J.;
RT   "Functional characterization of a novel mammalian zinc transporter,
RT   ZnT6.";
RL   J. Biol. Chem. 277:26389-26395(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RA   Zhu W., Mager S.;
RT   "Cloning of new mammalian zinc transporter-like genes.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
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].
RC   STRAIN=C57BL/6, C57BL/6J, and FVB/N;
RC   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: Zinc-efflux transporter which allocates the cytoplasmic
CC       zinc to the trans-Golgi network (TGN) as well as the vesicular
CC       compartment.
CC   -!- SUBUNIT: Heterooligomer. Interacts with ZNT5 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC       membrane; Multi-pass membrane protein. Note=Found in vesicules.
CC   -!- TISSUE SPECIFICITY: Expressed in brain and liver, and to a lower
CC       extent also in lung. Highly expressed in brain (at protein level).
CC   -!- MISCELLANEOUS: Seems to have lost most of the histidine residues
CC       in the loop between the fourth and fifth transmembrane regions and
CC       appears to exert transport function by forming complexes with
CC       ZNT5.
CC   -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC       transporter (TC 2.A.4) family. SLC30A subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH05753.1; Type=Erroneous initiation;
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DR   EMBL; AF395840; AAM27917.1; -; mRNA.
DR   EMBL; AF233346; AAL83717.1; -; mRNA.
DR   EMBL; AK082907; BAC38680.1; -; mRNA.
DR   EMBL; AK150342; BAE29482.1; -; mRNA.
DR   EMBL; AK151120; BAE30129.1; -; mRNA.
DR   EMBL; BC005753; AAH05753.1; ALT_INIT; mRNA.
DR   EMBL; BC066162; AAH66162.1; -; mRNA.
DR   EMBL; BC068169; AAH68169.1; -; mRNA.
DR   IPI; IPI00469280; -.
DR   RefSeq; NP_659047.2; NM_144798.5.
DR   UniGene; Mm.243943; -.
DR   ProteinModelPortal; Q8BJM5; -.
DR   STRING; Q8BJM5; -.
DR   PhosphoSite; Q8BJM5; -.
DR   PRIDE; Q8BJM5; -.
DR   Ensembl; ENSMUST00000024870; ENSMUSP00000024870; ENSMUSG00000024069.
DR   GeneID; 210148; -.
DR   KEGG; mmu:210148; -.
DR   UCSC; uc008dob.1; mouse.
DR   CTD; 210148; -.
DR   MGI; MGI:2386741; Slc30a6.
DR   eggNOG; roNOG12933; -.
DR   GeneTree; ENSGT00510000046571; -.
DR   HOGENOM; HBG443978; -.
DR   HOVERGEN; HBG106400; -.
DR   InParanoid; Q8BJM5; -.
DR   OMA; GKNVNPV; -.
DR   OrthoDB; EOG4FXR7B; -.
DR   PhylomeDB; Q8BJM5; -.
DR   NextBio; 372890; -.
DR   ArrayExpress; Q8BJM5; -.
DR   Bgee; Q8BJM5; -.
DR   Genevestigator; Q8BJM5; -.
DR   GO; GO:0005794; C:Golgi apparatus; 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:0005385; F:zinc ion transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0006895; P:Golgi to endosome transport; IDA:MGI.
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   Golgi apparatus; Ion transport; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix; Transport; Zinc; Zinc transport.
FT   CHAIN         1    460       Zinc transporter 6.
FT                                /FTId=PRO_0000312574.
FT   TOPO_DOM      1     33       Cytoplasmic (Potential).
FT   TRANSMEM     34     54       Helical; (Potential).
FT   TOPO_DOM     55     64       Extracellular (Potential).
FT   TRANSMEM     65     85       Helical; (Potential).
FT   TOPO_DOM     86     98       Cytoplasmic (Potential).
FT   TRANSMEM     99    119       Helical; (Potential).
FT   TOPO_DOM    120    134       Extracellular (Potential).
FT   TRANSMEM    135    155       Helical; (Potential).
FT   TOPO_DOM    156    200       Cytoplasmic (Potential).
FT   TRANSMEM    201    221       Helical; (Potential).
FT   TOPO_DOM    222    223       Extracellular (Potential).
FT   TRANSMEM    224    244       Helical; (Potential).
FT   TOPO_DOM    245    460       Cytoplasmic (Potential).
FT   MOD_RES     382    382       Phosphoserine (By similarity).
FT   CONFLICT     80     80       S -> R (in Ref. 3; BAE29482 and 4;
FT                                AAH68169).
FT   CONFLICT     81     81       Y -> H (in Ref. 1; AAM27917).
FT   CONFLICT    128    128       E -> G (in Ref. 1; AAM27917).
FT   CONFLICT    161    168       AYVSEAAS -> GRVGGRVG (in Ref. 4;
FT                                AAH05753).
FT   CONFLICT    225    225       F -> C (in Ref. 4; AAH68169).
FT   CONFLICT    292    292       F -> L (in Ref. 1; AAM27917).
FT   CONFLICT    308    308       N -> S (in Ref. 3; BAE29482 and 4;
FT                                AAH68169).
FT   CONFLICT    314    314       A -> T (in Ref. 2; AAL83717).
FT   CONFLICT    324    326       VST -> ASS (in Ref. 2; AAL83717).
FT   CONFLICT    331    331       I -> N (in Ref. 2; AAL83717).
SQ   SEQUENCE   460 AA;  51027 MW;  A3E910CE96D16015 CRC64;
     MGTIHLFRKP QRSFFGKLLQ EFRLVAADRR SWKILLFGAI NVLCTGFLLM WCSSTNSIAL
     TAYTYLTIFD LFSLITCLIS YWVMMRKPSP VYSFGFERLE VLAVFASTVL AQLGALFILK
     ESAERFLEQP EIHTGRLLVG TFVALSFNLF TMLSIRNKPF AYVSEAASTS WLQEHVADLS
     RSLCGLIPGL SSIFLPRMNP FVLIDLAGAF ALCITYMLIE INNYFAVDTA SAIAIALMTF
     GTMYPMSVYS GKVLLQTTPP HVIGQLDKLI REVSTLDGVL EVRNEHFWTL GFGSLAGSVH
     VRIRRDANEQ MVLAHVSNRL CTLVSTLTVQ IFKDDWIRPA LSSGPVAPNV LNFSDHHVIP
     MPLLKNVDER TPVTSTPAKP SSPPPEFSFN TPGKNVSPVI LLNTQTRPYS LGLNRGHTPY
     SSVFSQGLAF PGVGAGQGLR PTFPHIPSRY GINRMGQPRP
//
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;
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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   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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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   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   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;
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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   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   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   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   CLAP2_MOUSE             Reviewed;        1286 AA.
AC   Q8BRT1; Q8CHE3; Q99JI3; Q9DB80;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 77.
DE   RecName: Full=CLIP-associating protein 2;
DE   AltName: Full=Cytoplasmic linker-associated protein 2;
GN   Name=Clasp2; Synonyms=Kiaa0627;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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   ALTERNATIVE SPLICING, TISSUE SPECIFICITY, INTERACTION WITH CLIP2 AND
RP   RSN, AND MUTAGENESIS OF CYS-6 AND CYS-10.
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex, 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 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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-1286 (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   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-581, 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   SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=16123238; DOI=10.1530/rep.1.00651;
RA   Moore C.A., Zernicka-Goetz M.;
RT   "PAR-1 and the microtubule-associated proteins CLASP2 and dynactin-p50
RT   have specific localisation on mouse meiotic and first mitotic
RT   spindles.";
RL   Reproduction 130:311-320(2005).
RN   [8]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16914514; DOI=10.1091/mbc.E06-07-0579;
RA   Pereira A.L., Pereira A.J., Maia A.R.R., Drabek K., Sayas C.L.,
RA   Hergert P.J., Lince-Faria M., Matos I., Duque C., Stepanova T.,
RA   Rieder C.L., Earnshaw W.C., Galjart N., Maiato H.;
RT   "Mammalian CLASP1 and CLASP2 cooperate to ensure mitotic fidelity by
RT   regulating spindle and kinetochore function.";
RL   Mol. Biol. Cell 17:4526-4542(2006).
RN   [9]
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241 (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   [11]
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: 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.
CC   -!- SUBUNIT: Interacts with ERC1, MAPRE3, microtubules and PHLDB2. The
CC       interaction with ERC1 may be mediated by PHLDB2. Interacts with
CC       MAPRE1; probably required for targeting to the growing microtubule
CC       plus ends. Interacts with GCC2; recruits CLASP2 to the Golgi
CC       membranes (By similarity). Interacts with CLIP2 and RSN.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
CC       cytoskeleton, centrosome. Chromosome, centromere, kinetochore.
CC       Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle
CC       pole. Golgi apparatus. Golgi apparatus, trans-Golgi network (By
CC       similarity). Note=Localizes to microtubule plus ends. Localizes to
CC       centrosomes, kinetochores and the mitotic spindle from
CC       prometaphase. Subsequently localizes to the spindle midzone from
CC       anaphase and to the midbody from telophase. In migrating cells
CC       localizes to the plus ends of microtubules within the cell body
CC       and to the entire microtubule lattice within the lamella.
CC       Localizes to the cell cortex and this requires ERC1 and PHLDB2 (By
CC       similarity). Also localizes to meiotic spindle poles.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BRT1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BRT1-5; Sequence=VSP_015808, VSP_015811;
CC         Note=Phosphorylated on Ser-241;
CC       Name=3;
CC         IsoId=Q8BRT1-6; Sequence=VSP_015809, VSP_015810, VSP_015812;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and at low levels in
CC       heart, kidney and lung.
CC   -!- DEVELOPMENTAL STAGE: Expressed in oocytes and early 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   -!- PTM: Phosphorylated by GSK3B. Phosphorylation by GSK3B may
CC       negatively regulate binding to microtubule lattices in lamella.
CC       Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity). Isoform 2 is phosphorylated on Ser-241.
CC   -!- SIMILARITY: Belongs to the CLASP family.
CC   -!- SIMILARITY: Contains 5 HEAT repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC41436.2; Type=Frameshift; Positions=737;
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DR   EMBL; AJ276961; CAC35161.1; -; mRNA.
DR   EMBL; AK043551; BAC31579.1; -; mRNA.
DR   EMBL; AK005146; BAB23842.1; -; mRNA.
DR   EMBL; BC030468; AAH30468.1; -; mRNA.
DR   EMBL; AB093252; BAC41436.2; ALT_FRAME; Transcribed_RNA.
DR   IPI; IPI00407863; -.
DR   IPI; IPI00654284; -.
DR   IPI; IPI00875254; -.
DR   UniGene; Mm.222272; -.
DR   ProteinModelPortal; Q8BRT1; -.
DR   SMR; Q8BRT1; 1054-1270.
DR   STRING; Q8BRT1; -.
DR   PhosphoSite; Q8BRT1; -.
DR   PRIDE; Q8BRT1; -.
DR   Ensembl; ENSMUST00000035089; ENSMUSP00000035089; ENSMUSG00000033392.
DR   Ensembl; ENSMUST00000111848; ENSMUSP00000107479; ENSMUSG00000033392.
DR   Ensembl; ENSMUST00000111849; ENSMUSP00000107480; ENSMUSG00000033392.
DR   UCSC; uc009rwt.1; mouse.
DR   UCSC; uc009rwv.1; mouse.
DR   MGI; MGI:1923749; Clasp2.
DR   GeneTree; ENSGT00390000001762; -.
DR   HOVERGEN; HBG079692; -.
DR   ArrayExpress; Q8BRT1; -.
DR   Bgee; Q8BRT1; -.
DR   CleanEx; MM_CLASP2; -.
DR   Genevestigator; Q8BRT1; -.
DR   GermOnline; ENSMUSG00000033392; Mus musculus.
DR   GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IDA:MGI.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR   GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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:0007126; P:meiosis; 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   Gene3D; G3DSA:1.25.10.10; ARM-like; 3.
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; Cell division; Centromere;
KW   Chromosome; Coiled coil; Cytoplasm; Cytoskeleton; Golgi apparatus;
KW   Kinetochore; Meiosis; Microtubule; Mitosis; Phosphoprotein; Repeat.
FT   CHAIN         1   1286       CLIP-associating protein 2.
FT                                /FTId=PRO_0000089850.
FT   REPEAT      179    214       HEAT 1.
FT   REPEAT      215    251       HEAT 2.
FT   REPEAT      764    801       HEAT 3.
FT   REPEAT     1090   1127       HEAT 4.
FT   REPEAT     1208   1245       HEAT 5.
FT   REGION        1     40       Golgi localization.
FT   REGION      450    565       Interaction with microtubules, MAPRE1 and
FT                                MAPRE3 (By similarity).
FT   REGION      864   1286       Interaction with RSN and localization to
FT                                the Golgi and kinetochores (By
FT                                similarity).
FT   REGION     1009   1286       Required for cortical localization (By
FT                                similarity).
FT   COILED     1047   1076       Potential.
FT   MOTIF       500    503       Microtubule tip localization signal.
FT   MOTIF       523    526       Microtubule tip localization signal.
FT   COMPBIAS    459    572       Ser-rich.
FT   MOD_RES      14     14       Phosphoserine.
FT   MOD_RES     332    332       Phosphoserine (By similarity).
FT   MOD_RES     333    333       Phosphoserine (By similarity).
FT   MOD_RES     336    336       Phosphoserine (By similarity).
FT   MOD_RES     374    374       Phosphoserine (By similarity).
FT   MOD_RES     376    376       Phosphoserine (By similarity).
FT   MOD_RES     513    513       Phosphoserine.
FT   MOD_RES     529    529       Phosphoserine (By similarity).
FT   MOD_RES     531    531       Phosphoserine (By similarity).
FT   MOD_RES     535    535       Phosphoserine (By similarity).
FT   MOD_RES     568    568       Phosphoserine (By similarity).
FT   MOD_RES     581    581       Phosphoserine.
FT   MOD_RES     986    986       Phosphoserine (By similarity).
FT   MOD_RES    1021   1021       Phosphoserine (By similarity).
FT   MOD_RES    1045   1045       Phosphoserine (By similarity).
FT   MOD_RES    1049   1049       Phosphoserine (By similarity).
FT   VAR_SEQ       1     12       MRRLICKRICDY -> MEPRGAEYFCAQVLQKDVSGRLQAG
FT                                EELLLCLGTPGAIPDLEDDPSRLAKTVDALTRWVGSSNYRV
FT                                SLLGLEILSAFVDRLSTRFKSYVTMVTTALIDRMGDVKDKV
FT                                REEAQNLTLKLMDEVAPPMYIWEQLASGFKHKNFRSREGVC
FT                                LCLIETLNIFGTQPLVISKLVPHLCVLFGDSNSQVRNAALS
FT                                AVVEIYRHVGEKLRIDLCKRDIPPARLEMVLAKFDEVQNSG
FT                                GMILSVCKD (in isoform 2).
FT                                /FTId=VSP_015808.
FT   VAR_SEQ       1     12       MRRLICKRICDY -> MAMGDD (in isoform 3).
FT                                /FTId=VSP_015809.
FT   VAR_SEQ     119    173       LKKIRSLLVAGAAQYDCFFQHLRLLDGALKLSAKDLRSQVV
FT                                REACITVAHLSTVL -> CMSCSLVASEVERALAWPLWSHL
FT                                ATYQHHCHCTLSHEDLPEKRLTSPVSSAFVQH (in
FT                                isoform 3).
FT                                /FTId=VSP_015810.
FT   VAR_SEQ     142   1054       Missing (in isoform 2).
FT                                /FTId=VSP_015811.
FT   VAR_SEQ     174   1286       Missing (in isoform 3).
FT                                /FTId=VSP_015812.
FT   MUTAGEN       6      6       C->S: Impairs Golgi localization; when
FT                                associated with S-10.
FT   MUTAGEN      10     10       C->S: Impairs Golgi localization; when
FT                                associated with S-6.
FT   CONFLICT    657    657       S -> T (in Ref. 4; BAC41436).
FT   CONFLICT    683    683       I -> V (in Ref. 4; BAC41436).
FT   CONFLICT    699    699       P -> L (in Ref. 4; BAC41436).
FT   CONFLICT    702    702       K -> KR (in Ref. 4; BAC41436).
SQ   SEQUENCE   1286 AA;  140739 MW;  5B208D8F4E90CB93 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 SQPGSRSGSP GRVLTTTALS
     TVSSGAQRVL VNSASAQKRS KIPRSQGCSR EASPSRLSVA RSSRIPRPSV SQGCSREASR
     ESSRDTSPVR SFQPLGPGYG ISQSSRLSSS VSAMRVLNTG SDVEEAVADA LLLGDIRTKK
     KPARRRYESY GMHSDDDANS DASSACSERS YSSRNGSIPT YMRQTEDVAE VLNRCASSNW
     SERKEGLLGL QNLLKNQRTL SRIELKRLCE IFTRMFADPH GKVFSMFLET LVDFIQVHKD
     DLQDWLFVLL TQLLKKMGAD LLGSVQAKVQ KALDITRESF PNDLQFNILM RFTVDQTQTP
     SLKVKVAILK YIETLAKQMD PRDFTNSSET RLAVSRVITW TTEPKSSDVR KAAQSVLISL
     FELNTPEFTM LLGALPKTFQ DGATKLLHNH LRNTGNGTQS SMGSPLTRPT PRSPANWSSP
     LTSPTNTSQN TLSPSAFDYD TENMNSEDIY SSLRGVTEAI QNFSFRSQED MSEPVRRDPK
     KEDGDTICSG PGMSDPRAGG DAADGSQPAL DNKASLLHSM PLHSSPRSRD YNPYNYSDSI
     SPFNKSALKE AMFDDDADQF PDDLSLDHSD LVAELLKELS NHNERIEERK IALYELMKLT
     QEESFSVWDE HFKTILLLLL ETLGDKEPTI RALALKVLKE ILRHQPARFK NYAELTVMKT
     LEAHKDPHKE VVRSAEEAAS VLATSISPEQ CIKVLCPIIQ TADYPINLAA IKMQTKVIER
     VSKETLNMLL PEIMPGLIQG YDNSESSVRK ACVFCLVAVH AVIGDELKPH LSQLTGSKMK
     LLNLYIKRAQ TGSAGADPTA DVSGQS
//
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   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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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   TOX4_MOUSE              Reviewed;         619 AA.
AC   Q8BU11; Q80UI2; Q99PN9; Q9CS16;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2003, sequence version 2.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=TOX high mobility group box family member 4;
DE   AltName: Full=Epidermal Langerhans cell protein LCP1;
GN   Name=Tox4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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   Luy M.A., Reske K.;
RT   "Cloning of a novel gene expressed differentially in maturing
RT   epidermal Langerhans cells.";
RL   Submitted (JAN-2000) 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].
RC   TISSUE=Trophoblast;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and 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-182, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.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 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   -!- SUBUNIT: Component of the PTW/PP1 phosphatase complex, composed of
CC       PPP1R10/PNUTS, TOX4, WDR82 and PPP1CA or PPP1CB or PPP1CC.
CC       Interacts with PPP1R10/PNUTS (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Note=Associated
CC       with chromatin.
CC   -!- SIMILARITY: Contains 1 HMG box DNA-binding domain.
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DR   EMBL; AF228408; AAK00713.1; -; mRNA.
DR   EMBL; AK019980; BAB31949.1; -; mRNA.
DR   EMBL; AK088144; BAC40170.1; -; mRNA.
DR   EMBL; BC050091; AAH50091.1; -; mRNA.
DR   IPI; IPI00121251; -.
DR   UniGene; Mm.246237; -.
DR   ProteinModelPortal; Q8BU11; -.
DR   SMR; Q8BU11; 219-291.
DR   IntAct; Q8BU11; 4.
DR   PhosphoSite; Q8BU11; -.
DR   PRIDE; Q8BU11; -.
DR   Ensembl; ENSMUST00000022766; ENSMUSP00000022766; ENSMUSG00000016831.
DR   Ensembl; ENSMUST00000071842; ENSMUSP00000071742; ENSMUSG00000016831.
DR   MGI; MGI:1915389; Tox4.
DR   GeneTree; ENSGT00560000076898; -.
DR   HOVERGEN; HBG051013; -.
DR   InParanoid; Q8BU11; -.
DR   OrthoDB; EOG4JT05P; -.
DR   PhylomeDB; Q8BU11; -.
DR   ArrayExpress; Q8BU11; -.
DR   Bgee; Q8BU11; -.
DR   CleanEx; MM_TOX4; -.
DR   Genevestigator; Q8BU11; -.
DR   GermOnline; ENSMUSG00000016831; Mus musculus.
DR   GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
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   1: Evidence at protein level;
KW   DNA-binding; Nucleus; Phosphoprotein.
FT   CHAIN         1    619       TOX high mobility group box family member
FT                                4.
FT                                /FTId=PRO_0000048569.
FT   DNA_BIND    223    291       HMG box.
FT   MOTIF       213    218       Nuclear localization signal (Potential).
FT   COMPBIAS    401    522       Gln/Pro-rich.
FT   COMPBIAS    426    432       Poly-Ala.
FT   MOD_RES     176    176       Phosphothreonine (By similarity).
FT   MOD_RES     178    178       Phosphoserine (By similarity).
FT   MOD_RES     180    180       Phosphothreonine (By similarity).
FT   MOD_RES     182    182       Phosphoserine.
FT   CONFLICT      3      3       F -> S (in Ref. 1; AAK00713).
FT   CONFLICT    243    243       G -> R (in Ref. 2; BAC40170).
FT   CONFLICT    321    321       T -> A (in Ref. 2; BAB31949).
FT   CONFLICT    365    365       I -> T (in Ref. 3; AAH50091).
FT   CONFLICT    425    425       Q -> R (in Ref. 3; AAH50091).
FT   CONFLICT    446    446       L -> S (in Ref. 1; AAK00713).
FT   CONFLICT    453    453       P -> T (in Ref. 2; BAB31949).
SQ   SEQUENCE   619 AA;  65991 MW;  23250E4471041322 CRC64;
     MEFPGGNDNY LTITGPSHPF LSGAETFHTP SLGDEEFEIP PISLDSDPSL AVSDVVGHFD
     DLADPSSSQD GSFSAQYGVQ TLDMPVGMTH GLMEQGGGLL SGGLTMDLDH SIGTQYSANP
     PVTIDVPMTD MTSGLMGHSQ LTTIDQSELS SQLGLSLGGG TILPPAQSPE DRLSTTPSPT
     NSLHEDGVDD FRRQLPAQKT VVVETGKKQK APKKRKKKDP NEPQKPVSAY ALFFRDTQAA
     IKGQNPNATF GEVSKIVASM WDSLGEEQKQ VYKRKTEAAK KEYLKALAAY KDNQECQATV
     ETVELDPVPQ SQTPSPPPVT TADPASPAPA STESPALPPC IIVNSTLSSY VANQASSGPG
     GQPNITKLII TKQMLPSSIT MSQGGMVTVI PATVVTSRGL QVGQTSTATI QPSQQAQIVT
     RSVLQAAAAA AASMQLPPPR LQPPPLQQMP QPPTQQQVTI LQQPPPLQAM QQPPPQKVRI
     NLQQQPPPLQ SKIVPPPTLK IQTTVVPPTV ESSPEQPMNS SPEAHTVEAT SPETICEMIA
     DVVPEVESPS QMDVELVSGS PVALSPQPRC VRSGCENPPV VSKDWDNEYC SNECVVKHCR
     DVFLAWVASR NPNSVVFVK
//
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.
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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   CREST_MOUSE             Reviewed;         402 AA.
AC   Q8BW22; Q6A014; Q7TQF3; Q8BYQ7;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Calcium-responsive transactivator;
DE   AltName: Full=SS18-like protein 1;
GN   Name=Ss18l1; Synonyms=Crest, Kiaa0693;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; 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=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 GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting 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, AND DISRUPTION PHENOTYPE.
RX   PubMed=14716005; DOI=10.1126/science.1089845;
RA   Aizawa H., Hu S.-C., Bobb K., Balakrishnan K., Ince G., Gurevich I.,
RA   Cowan M., Ghosh A.;
RT   "Dendrite development regulated by CREST, a calcium-regulated
RT   transcriptional activator.";
RL   Science 303:197-202(2004).
RN   [6]
RP   INTERACTION WITH THE NBAF COMPLEX.
RX   PubMed=17920018; DOI=10.1016/j.neuron.2007.08.021;
RA   Wu J.I., Lessard J., Olave I.A., Qiu Z., Ghosh A., Graef I.A.,
RA   Crabtree G.R.;
RT   "Regulation of dendritic development by neuron-specific chromatin
RT   remodeling complexes.";
RL   Neuron 56:94-108(2007).
RN   [7]
RP   FUNCTION.
RX   PubMed=19081374; DOI=10.1016/j.neuron.2008.09.040;
RA   Qiu Z., Ghosh A.;
RT   "A calcium-dependent switch in a CREST-BRG1 complex regulates
RT   activity-dependent gene expression.";
RL   Neuron 60:775-787(2008).
CC   -!- FUNCTION: Transcriptional activator which is required for calcium-
CC       dependent dendritic growth and branching in cortical neurons.
CC       Recruits CREB-binding protein (CREBBP) to nuclear bodies.
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-HDAC1
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   -!- SUBUNIT: Homodimer. Dimerization may be necessary for its function
CC       in neuronal dendritic development. Interacts (via C-terminus) with
CC       CREBBP (via N-terminus), EP300 and SMARCA4/BRG1. Interacts with
CC       the nBAF complex. Association with CREBBP facilitates
CC       transcription while the association with SMARCA4/BRG1 suppresses
CC       CREST-mediated transcription in resting neurons (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Chromosome,
CC       centromere, kinetochore (By similarity). Note=Localizes to nuclear
CC       bodies. Co-localizes with SGOL1 at kinetochore (By similarity).
CC   -!- DOMAIN: The MFD (multi-functional domain) domain is involved in
CC       transcription transactivation, nuclear body targeting and
CC       dimerization (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice are smaller than littermates and show
CC       coordination defects. There is increased mortality in beginning at
CC       about P14, and about 80% die by P28. Less than 20% survive to
CC       adulthood, and they are infertile.
CC   -!- SIMILARITY: Belongs to the SS18 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK173004; BAD32282.1; -; mRNA.
DR   EMBL; AK038669; BAC30089.1; -; mRNA.
DR   EMBL; AK054560; BAC35824.1; -; mRNA.
DR   EMBL; AK133944; BAE21942.1; -; mRNA.
DR   EMBL; AL663067; CAM18353.1; -; Genomic_DNA.
DR   EMBL; BC053087; AAH53087.1; -; mRNA.
DR   EMBL; BC054730; AAH54730.1; -; mRNA.
DR   IPI; IPI00387517; -.
DR   RefSeq; NP_848865.4; NM_178750.5.
DR   UniGene; Mm.481027; -.
DR   STRING; Q8BW22; -.
DR   Ensembl; ENSMUST00000041126; ENSMUSP00000041288; ENSMUSG00000039086.
DR   GeneID; 269397; -.
DR   KEGG; mmu:269397; -.
DR   UCSC; uc008oic.1; mouse.
DR   CTD; 269397; -.
DR   MGI; MGI:2444061; Ss18l1.
DR   GeneTree; ENSGT00500000044808; -.
DR   HOVERGEN; HBG003892; -.
DR   InParanoid; Q8BW22; -.
DR   OMA; KTAECTQ; -.
DR   OrthoDB; EOG4F4SBW; -.
DR   PhylomeDB; Q8BW22; -.
DR   ArrayExpress; Q8BW22; -.
DR   Bgee; Q8BW22; -.
DR   Genevestigator; Q8BW22; -.
DR   GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
DR   GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; IDA:MGI.
DR   GO; GO:0016563; F:transcription activator activity; ISS:UniProtKB.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0016358; P:dendrite development; IMP:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007726; SSXT.
DR   PANTHER; PTHR23107; SSXT; 1.
DR   Pfam; PF05030; SSXT; 1.
PE   1: Evidence at protein level;
KW   Activator; Calcium; Centromere; Chromatin regulator; Chromosome;
KW   Kinetochore; Nucleus; Repeat; Transcription; Transcription regulation.
FT   CHAIN         1    402       Calcium-responsive transactivator.
FT                                /FTId=PRO_0000391346.
FT   REGION        1    148       N-terminal auto-inhibitory domain;
FT                                necessary for interaction with
FT                                SMARCA4/BRG1 (By similarity).
FT   REGION      149    238       Methionine-rich intra-molecular domain
FT                                (By similarity).
FT   REGION      252    323       MFD domain (By similarity).
FT   REGION      340    402       Necessary for nuclear localization (By
FT                                similarity).
FT   REGION      393    402       Necessary for interaction with CREBBP and
FT                                for the recruitment of CREBBP to the
FT                                nuclear bodies (By similarity).
FT   MOTIF        50     53       SH2-binding (Potential).
FT   MOTIF       359    362       SH2-binding (Potential).
FT   MOTIF       377    385       SH3-binding (Potential).
FT   MOTIF       397    400       SH2-binding (Potential).
FT   COMPBIAS    197    402       Gln-rich.
FT   CONFLICT    130    130       V -> L (in Ref. 2; BAC30089).
FT   CONFLICT    159    159       S -> I (in Ref. 4; AAH54730).
SQ   SEQUENCE   402 AA;  43729 MW;  9C309B9E7446CCAA CRC64;
     MSVAFASARP RGKGEVTQQT IQKMLDENHH LIQCILDYQS KGKTAECTQY QQILHRNLVY
     LATIADSNQN MQSLLPAPPT QNMNLGPGAL SQSGSSQGLH PQGSLSDTVS TGLPPASLMQ
     GQIGNGPNHV SMQQTAQSTL PTTSMSLSGS GHGTGPGYSH SGPTSQSVPM QGQGAISNYV
     SRTNINMQSN PVSMMHQQAA TSHYNSAQGG SQHYQGQAPI AMMGQGGQGG SMMGQRPMAP
     YRPSQQGSSQ QYLGQEEYYS EQYSHSQGSA EPMSQQYYPD GHGDYAYQQS SYTEQSYDRS
     FEDPTQHYYE GGNSQYSQQQ AGYQQGTAQQ QTYSQQQYPN QQSYPGQQQG YGPAQGAPSQ
     YSSYQQGQGQ QYGSYRTSQT GPSAQQQRPY GYEQGQYGNY QQ
//
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   IFFO1_MOUSE             Reviewed;         562 AA.
AC   Q8BXL9; Q3TQI1; Q6PFE6; Q8BXS3; Q8C1D6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Intermediate filament family orphan 1;
GN   Name=Iffo1; Synonyms=Iffo;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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 6).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, 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 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).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q8BXL9-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q8BXL9-2; Sequence=VSP_030786;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8BXL9-3; Sequence=VSP_030785, VSP_030787;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q8BXL9-4; Sequence=VSP_030785, VSP_030788;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q8BXL9-5; Sequence=VSP_030787;
CC         Note=No experimental confirmation available;
CC       Name=6;
CC         IsoId=Q8BXL9-6; Sequence=VSP_030788;
CC         Note=No experimental confirmation available;
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; AK028273; BAC25852.1; -; mRNA.
DR   EMBL; AK044382; BAC31894.1; -; mRNA.
DR   EMBL; AK044728; BAC32053.1; -; mRNA.
DR   EMBL; AK163571; BAE37401.1; -; mRNA.
DR   EMBL; BC057601; AAH57601.2; -; mRNA.
DR   IPI; IPI00226745; -.
DR   IPI; IPI00742423; -.
DR   IPI; IPI00885688; -.
DR   IPI; IPI00885752; -.
DR   IPI; IPI00885836; -.
DR   IPI; IPI00885898; -.
DR   RefSeq; NP_001034758.1; NM_001039669.2.
DR   RefSeq; NP_848902.4; NM_178787.5.
DR   UniGene; Mm.129415; -.
DR   ProteinModelPortal; Q8BXL9; -.
DR   SMR; Q8BXL9; 447-524.
DR   PRIDE; Q8BXL9; -.
DR   Ensembl; ENSMUST00000051171; ENSMUSP00000056373; ENSMUSG00000038271.
DR   Ensembl; ENSMUST00000088276; ENSMUSP00000085614; ENSMUSG00000038271.
DR   GeneID; 320678; -.
DR   KEGG; mmu:320678; -.
DR   UCSC; uc009dto.1; mouse.
DR   CTD; 320678; -.
DR   MGI; MGI:2444516; Iffo1.
DR   eggNOG; roNOG11597; -.
DR   GeneTree; ENSGT00510000046803; -.
DR   HOGENOM; HBG444425; -.
DR   HOVERGEN; HBG100545; -.
DR   InParanoid; Q8BXL9; -.
DR   OMA; AGPLGDS; -.
DR   OrthoDB; EOG4N8R4T; -.
DR   PhylomeDB; Q8BXL9; -.
DR   NextBio; 397195; -.
DR   ArrayExpress; Q8BXL9; -.
DR   Bgee; Q8BXL9; -.
DR   Genevestigator; Q8BXL9; -.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil.
FT   CHAIN         1    562       Intermediate filament family orphan 1.
FT                                /FTId=PRO_0000316795.
FT   COILED       85    117       Potential.
FT   COILED      237    301       Potential.
FT   COILED      458    504       Potential.
FT   COMPBIAS    541    545       Poly-Pro.
FT   VAR_SEQ       1    191       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_030785.
FT   VAR_SEQ     259    562       Missing (in isoform 2).
FT                                /FTId=VSP_030786.
FT   VAR_SEQ     358    360       Missing (in isoform 3 and isoform 5).
FT                                /FTId=VSP_030787.
FT   VAR_SEQ     358    358       Missing (in isoform 4 and isoform 6).
FT                                /FTId=VSP_030788.
FT   CONFLICT    291    291       A -> P (in Ref. 1; BAC25852).
FT   CONFLICT    331    331       C -> W (in Ref. 1; BAC25852).
FT   CONFLICT    345    345       Q -> H (in Ref. 1; BAC25852).
FT   CONFLICT    454    454       Q -> QQ (in Ref. 1; BAC25852 and 2;
FT                                AAH57601).
SQ   SEQUENCE   562 AA;  62415 MW;  4310CC2DEAC8B604 CRC64;
     MNPLFGPNLF LLQQEQQGLA GPLGDPLGGD HFAGGGDLAS APLASAGPSA YSPPGPGPAP
     PAAMALRNDL GSNINVLKTL NLRFRCFLAK VHELERRNRL LEKQLQQALE EGKQGRRGLA
     RRDQAVQTGF ISPIRPLGLP LSSRPAAVCP PSARVLGSPS RSPAGPLASS AACHTSSSTS
     TSTAFSSSTR FMPGTIWSFS HARRLGPGLE PTLVQGPGLS WVHPDGVGVQ IDTITPEIRA
     LYNVLAKVKR ERDEYKRRWE EEYTVRIQLQ ERVTELQEEA QEADACQEEL AMKVEQLKAE
     LVVFKGLMSN NLTELDTKIQ EKAMKVDMDI CRRIDITAKL CDLAQQRNCE DMIQMFQKKL
     VPSMGGRKRE RKAAVEEDTS LSESDGPRQP EGAEEESTAL SINEEMQRML SQLREYDFED
     DCDSLTWEET EETLLLWEDF SGYAMAAAEA QGEQEDSLEK VIKDTESLFK TREKEYQETI
     DQIELELATA KNDMNRHLHE YMEMCSMKRG LDVQMETCRR LITQSGDRKS PAFTAVPLSD
     PPPPPSETED SDRDVSSDSS MR
//
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   PGLT1_MOUSE             Reviewed;         392 AA.
AC   Q8BYB9; Q8R0H7;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Protein O-glucosyltransferase 1;
DE            EC=2.4.1.-;
DE   AltName: Full=CAP10-like 46 kDa protein;
DE   AltName: Full=KTEL motif-containing protein 1;
DE   Flags: Precursor;
GN   Name=Poglut1; Synonyms=Clp46, Ktelc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; 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, 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=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: UDP-glucosyltransferase (By similarity).
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity).
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 90 family.
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DR   EMBL; AK031608; BAC27475.1; -; mRNA.
DR   EMBL; AK035948; BAC29255.1; -; mRNA.
DR   EMBL; AK036224; BAC29351.1; -; mRNA.
DR   EMBL; AK041321; BAC30905.1; -; mRNA.
DR   EMBL; BC026809; AAH26809.1; -; mRNA.
DR   IPI; IPI00453707; -.
DR   RefSeq; NP_759012.1; NM_172380.3.
DR   UniGene; Mm.284366; -.
DR   UniGene; Mm.475345; -.
DR   CAZy; GT90; Glycosyltransferase Family 90.
DR   PRIDE; Q8BYB9; -.
DR   Ensembl; ENSMUST00000036210; ENSMUSP00000038166; ENSMUSG00000034064.
DR   GeneID; 224143; -.
DR   KEGG; mmu:224143; -.
DR   UCSC; uc007zfc.1; mouse.
DR   CTD; 224143; -.
DR   MGI; MGI:2444232; Ktelc1.
DR   GeneTree; ENSGT00530000063132; -.
DR   HOGENOM; HBG715408; -.
DR   HOVERGEN; HBG069044; -.
DR   InParanoid; Q8BYB9; -.
DR   OMA; DEWQEFF; -.
DR   OrthoDB; EOG4SN1P0; -.
DR   PhylomeDB; Q8BYB9; -.
DR   NextBio; 377117; -.
DR   ArrayExpress; Q8BYB9; -.
DR   Bgee; Q8BYB9; -.
DR   CleanEx; MM_KTELC1; -.
DR   Genevestigator; Q8BYB9; -.
DR   GermOnline; ENSMUSG00000034064; Mus musculus.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR   GO; GO:0035251; F:UDP-glucosyltransferase activity; ISS:UniProtKB.
DR   InterPro; IPR006598; LipoPS_modifying.
DR   Pfam; PF05686; DUF821; 1.
DR   SMART; SM00672; CAP10; 1.
DR   PROSITE; PS00014; ER_TARGET; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Signal;
KW   Transferase.
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24    392       Protein O-glucosyltransferase 1.
FT                                /FTId=PRO_0000246686.
FT   MOTIF       389    392       Prevents secretion from ER (Potential).
FT   CARBOHYD     53     53       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    204    204       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    373    373       N-linked (GlcNAc...) (Potential).
FT   CONFLICT     53     53       N -> S (in Ref. 1; BAC30905).
SQ   SEQUENCE   392 AA;  46379 MW;  CAAD9133E47D3EF0 CRC64;
     MERRAGSRLR AWMLLLLLCP VQGRQKDSGS KWKVFLDQIN RALENYEPCS SQNCSCYHGV
     IEEDLTPFRG GISRKMMAEV VRRKLGTHYQ IIKNRLFRED DCMFPSRCSG VEHFILEVIH
     RLPDMEMVIN VRDYPQVPKW MEPTIPVFSF SKTSEYHDIM YPAWTFWEGG PAVWPLYPTG
     LGRWDLFRED LLRSAAQWPW EKKNSTAYFR GSRTSPERDP LILLSRKNPK LVDAEYTKNQ
     AWKSMKDTLG KPAAKDVHLI DHCKYRYLFN FRGVAASFRF KHLFLCGSLV FHVGDEWVEF
     FYPQLKPWVH YIPVKTDLSN VQELLQFVKA NDDIAQEIAK RGSQFIINHL QMDDITCYWE
     NLLTDYSKFL SYNVTRRKDY YQIVPRRLKT EL
//
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   YTHD3_MOUSE             Reviewed;         585 AA.
AC   Q8BYK6; Q3UVI5; Q6NXJ6; Q6NXJ8; Q8BKB6;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=YTH domain family protein 3;
GN   Name=Ythdf3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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, Hypothalamus, 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] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and 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   [3]
RP   PROTEIN SEQUENCE OF 196-206, 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=3;
CC       Name=1;
CC         IsoId=Q8BYK6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BYK6-2; Sequence=VSP_017833;
CC       Name=3;
CC         IsoId=Q8BYK6-3; Sequence=VSP_017834;
CC   -!- SIMILARITY: Contains 1 YTH domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK137245; BAE23284.1; -; mRNA.
DR   EMBL; AK039176; BAC30267.1; -; mRNA.
DR   EMBL; AK053736; BAC35498.1; -; mRNA.
DR   EMBL; BC057158; AAH57158.1; -; mRNA.
DR   EMBL; BC067040; AAH67040.1; -; mRNA.
DR   EMBL; BC067042; AAH67042.1; -; mRNA.
DR   IPI; IPI00227149; -.
DR   IPI; IPI00465894; -.
DR   IPI; IPI00742314; -.
DR   RefSeq; NP_001139391.1; NM_001145919.1.
DR   RefSeq; NP_766265.3; NM_172677.3.
DR   UniGene; Mm.23834; -.
DR   ProteinModelPortal; Q8BYK6; -.
DR   SMR; Q8BYK6; 412-552.
DR   PhosphoSite; Q8BYK6; -.
DR   PRIDE; Q8BYK6; -.
DR   Ensembl; ENSMUST00000050490; ENSMUSP00000062802; ENSMUSG00000047213.
DR   Ensembl; ENSMUST00000108345; ENSMUSP00000103982; ENSMUSG00000047213.
DR   Ensembl; ENSMUST00000108346; ENSMUSP00000103983; ENSMUSG00000047213.
DR   GeneID; 229096; -.
DR   KEGG; mmu:229096; -.
DR   UCSC; uc008org.1; mouse.
DR   UCSC; uc008orh.1; mouse.
DR   UCSC; uc008ori.1; mouse.
DR   CTD; 229096; -.
DR   MGI; MGI:1918850; Ythdf3.
DR   eggNOG; roNOG11283; -.
DR   HOVERGEN; HBG060315; -.
DR   OMA; PPMSDPY; -.
DR   OrthoDB; EOG4RR6H8; -.
DR   PhylomeDB; Q8BYK6; -.
DR   NextBio; 379337; -.
DR   ArrayExpress; Q8BYK6; -.
DR   Bgee; Q8BYK6; -.
DR   CleanEx; MM_YTHDF3; -.
DR   Genevestigator; Q8BYK6; -.
DR   InterPro; IPR007275; YTH_domain.
DR   PANTHER; PTHR12357; YTH; 1.
DR   Pfam; PF04146; YTH; 1.
DR   PROSITE; PS50882; YTH; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing.
FT   CHAIN         1    585       YTH domain family protein 3.
FT                                /FTId=PRO_0000230992.
FT   DOMAIN      416    550       YTH.
FT   COMPBIAS    226    340       Pro-rich.
FT   COMPBIAS    292    351       Gln-rich.
FT   COMPBIAS    571    574       Poly-Glu.
FT   VAR_SEQ       1     17       MSATSVDQRPKGQGNKV -> MFYLDLTLLHRATEETGEES
FT                                F (in isoform 2).
FT                                /FTId=VSP_017833.
FT   VAR_SEQ      45     45       Q -> QKYRRAKQLFHC (in isoform 3).
FT                                /FTId=VSP_017834.
FT   CONFLICT    231    231       A -> P (in Ref. 2; AAH67042).
FT   CONFLICT    502    502       E -> G (in Ref. 1; BAC30267).
FT   CONFLICT    531    531       N -> D (in Ref. 1; BAE23284).
SQ   SEQUENCE   585 AA;  63961 MW;  E6A12F76A3781770 CRC64;
     MSATSVDQRP KGQGNKVSVQ NGSIHQKDAV NDDDFEPYLS SQTNQNNSYP PMSDPYMPSY
     YAPSIGFPYS LGEAAWSTAG DQPMPYLTTY GQMSNGEHHY IPDGVFSQPG ALGNTPPFLG
     QHGFNFFPGN ADFSTWGTSG SQGQSTQNSA YSSSYGYPPS SLGRAITDGQ AGFGNDTLSK
     VPGISSIEQG MTGLKIGGDL TAAVTKTVGT ALSSSGMTSI ATNNVPPVSS AAPKPTSWAA
     IARKPAKPQP KLKPKGNVGI GGSAVPPPPI KHNMNIGTWD EKGSVVKAPP TQPVLPPQTI
     IQQPQPLIQP PPLVQSQLPQ QQPQPPQPQQ QQGPQPQAQP HQVQSQQPQL QNRWVAPRNR
     GTGFNQNNGT GSENFGLGVV PVSASPSSVE VHPVLEKLKA INNYNPKDFD WNLKNGRVFI
     IKSYSEDDIH RSIKYSIWCS TEHGNKRLDA AYRSLNGKGP LYLLFSVNGS GHFCGVAEMK
     SVVDYNAYAG VWSQDKWKGK FEVKWIFVKD VPNNQLRHIR LENNDNKPVT NSRDTQEVPL
     EKAKQVLKII ATFKHTTSIF DDFAHYEKRQ EEEEAMRRER NRNKQ
//
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;
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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.
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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   A16L1_MOUSE             Reviewed;         607 AA.
AC   Q8C0J2; Q6KAT7; Q80U97; Q80U98; Q80U99; Q80Y53; Q9DB63;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Autophagy-related protein 16-1;
DE   AltName: Full=APG16-like 1;
GN   Name=Atg16l1; Synonyms=Apg16l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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, TISSUE
RP   SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH ATG5.
RX   MEDLINE=22552481; PubMed=12665549; DOI=10.1242/jcs.00381;
RA   Mizushima N., Kuma A., Kobayashi Y., Yamamoto A., Matsubae M.,
RA   Takao T., Natsume T., Ohsumi Y., Yoshimori T.;
RT   "Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic
RT   isolation membrane with the Apg12-Apg5 conjugate.";
RL   J. Cell Sci. 116:1679-1688(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
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   [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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.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 an essential role in autophagy.
CC   -!- SUBUNIT: Homooligomer. Interacts with ATG5. Part of either the
CC       minor and major complexes respectively composed of 4 sets of
CC       ATG12-ATG5 and ATG16L1 (400 kDa) or 8 sets of ATG12-ATG5 and
CC       ATG16L1 (800 kDa).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Preautophagosomal structure
CC       membrane; Peripheral membrane protein. Note=Localized to
CC       preautophagosomal structure (PAS) where it is involved in the
CC       membrane targeting of ATG5.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1; Synonyms=Apg16Lbeta;
CC         IsoId=Q8C0J2-1; Sequence=Displayed;
CC       Name=2; Synonyms=Apg16Lalpha;
CC         IsoId=Q8C0J2-2; Sequence=VSP_013391;
CC         Note=No experimental confirmation available;
CC       Name=3; Synonyms=Apg16Lgamma;
CC         IsoId=Q8C0J2-3; Sequence=VSP_013392;
CC       Name=4;
CC         IsoId=Q8C0J2-4; Sequence=VSP_013392, VSP_013394, VSP_013395;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q8C0J2-5; Sequence=VSP_013391, VSP_013393;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Widely expressed. In the liver, isoform 2 is
CC       highly expressed and isoform 1 is weakly expressed. Isoform 3 is
CC       expressed in the brain.
CC   -!- SIMILARITY: Belongs to the WD repeat ATG16 family.
CC   -!- SIMILARITY: Contains 7 WD repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD21370.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB087879; BAC55090.1; -; mRNA.
DR   EMBL; AB087880; BAC55091.1; -; mRNA.
DR   EMBL; AB087881; BAC55092.1; -; mRNA.
DR   EMBL; AK005181; BAB23866.1; -; mRNA.
DR   EMBL; AK030983; BAC27201.1; -; mRNA.
DR   EMBL; AK131120; BAD21370.1; ALT_INIT; Transcribed_RNA.
DR   EMBL; BC049122; AAH49122.1; -; mRNA.
DR   IPI; IPI00223832; -.
DR   IPI; IPI00403350; -.
DR   IPI; IPI00554838; -.
DR   IPI; IPI00554885; -.
DR   IPI; IPI00555120; -.
DR   RefSeq; NP_084122.2; NM_029846.3.
DR   UniGene; Mm.272972; -.
DR   ProteinModelPortal; Q8C0J2; -.
DR   SMR; Q8C0J2; 308-605.
DR   DIP; DIP-31966N; -.
DR   MINT; MINT-136268; -.
DR   STRING; Q8C0J2; -.
DR   PhosphoSite; Q8C0J2; -.
DR   REPRODUCTION-2DPAGE; Q8C0J2; -.
DR   PRIDE; Q8C0J2; -.
DR   Ensembl; ENSMUST00000027512; ENSMUSP00000027512; ENSMUSG00000026289.
DR   Ensembl; ENSMUST00000113188; ENSMUSP00000108813; ENSMUSG00000026289.
DR   Ensembl; ENSMUST00000113190; ENSMUSP00000108815; ENSMUSG00000026289.
DR   GeneID; 77040; -.
DR   KEGG; mmu:77040; -.
DR   UCSC; uc007bxk.1; mouse.
DR   UCSC; uc007bxl.1; mouse.
DR   UCSC; uc007bxm.1; mouse.
DR   UCSC; uc007bxn.1; mouse.
DR   CTD; 77040; -.
DR   MGI; MGI:1924290; Atg16l1.
DR   eggNOG; roNOG13874; -.
DR   GeneTree; ENSGT00600000084184; -.
DR   HOVERGEN; HBG050534; -.
DR   OMA; ETECQEL; -.
DR   OrthoDB; EOG4SXNC8; -.
DR   PhylomeDB; Q8C0J2; -.
DR   NextBio; 346354; -.
DR   ArrayExpress; Q8C0J2; -.
DR   Bgee; Q8C0J2; -.
DR   CleanEx; MM_ATG16L1; -.
DR   Genevestigator; Q8C0J2; -.
DR   GermOnline; ENSMUSG00000026289; Mus musculus.
DR   GO; GO:0005776; C:autophagic vacuole; IDA:MGI.
DR   GO; GO:0034045; C:pre-autophagosomal structure membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0000045; P:autophagic vacuole assembly; TAS:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR013923; Autophagy-rel_prot_16.
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; PF08614; ATG16; 1.
DR   Pfam; PF00400; WD40; 7.
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   Alternative splicing; Autophagy; Coiled coil; Cytoplasm; Membrane;
KW   Phosphoprotein; Protein transport; Repeat; Transport; WD repeat.
FT   CHAIN         1    607       Autophagy-related protein 16-1.
FT                                /FTId=PRO_0000050849.
FT   REPEAT      320    359       WD 1.
FT   REPEAT      364    403       WD 2.
FT   REPEAT      406    445       WD 3.
FT   REPEAT      447    484       WD 4.
FT   REPEAT      486    525       WD 5.
FT   REPEAT      532    573       WD 6.
FT   REPEAT      575    607       WD 7.
FT   COILED       79    230       Potential.
FT   MOD_RES     287    287       Phosphoserine (By similarity).
FT   MOD_RES     289    289       Phosphoserine.
FT   MOD_RES     290    290       Phosphoserine (By similarity).
FT   MOD_RES     304    304       Phosphoserine (By similarity).
FT   VAR_SEQ     266    284       Missing (in isoform 2 and isoform 5).
FT                                /FTId=VSP_013391.
FT   VAR_SEQ     284    284       G -> GLSESPLLGHHSSDAAR (in isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_013392.
FT   VAR_SEQ     442    442       C -> CEEMQSLCVLMVFGFLSG (in isoform 5).
FT                                /FTId=VSP_013393.
FT   VAR_SEQ     443    452       IKTVFAGSSC -> EEMQSLCVFM (in isoform 4).
FT                                /FTId=VSP_013394.
FT   VAR_SEQ     453    607       Missing (in isoform 4).
FT                                /FTId=VSP_013395.
FT   CONFLICT     83     83       Q -> H (in Ref. 1; BAC55090/BAC55091/
FT                                BAC55092 and 2; BAB23866).
SQ   SEQUENCE   607 AA;  68172 MW;  63920320883A69DF CRC64;
     MSSGLRAADF PRWKRHIAEE LRRRDRLQRQ AFEEIILQYT KLLEKSDLHS VLTQKLQAEK
     HDMPNRHEIS PGHDGAWNDS QLQEMAQLRI KHQEELTELH KKRGELAQLV IDLNNQMQQK
     DKEIQMNEAK ISEYLQTISD LETNCLDLRT KLQDLEVANQ TLKDEYDALQ ITFTALEEKL
     RKTTEENQEL VTRWMAEKAQ EANRLNAENE KDSRRRQARL QKELAEAAKE PLPVEQDDDI
     EVIVDETSDH TEETSPVRAV SRAATKRLSQ PAGGLLDSIT NIFGRRSVSS IPVPQDIMDT
     HPASGKDVRV PTTASYVFDA HDGEVNAVQF SPGSRLLATG GMDRRVKLWE AFGDKCEFKG
     SLSGSNAGIT SIEFDSAGAY LLAASNDFAS RIWTVDDYRL RHTLTGHSGK VLSAKFLLDN
     ARIVSGSHDR TLKLWDLRSK VCIKTVFAGS SCNDIVCTEQ CVMSGHFDKK IRFWDIRSES
     VVREMELLGK ITALDLNPER TELLSCSRDD LLKVIDLRTN AVKQTFSAPG FKCGSDWTRV
     VFSPDGSYVA AGSAEGSLYV WSVLTGKVEK VLSKQHSSSI NAVAWAPSGL HVVSVDKGSR
     AVLWAQP
//
ID   ZN451_MOUSE             Reviewed;        1056 AA.
AC   Q8C0P7;
DT   24-OCT-2003, 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 451;
GN   Name=Znf451; Synonyms=Zfp451;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; 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: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family.
CC   -!- SIMILARITY: Contains 12 C2H2-type zinc fingers.
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DR   EMBL; AK030088; BAC26778.1; -; mRNA.
DR   IPI; IPI00223899; -.
DR   RefSeq; NP_598578.1; NM_133817.2.
DR   UniGene; Mm.289103; -.
DR   UniGene; Mm.440137; -.
DR   ProteinModelPortal; Q8C0P7; -.
DR   SMR; Q8C0P7; 152-272, 310-337, 364-389, 462-554, 601-692, 740-811.
DR   STRING; Q8C0P7; -.
DR   PRIDE; Q8C0P7; -.
DR   Ensembl; ENSMUST00000019861; ENSMUSP00000019861; ENSMUSG00000042197.
DR   GeneID; 98403; -.
DR   KEGG; mmu:98403; -.
DR   UCSC; uc007anz.1; mouse.
DR   CTD; 98403; -.
DR   MGI; MGI:2137896; Zfp451.
DR   HOGENOM; HBG279770; -.
DR   HOVERGEN; HBG057364; -.
DR   InParanoid; Q8C0P7; -.
DR   OMA; GHRYFYE; -.
DR   OrthoDB; EOG4H729R; -.
DR   PhylomeDB; Q8C0P7; -.
DR   NextBio; 353460; -.
DR   ArrayExpress; Q8C0P7; -.
DR   Bgee; Q8C0P7; -.
DR   CleanEx; MM_ZFP451; -.
DR   Genevestigator; Q8C0P7; -.
DR   GermOnline; ENSMUSG00000042197; 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; 12.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1   1056       Zinc finger protein 451.
FT                                /FTId=PRO_0000047599.
FT   ZN_FING     169    195       C2H2-type 1.
FT   ZN_FING     212    234       C2H2-type 2; degenerate.
FT   ZN_FING     253    277       C2H2-type 3.
FT   ZN_FING     315    338       C2H2-type 4; atypical.
FT   ZN_FING     362    385       C2H2-type 5.
FT   ZN_FING     494    517       C2H2-type 6.
FT   ZN_FING     527    550       C2H2-type 7.
FT   ZN_FING     604    629       C2H2-type 8; atypical.
FT   ZN_FING     634    657       C2H2-type 9.
FT   ZN_FING     665    688       C2H2-type 10.
FT   ZN_FING     751    774       C2H2-type 11.
FT   ZN_FING     787    810       C2H2-type 12.
SQ   SEQUENCE   1056 AA;  120070 MW;  7D8FBC0B50ECA622 CRC64;
     MGDPGPEIIE SVPPAGPEAS ESTTDENEDD IQFVSEGPLR PVLEYIDLVS SDDEEPSTSH
     SDENFKCKDY IDHQKDKVAL TLARLARHVE VEKQQKEEKN RAFREKIDFQ HAHGLQELEF
     IQGHSETEAA RQCVDQWLKM PGLRTNAANS GTKRSFQRGG RMWRSEKPIL CPIMHCNKEF
     DNGHLLLGHL KRFDHSPCDP TITLHGPLAN SFACAVCYEH FVTQQQYKDH LLSRTAAADG
     HSNSLLPQII QCYACPQCFL LFSTKDECLK HMSTKNHFHQ SFKLSDNKGT ARPISFPSFA
     KKRLVSLCKD VPFQVKCVAC HQTLRSHMEL TAHFRVRCQN AGPVAIAEKS ITQVAKEFIV
     RGYCSDCNQV FMDVASTQSH KNSGHKITLA NSVEESVLLY CHISEGSRPP CDLHLFSQPK
     ISSLKRILSV KESSAEDCIV PTKKVNLGVE SLGGATRVQR QSPAVTAWFC ECRRQFPSEE
     AVEKHVFSAN TMCYKCVVCG KVCEDSGVMR LHMSRFHGGA HLNNFLFWCR TCKKELVKKD
     AIMAHITEFH SGHRYFYEMD EVEEEEEEAM PSSSVESHLN TDKPPSPIAV VDHCPANSPP
     RGRWQCRICE DMFESQECVK QHCMSLTSHR FHRYSCAHCR KTFHKVETLY RHCQDEHDSE
     IMMKYFCGLC DLIFNKEEEF LSHYKEHHSI DYVFVSEKTK TSIKTEGDFK IVETSSLLSC
     GCHESYMCKI NRKEDYDRCL PVLLEKGRLW FRCSSCSATA QNVTDINTHV CQVHRKEKSE
     EEQQYVIKCG ICTKAFQNTE SAQQHFHRKH AALQKPTATP GGANRSSTCQ LAASASHAEK
     NLKQPSSQKH SDVEKGAEHD VRCQNIEEEV ELPDVDYLRT MTHIVFVDFD NWSNFFGHLP
     GHLNQGTFIW GFQGGNTNWK PPLSCKVYNY LSRIGCFFLH PRCSKRKDAA DFAICMHAGR
     LDEQLPKQIP FTILSGDQGF LELENQFKKT QRPAHILNPH HLEGDMMCAL LNSISDTTKE
     CDSDDSSGMK GSPAEELRAT EDVELEEAIR RSLEEM
//
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   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   SH3R3_MOUSE             Reviewed;         878 AA.
AC   Q8C120; Q3V0K8; Q3V0Q0;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=SH3 domain-containing RING finger protein 3;
DE   AltName: Full=Plenty of SH3s 2;
DE   AltName: Full=SH3 multiple domains protein 4;
GN   Name=Sh3rf3; Synonyms=Posh2, Sh3md4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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 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   [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   -!- SUBUNIT: Interacts with PAK2 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8C120-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C120-2; Sequence=VSP_024719;
CC       Name=3;
CC         IsoId=Q8C120-3; Sequence=VSP_024718, VSP_024720, VSP_024721,
CC                                  VSP_024722, VSP_024723;
CC       Name=4;
CC         IsoId=Q8C120-4; Sequence=VSP_024724, VSP_024725;
CC   -!- DOMAIN: The third SH3 domain mediates interaction with PAK2 (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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC153367; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC159909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK029202; BAC26346.1; -; mRNA.
DR   EMBL; AK132983; BAE21454.1; -; mRNA.
DR   EMBL; AK133071; BAE21496.1; -; mRNA.
DR   EMBL; BC057304; AAH57304.1; -; mRNA.
DR   IPI; IPI00283065; -.
DR   IPI; IPI00653897; -.
DR   IPI; IPI00845734; -.
DR   IPI; IPI00845810; -.
DR   RefSeq; NP_766376.2; NM_172788.3.
DR   UniGene; Mm.333078; -.
DR   UniGene; Mm.410104; -.
DR   HSSP; Q8C1E3; 2CUC.
DR   ProteinModelPortal; Q8C120; -.
DR   SMR; Q8C120; 51-97, 186-311, 461-519, 821-877.
DR   PhosphoSite; Q8C120; -.
DR   PRIDE; Q8C120; -.
DR   Ensembl; ENSMUST00000099724; ENSMUSP00000097312; ENSMUSG00000037990.
DR   GeneID; 237353; -.
DR   KEGG; mmu:237353; -.
DR   NMPDR; fig|10090.3.peg.13711; -.
DR   UCSC; uc007fdk.1; mouse.
DR   CTD; 237353; -.
DR   MGI; MGI:2444637; Sh3rf3.
DR   eggNOG; roNOG07828; -.
DR   GeneTree; ENSGT00550000074287; -.
DR   HOGENOM; HBG506330; -.
DR   HOVERGEN; HBG069552; -.
DR   InParanoid; Q8C120; -.
DR   OMA; PTHDPQV; -.
DR   OrthoDB; EOG4PG61S; -.
DR   PhylomeDB; Q8C120; -.
DR   NextBio; 383312; -.
DR   ArrayExpress; Q8C120; -.
DR   Bgee; Q8C120; -.
DR   Genevestigator; Q8C120; -.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR000108; p67phox.
DR   InterPro; IPR001452; SH3_domain.
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   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   2: Evidence at transcript level;
KW   Alternative splicing; Metal-binding; Phosphoprotein; Repeat;
KW   SH3 domain; Zinc; Zinc-finger.
FT   CHAIN         1    878       SH3 domain-containing RING finger protein
FT                                3.
FT                                /FTId=PRO_0000284884.
FT   DOMAIN      187    246       SH3 1.
FT   DOMAIN      249    312       SH3 2.
FT   DOMAIN      458    519       SH3 3.
FT   DOMAIN      819    878       SH3 4.
FT   ZN_FING      52     93       RING-type.
FT   MOD_RES     395    395       Phosphoserine (By similarity).
FT   MOD_RES     536    536       Phosphoserine (By similarity).
FT   MOD_RES     792    792       Phosphoserine (By similarity).
FT   VAR_SEQ       1    415       Missing (in isoform 3).
FT                                /FTId=VSP_024718.
FT   VAR_SEQ       1    261       Missing (in isoform 2).
FT                                /FTId=VSP_024719.
FT   VAR_SEQ     416    428       GELAHLSCTVPTQ -> MDAPEKYTERATP (in
FT                                isoform 3).
FT                                /FTId=VSP_024720.
FT   VAR_SEQ     429    438       DSSSAGPVPT -> VIPRAGGLCP (in isoform 4).
FT                                /FTId=VSP_024724.
FT   VAR_SEQ     439    878       Missing (in isoform 4).
FT                                /FTId=VSP_024725.
FT   VAR_SEQ     518    518       S -> SRSPHPSHSGEVRVRLAQE (in isoform 3).
FT                                /FTId=VSP_024721.
FT   VAR_SEQ     712    741       KEKKSGLLKLLAGASTKKKSRSPPSVSPTH -> VSGPSWA
FT                                NPEPGAGWLLGPSHTLANGAENR (in isoform 3).
FT                                /FTId=VSP_024722.
FT   VAR_SEQ     742    878       Missing (in isoform 3).
FT                                /FTId=VSP_024723.
SQ   SEQUENCE   878 AA;  93130 MW;  A1B274FE31334F3A CRC64;
     MLLGASWLCA SKAAATAARG EGEDRQGEQQ RGAQARTEED MDESSLLDLL ECSVCLERLD
     TTAKVLPCQH TFCRRCLESI VCSRHELRCP ECRILVGCGV DELPANILLV RLLDGIRQRP
     RTGASPGSSP PARPGPGTFS ALAGGAGGAT GSPPCSPVFL SAAAGSSTSS LCDVATNRSV
     PVAKTLSQLP YAKALYSYEG KEPGDLKFNK GDIIILRRKV DENWYHGELQ GMHGFLPASY
     IQCVRPLPQA LPQGKALYDF EMKDRDQDKD CLTFTKDEVL TVIRRVDDNW AEGMLGDKIG
     IFPLLYVELN DSAKQLIEMD KLCPAATTAY NYDALLSSDP STVASVAPGP TLSSSGAVSA
     FQRRVDSKKN AKKRHSFTAL SVTHKSSQAA SHRHSMEISA PVLISSSDPR AAARIGELAH
     LSCTVPTQDS SSAGPVPTAL PRAAAVAGEQ GMSPKVQLPL NVYLALYAYK PQKNDELELR
     KGEMYRVLEK CQDGWFKGAS LKTGVSGVFP GNYVTPVSRV PGGGAGLPWN NVLGGSPLAK
     GMATIMHPGG GSLSSPATAA RSALPLTTLQ DHMQHPATSL PTGSCLRHSA QPTASQAGDT
     TIPTATHASA QALDRPTATV SPLRTQTSPS RLPSTGLRPR SVASPQHGQQ SPAQMCPRPA
     IPFTSAASAI TPPNVSAANL SGEVGGTPIS GLSTPSLINT GFKPDDKKNE KKEKKSGLLK
     LLAGASTKKK SRSPPSVSPT HDPQSAMDTS LQGAMGPEVS PLTVHGRAGS CPIESEMQGA
     IGLEPLHRKA GSLDLNFSLS PSRQATLSMA SIRPEPKPLP RERYRVVVSY PPQSEAEIEL
     KEGDIVFVHK KHEDGWFKGT LQRNGRTGLF PGSFVESF
//
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   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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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   ENDD1_MOUSE             Reviewed;         501 AA.
AC   Q8C522; Q4VA96; Q8C5M1; Q8VE35;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Endonuclease domain-containing 1 protein;
DE            EC=3.1.30.-;
DE   Flags: Precursor;
GN   Name=Endod1; Synonyms=Kiaa0830;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; 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 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, 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   PROTEIN SEQUENCE OF 195-208 AND 239-252, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: May act as a DNase and a RNase (Potential).
CC   -!- SUBCELLULAR LOCATION: Secreted (Potential).
CC   -!- SIMILARITY: Belongs to the DNA/RNA non-specific endonuclease
CC       family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK078056; BAC37111.1; -; mRNA.
DR   EMBL; AK079741; BAC37737.1; -; mRNA.
DR   EMBL; BC019813; AAH19813.1; -; mRNA.
DR   EMBL; BC096490; AAH96490.1; -; mRNA.
DR   IPI; IPI00470004; -.
DR   RefSeq; NP_082289.2; NM_028013.3.
DR   UniGene; Mm.41423; -.
DR   ProteinModelPortal; Q8C522; -.
DR   STRING; Q8C522; -.
DR   PhosphoSite; Q8C522; -.
DR   PRIDE; Q8C522; -.
DR   Ensembl; ENSMUST00000041780; ENSMUSP00000045861; ENSMUSG00000037419.
DR   GeneID; 71946; -.
DR   KEGG; mmu:71946; -.
DR   UCSC; uc009oel.1; mouse.
DR   CTD; 71946; -.
DR   MGI; MGI:1919196; Endod1.
DR   HOVERGEN; HBG081477; -.
DR   InParanoid; Q8C522; -.
DR   OMA; LRILCCL; -.
DR   OrthoDB; EOG4THVTB; -.
DR   NextBio; 335016; -.
DR   ArrayExpress; Q8C522; -.
DR   Bgee; Q8C522; -.
DR   CleanEx; MM_ENDOD1; -.
DR   Genevestigator; Q8C522; -.
DR   GermOnline; ENSMUSG00000037419; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR   InterPro; IPR020821; Extracellular_endonuc_su_A.
DR   Gene3D; G3DSA:3.40.570.10; Endonuclease; 1.
DR   SMART; SM00892; Endonuclease_NS; 1.
DR   SMART; SM00477; NUC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Endonuclease; Hydrolase;
KW   Nuclease; Secreted; Signal.
FT   SIGNAL        1     21       Potential.
FT   CHAIN        22    501       Endonuclease domain-containing 1 protein.
FT                                /FTId=PRO_0000019925.
FT   MOD_RES     408    408       N6-acetyllysine (By similarity).
FT   CONFLICT    118    118       L -> V (in Ref. 2; AAH19813).
FT   CONFLICT    148    148       P -> H (in Ref. 2; AAH19813).
FT   CONFLICT    396    396       V -> L (in Ref. 1; BAC37111).
FT   CONFLICT    440    440       T -> S (in Ref. 2; AAH19813).
FT   CONFLICT    463    463       T -> N (in Ref. 1; BAC37111).
SQ   SEQUENCE   501 AA;  55262 MW;  18E08148DD8D42B7 CRC64;
     MGCARWLALG GLLALAGLLQ ARLLLPQQAG FGECDRFFYK GTPPAGLATE AHVRICQRFA
     GSERFATLYS PGHRIPVFSA FRAARPASRS AEQRGLLEPQ IDDPDSNLEE VIDEANALTS
     VDNLGSKQAL NADYIDSDYE IGQLYPFPLN SDLQMATFPL TNSVPMTQSF RERWHMNLNS
     LMDRALIPHC SEGKDLYILT GAVPSEHRVK GKVTIPEFVW LAACCAVPGE GWAMGFIKHT
     QDIDVIEDVM LRDLEKLLPH KPQLFQDNCG EMEQDTEKMK KILEVVNQVQ DEERSLQSQE
     RMSPLASTQS QRSALLSPEA PPEGGSSFLG QVLGFLATPF IKLFQLIYYL VTAVLRNIVH
     LLWLVAKQAI NTVESCLYHL GEATVSYLVA IGQELVSIPW KVLKVVAKVI RAFLRILCCL
     LKAVCRALSI PLRVLVDVAT FPVYTVGAIP IVCKDIAVGL GGTLSLLFDT AFGTVGGLFQ
     IVFSVFKRIG YKVTLDNSGE F
//
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   Distributed under the Creative Commons Attribution-NoDerivs License
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   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   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   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   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;
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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   EPC1_MOUSE              Reviewed;         813 AA.
AC   Q8C9X6; B2RRY2; Q9Z299;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Enhancer of polycomb homolog 1;
GN   Name=Epc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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=98407961; PubMed=9735366;
RA   Stankunas K., Berger J., Ruse C., Sinclair D.A.R., Randazzo F.,
RA   Brock H.W.;
RT   "The enhancer of polycomb gene of Drosophila encodes a chromatin
RT   protein conserved in yeast and mammals.";
RL   Development 125:4055-4066(1998).
RN   [2]
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   [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: Component of the NuA4 histone acetyltransferase (HAT)
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. NuA4 may also
CC       play a direct role in DNA repair when directly recruited to sites
CC       of DNA damage (By similarity).
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. HTATTIP/TIP60, EPC1, and
CC       ING3 together constitute a minimal HAT complex termed Piccolo
CC       NuA4. Component of a NuA4-related complex which contains EP400,
CC       TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49,
CC       RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. The NuA4
CC       complex interacts with MYC. EPC1 interacts with TRIM27 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8C9X6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C9X6-2; Sequence=VSP_012878;
CC   -!- TISSUE SPECIFICITY: Expressed in adult brain, heart, kidney,
CC       liver, lung, skeletal muscle and testis.
CC   -!- SIMILARITY: Belongs to the enhancer of polycomb family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF079765; AAC64272.1; -; mRNA.
DR   EMBL; AK040254; BAC30552.1; -; mRNA.
DR   EMBL; BC138622; AAI38623.1; -; mRNA.
DR   EMBL; BC138623; AAI38624.1; -; mRNA.
DR   IPI; IPI00177080; -.
DR   IPI; IPI00227740; -.
DR   RefSeq; NP_031961.1; NM_007935.1.
DR   RefSeq; NP_081773.1; NM_027497.2.
DR   UniGene; Mm.312133; -.
DR   ProteinModelPortal; Q8C9X6; -.
DR   STRING; Q8C9X6; -.
DR   PhosphoSite; Q8C9X6; -.
DR   PRIDE; Q8C9X6; -.
DR   Ensembl; ENSMUST00000028100; ENSMUSP00000028100; ENSMUSG00000024240.
DR   Ensembl; ENSMUST00000115870; ENSMUSP00000111536; ENSMUSG00000024240.
DR   GeneID; 13831; -.
DR   KEGG; mmu:13831; -.
DR   UCSC; uc008dzi.1; mouse.
DR   UCSC; uc008dzj.1; mouse.
DR   CTD; 13831; -.
DR   MGI; MGI:1278322; Epc1.
DR   GeneTree; ENSGT00390000013262; -.
DR   HOGENOM; HBG355238; -.
DR   HOVERGEN; HBG051489; -.
DR   InParanoid; Q8C9X6; -.
DR   OMA; ENHESEK; -.
DR   OrthoDB; EOG4HMJ90; -.
DR   NextBio; 284644; -.
DR   ArrayExpress; Q8C9X6; -.
DR   Bgee; Q8C9X6; -.
DR   CleanEx; MM_EPC1; -.
DR   Genevestigator; Q8C9X6; -.
DR   GermOnline; ENSMUSG00000024240; Mus musculus.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
DR   GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR   GO; GO:0040008; P:regulation of growth; 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   Acetylation; Activator; Alternative splicing; Chromatin regulator;
KW   Growth regulation; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    813       Enhancer of polycomb homolog 1.
FT                                /FTId=PRO_0000214154.
FT   MOD_RES     356    356       Phosphoserine (By similarity).
FT   MOD_RES     511    511       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1     51       MSKLSFRARALDASKPLPVFRCEDLPDLHEYASINRAVPQM
FT                                PTGMEKEEES -> M (in isoform 2).
FT                                /FTId=VSP_012878.
SQ   SEQUENCE   813 AA;  90411 MW;  E6F3CD987FC55905 CRC64;
     MSKLSFRARA LDASKPLPVF RCEDLPDLHE YASINRAVPQ MPTGMEKEEE SEHHLQRAIS
     AQQVYGEKRD NMVIPVPEAE SNIAYYESIY PGEFRMPKQL IHIQPFSLDA EQPDYDLDSE
     DEVFVNKLKK KMDICPLQFE EMIDRLEKGS GQQPVSLQEA KLLLKEDDEL IREVYEYWIK
     KRKTCRGSSL IPLVKQEKRD GSSTNDPYVA FRRRTEKMQT RKNRKNDEAS YEKMLKLRRD
     LSRAVTILEM IKRREKSKRE LLHLTLEIME KRYNLGDYSG EIMSEVMAQR QPVKPTYAIP
     IIPITNSSQF KHQDATDSKE FKVNKQDKAD LIRPKRKYEK KPKVLPPSAA APQQQSPAAL
     PGFSAKDLNQ YDFPSSDEEP LSQVLSGSSE AEEENDPDGP FAFRRKAGCQ YYAPHLDQTG
     NWPWTSPKDG GLGDVRYRYC LTTLTVPQRC LGFARRRVGR GGRVVLDRAH SDYDSMFHHL
     DLDMLSSPQP SPVNQFANTS EPNTSDRSSS KDLSQILVDI KSCRWRHFRP RTPSLPDSDS
     GELSSRKLHR SISRAGAAQP GAHTCSTSTQ NRSSSGSAHC AFTAEQYQQH QQQLALMQQQ
     QLAQTQQQQQ ANSSSSAAAQ QGFVSKTLDS ASAQFAASAL MTSEQLLGFK VKDDVVLGLG
     VNGVLPASGV YKGLHLSSTT PTALVHTSPS TAGSTLLQPS NITQTSGSHS SLSHQVTAAS
     SATTQVLFGN NIRLTVPSSV PTVNSVTPIN ARHIPRTLSA VPPSALKLAA AANCQVSKVP
     SSSSVDSVPR ENHESEKPAL NNIADNTVAM EVT
//
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;
CC   -----------------------------------------------------------------------
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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   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;
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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   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;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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   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.
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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   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.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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;
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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   ASPP2_MOUSE             Reviewed;        1128 AA.
AC   Q8CG79; Q3UYM7; Q8K2L5;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Apoptosis-stimulating of p53 protein 2;
DE   AltName: Full=Tumor suppressor p53-binding protein 2;
DE            Short=53BP2;
DE            Short=p53-binding protein 2;
DE            Short=p53BP2;
GN   Name=Tp53bp2; Synonyms=Aspp2, Trp53bp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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; 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 270-1128.
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., 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-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: Regulator that plays a central role in regulation of
CC       apoptosis and cell growth via its interactions. Regulates p53/TP53
CC       by enhancing the DNA binding and transactivation function of
CC       p53/TP53 on the promoters of proapoptotic genes in vivo. Inhibits
CC       the ability of APPBP1 to conjugate NEDD8 to CUL1, and thereby
CC       decreases APPBP1 ability to induce apoptosis. Impedes cell cycle
CC       progression at G2/M. Its apoptosis-stimulating activity is
CC       inhibited by its interaction with DDX42 (By similarity).
CC   -!- SUBUNIT: Binds to the central domain of p53/TP53 as well as to
CC       BCL2. Interacts with protein phosphatase 1. Interacts with RELA
CC       NF-kappa-B subunit. This interaction probably prevents the
CC       activation of apoptosis, possibly by preventing its interaction
CC       with p53/TP53. Interacts with APC2 and APPBP1. Interacts with
CC       DDX42 (via the C-terminus); the interaction is not inhibited by
CC       TP53BP2 ubiquitination and is independent of p53/TP53 (By
CC       similarity).
CC   -!- INTERACTION:
CC       P35569:Irs1; NbExp=1; IntAct=EBI-645416, EBI-400825;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region (By
CC       similarity). Nucleus (By similarity). Note=Predominantly found in
CC       the perinuclear region (By similarity). Some small fraction is
CC       nuclear (By similarity).
CC   -!- DOMAIN: The ankyrin repeats and the SH3 domain are required for a
CC       specific interactions with p53/TP53 (By similarity).
CC   -!- SIMILARITY: Belongs to the ASPP family.
CC   -!- SIMILARITY: Contains 2 ANK repeats.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BC042874; Type=Frameshift; Positions=23;
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DR   EMBL; AC131742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC030894; AAH30894.1; -; mRNA.
DR   EMBL; BC042874; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; CB248714; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK134556; BAE22185.1; -; mRNA.
DR   IPI; IPI00229434; -.
DR   RefSeq; NP_775554.2; NM_173378.2.
DR   UniGene; Mm.287450; -.
DR   ProteinModelPortal; Q8CG79; -.
DR   SMR; Q8CG79; 1-83, 926-1118.
DR   IntAct; Q8CG79; 2.
DR   STRING; Q8CG79; -.
DR   PhosphoSite; Q8CG79; -.
DR   PRIDE; Q8CG79; -.
DR   Ensembl; ENSMUST00000027791; ENSMUSP00000027791; ENSMUSG00000026510.
DR   Ensembl; ENSMUST00000117245; ENSMUSP00000112508; ENSMUSG00000026510.
DR   GeneID; 209456; -.
DR   KEGG; mmu:209456; -.
DR   UCSC; uc007dyc.1; mouse.
DR   CTD; 209456; -.
DR   MGI; MGI:2138319; Trp53bp2.
DR   eggNOG; roNOG11750; -.
DR   GeneTree; ENSGT00600000084381; -.
DR   HOGENOM; HBG443981; -.
DR   HOVERGEN; HBG050596; -.
DR   InParanoid; Q8CG79; -.
DR   OMA; GSERIAH; -.
DR   OrthoDB; EOG4KH2T7; -.
DR   NextBio; 372677; -.
DR   ArrayExpress; Q8CG79; -.
DR   Bgee; Q8CG79; -.
DR   Genevestigator; Q8CG79; -.
DR   GermOnline; ENSMUSG00000026510; 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:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0007417; P:central nervous system development; IMP:MGI.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0006917; P:induction of apoptosis; ISS:UniProtKB.
DR   GO; GO:0010212; P:response to ionizing radiation; IMP:MGI.
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   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; Cell cycle; Cytoplasm; Nucleus; Phosphoprotein;
KW   Repeat; SH3 domain; SH3-binding.
FT   CHAIN         1   1128       Apoptosis-stimulating of p53 protein 2.
FT                                /FTId=PRO_0000066965.
FT   REPEAT      958    987       ANK 1.
FT   REPEAT      991   1020       ANK 2.
FT   DOMAIN     1057   1119       SH3.
FT   REGION      332    348       Interaction with APPBP1 (By similarity).
FT   REGION      876   1128       Mediates interaction with APC2 (By
FT                                similarity).
FT   MOTIF       866    875       SH3-binding (Potential).
FT   COMPBIAS     92    133       Gln-rich.
FT   COMPBIAS    132    173       Gln-rich.
FT   MOD_RES     479    479       Phosphoserine.
FT   MOD_RES     555    555       Phosphoserine (By similarity).
FT   MOD_RES     568    568       Phosphoserine (By similarity).
FT   MOD_RES     697    697       Phosphoserine.
FT   CONFLICT    270    270       L -> V (in Ref. 3; BAE22185).
FT   CONFLICT    367    382       VKPALPDGSLLMQSAE -> DAWVAHASAHASAHAS (in
FT                                Ref. 2; AAH30894).
SQ   SEQUENCE   1128 AA;  125301 MW;  C5FF5D37D73187A0 CRC64;
     MMPMFLTVYL SNSEQHFTEV PVTPETICRD VVDLCKEPGE NDCHLAEVWC GSERPVADNE
     RMFDVLQRFG SQRNEVRFFL RHERPPNRDI VSGPRSQDPS VKRNGVKVPG EHRRKENGVN
     SPRLDLTLAE LQEMASRQQQ QIEAQQQMLA TKEQRLKFLK QQDQRQQQQA AEQEKLKRLR
     EIAESQEAKL KKVRALKGHV EQKRLSNGKL VEEIEQMNSL FQQKQRELVL AVSKVEELTR
     QLEMLKNGRI DGHHDNQSAV AELDRLYKEL QLRNKLNQEQ NAKLQQQREC LNKRNSEVAV
     MDKRVSELRD RLWKKKAALQ QKENLPVSPD GNLPQQAVSA PSRVAAVGPY IQSSTMPRMP
     SRPELLVKPA LPDGSLLMQS AEGPMKIQTL PNMRSGAASQ SKGSKAHPAS PDWNPSNADL
     LPSQGSSVPQ SAGTALDQVD DGEIAVREKE KKVRPFSMFD TVDQCAAPPS FGTLRKNQSS
     EDILRDAQAV NKNVAKVPPP VPTKPKQIHL PYFGQTAQSP SDMKPDGNAQ QLPIAATSVG
     AKLKPAGPQA RMLLSPGAPS GGQDQVLSPA SKQESPPAAA VRPFTPQPSK DTFPPAFRKP
     QTVAASSIYS MYTQQQAPGK NFQQAVQSAL TKTQPRGPHF SSVYGKPVIA AAQNPQQHPE
     NIYSCSQGKP GSPEPETETV SSVHESHENE RIPRPLSPTK LLPFLSNPYR NQSDADLEAL
     RKKLSNAPRP LKKRSSITEP EGPNGPNIQK LLYQRTTIAA METISVPSHP SKSPGSVTVN
     PESSVEIPNP YLHVEPEKEV GSLVPEPLSP EDMGSASTEN SDVPAPSAGL EYVSEGVTDS
     STNLQNNVEE TNPEAPHLLE VYLEEYPPYP PPPYPSGEPE VSEEDSARMR PPEITGQVSL
     PPGKRTNLRK TGSERIAHGM RVKFNPLALL LDSSLEGEFD LVQRIIYEVD DPSLPNDEGI
     TALHNAVCAG HTEIVKFLVQ FGVNVNAADS DGWTPLHCAA SCNNVQVCKF LVESGAAVFA
     MTYSDMQTAA DKCEEMEEGY TQCSQFLYGV QEKMGIMNKG VIYALWDYEP QHDDELLMKE
     GDCMTVIRRE DEEEIEWWWA RLNDKEGYVP RNLLGLYPRI KPRQRSLA
//
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   OGT1_MOUSE              Reviewed;        1046 AA.
AC   Q8CGY8; A2ALY1; Q6PG10; Q8BXH6; Q91Y38;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit;
DE            EC=2.4.1.-;
DE   AltName: Full=O-GlcNAc transferase subunit p110;
DE   AltName: Full=O-linked N-acetylglucosamine transferase 110 kDa subunit;
GN   Name=Ogt;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; 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;
RX   MEDLINE=22392505; PubMed=12504895; DOI=10.1016/S0003-9861(02)00578-7;
RA   Hanover J.A., Yu S., Lubas W.B., Shin S.H., Ragano-Caracciola M.,
RA   Kochran J., Love D.C.;
RT   "Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc
RT   transferase encoded by a single mammalian gene.";
RL   Arch. Biochem. Biophys. 409:287-297(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Skeletal muscle;
RA   Rumberger J.M., Wu T., Hering M.A., Marshall S.;
RT   "Molecular cloning of the mouse O-GlcNAc transferase.";
RL   Submitted (MAR-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] (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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 894-1046 (ISOFORMS 1/2).
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   [6]
RP   PROTEIN SEQUENCE OF 217-236 AND 421-440, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [7]
RP   INTERACTION WITH ATXN10.
RX   PubMed=16182253; DOI=10.1016/j.bbrc.2005.09.026;
RA   Andrali S.S., Maerz P., Ozcan S.;
RT   "Ataxin-10 interacts with O-GlcNAc transferase OGT in pancreatic beta
RT   cells.";
RL   Biochem. Biophys. Res. Commun. 337:149-153(2005).
CC   -!- FUNCTION: Addition of nucleotide-activated sugars directly onto
CC       the polypeptide through O-glycosidic linkage with the hydroxyl of
CC       serine or threonine. Mediates the O-glycosylation of MLL5 (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: UDP-N-acetyl-D-glucosamine + peptide = UDP +
CC       N-acetyl-beta-D-glucosaminyl-peptide.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBUNIT: Heterotrimer of two 110 kDa and one 70 kDa subunits. It
CC       is not known if the 70 kDa subunit is encoded by a separate gene
CC       or is the product of either of a proteolytic degradation or an
CC       alternative initiation of the 110 kDa subunit (By similarity).
CC       Component of the MLL5-L complex, at least composed of MLL5, STK38,
CC       PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with HCFC1
CC       (By similarity). Interacts with ATXN10.
CC   -!- INTERACTION:
CC       Q6B828:- (xeno); NbExp=1; IntAct=EBI-928496, EBI-909258;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CGY8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CGY8-2; Sequence=VSP_024844;
CC   -!- SIMILARITY: Belongs to the O-GlcNAc transferase family.
CC   -!- SIMILARITY: Contains 13 TPR repeats.
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DR   EMBL; AF539527; AAO17363.1; -; Genomic_DNA.
DR   EMBL; AF363030; AAK39123.1; -; mRNA.
DR   EMBL; AL806534; CAM21281.1; -; Genomic_DNA.
DR   EMBL; AL805980; CAM21281.1; JOINED; Genomic_DNA.
DR   EMBL; AL806534; CAM21282.1; -; Genomic_DNA.
DR   EMBL; AL805980; CAM21282.1; JOINED; Genomic_DNA.
DR   EMBL; AL805980; CAM25748.1; -; Genomic_DNA.
DR   EMBL; AL806534; CAM25748.1; JOINED; Genomic_DNA.
DR   EMBL; AL805980; CAM25749.1; -; Genomic_DNA.
DR   EMBL; AL806534; CAM25749.1; JOINED; Genomic_DNA.
DR   EMBL; BC057319; AAH57319.1; -; mRNA.
DR   EMBL; AK047095; BAC32961.1; -; mRNA.
DR   IPI; IPI00420870; -.
DR   IPI; IPI00845528; -.
DR   RefSeq; NP_631883.2; NM_139144.3.
DR   UniGene; Mm.259191; -.
DR   HSSP; O15294; 1W3B.
DR   ProteinModelPortal; Q8CGY8; -.
DR   SMR; Q8CGY8; 23-1030.
DR   IntAct; Q8CGY8; 1.
DR   STRING; Q8CGY8; -.
DR   CAZy; GT41; Glycosyltransferase Family 41.
DR   PRIDE; Q8CGY8; -.
DR   Ensembl; ENSMUST00000044475; ENSMUSP00000045409; ENSMUSG00000034160.
DR   GeneID; 108155; -.
DR   KEGG; mmu:108155; -.
DR   NMPDR; fig|10090.3.peg.21960; -.
DR   CTD; 108155; -.
DR   MGI; MGI:1339639; Ogt.
DR   eggNOG; roNOG07233; -.
DR   GeneTree; ENSGT00550000074327; -.
DR   HOGENOM; HBG317910; -.
DR   HOVERGEN; HBG000351; -.
DR   InParanoid; Q8CGY8; -.
DR   OMA; NEIFALR; -.
DR   OrthoDB; EOG4HQDHJ; -.
DR   PhylomeDB; Q8CGY8; -.
DR   NextBio; 360182; -.
DR   ArrayExpress; Q8CGY8; -.
DR   Bgee; Q8CGY8; -.
DR   Genevestigator; Q8CGY8; -.
DR   GO; GO:0008080; F:N-acetyltransferase activity; TAS:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006493; P:protein O-linked glycosylation; TAS: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; 10.
DR   SMART; SM00028; TPR; 12.
DR   PROSITE; PS50005; TPR; 12.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm;
KW   Direct protein sequencing; Glycosyltransferase; Nucleus;
KW   Phosphoprotein; Repeat; TPR repeat; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1046       UDP-N-acetylglucosamine--peptide N-
FT                                acetylglucosaminyltransferase 110 kDa
FT                                subunit.
FT                                /FTId=PRO_0000285216.
FT   REPEAT       21     54       TPR 1.
FT   REPEAT       89    122       TPR 2.
FT   REPEAT      123    156       TPR 3.
FT   REPEAT      157    190       TPR 4.
FT   REPEAT      191    224       TPR 5.
FT   REPEAT      225    258       TPR 6.
FT   REPEAT      259    292       TPR 7.
FT   REPEAT      293    326       TPR 8.
FT   REPEAT      327    360       TPR 9.
FT   REPEAT      361    394       TPR 10.
FT   REPEAT      395    428       TPR 11.
FT   REPEAT      429    462       TPR 12.
FT   REPEAT      463    473       TPR 13; truncated.
FT   MOTIF       487    503       Nuclear localization signal (Potential).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      20     20       Phosphoserine (By similarity).
FT   VAR_SEQ      13     22       Missing (in isoform 2).
FT                                /FTId=VSP_024844.
FT   CONFLICT     57     57       V -> A (in Ref. 1; AAO17363).
FT   CONFLICT    992    992       K -> R (in Ref. 2; AAK39123).
SQ   SEQUENCE   1046 AA;  116952 MW;  FD5EE12844E00097 CRC64;
     MASSVGNVAD STEPTKRMLS FQGLAELAHR EYQAGDFEAA ERHCMQLWRQ EPDNTGVLLL
     LSSIHFQCRR LDRSAHFSTL AIKQNPLLAE AYSNLGNVYK ERGQLQEAIE HYRHALRLKP
     DFIDGYINLA AALVAAGDME GAVQAYVSAL QYNPDLYCVR SDLGNLLKAL GRLEEAKACY
     LKAIETQPNF AVAWSNLGCV FNAQGEIWLA IHHFEKAVTL DPNFLDAYIN LGNVLKEARI
     FDRAVAAYLR ALSLSPNHAV VHGNLACVYY EQGLIDLAID TYRRAIELQP HFPDAYCNLA
     NALKEKGSVA EAEDCYNTAL RLCPTHADSL NNLANIKREQ GNIEEAVRLY RKALEVFPEF
     AAAHSNLASV LQQQGKLQEA LMHYKEAIRI SPTFADAYSN MGNTLKEMQD VQGALQCYTR
     AIQINPAFAD AHSNLASIHK DSGNIPEAIA SYRTALKLKP DFPDAYCNLA HCLQIVCDWT
     DYDERMKKLV SIVAEQLEKN RLPSVHPHHS MLYPLSHGFR KAIAERHGNL CLDKINVLHK
     PPYEHPKDLK LSDGRLRVGY VSSDFGNHPT SHLMQSIPGM HNPDKFEVFC YALSPDDGTN
     FRVKVMAEAN HFIDLSQIPC NGKAADRIHQ DGIHILVNMN GYTKGARNEL FALRPAPIQA
     MWLGYPGTSG ALFMDYIITD QETSPAEVAE QYSEKLAYMP HTFFIGDHAN MFPHLKKKAV
     IDFKSNGHIY DNRIVLNGID LKAFLDSLPD VKIVKMKCPD GGDNPDSSNT ALNMPVIPMN
     TIAEAVIEMI NRGQIQITIN GFSISNGLAT TQINNKAATG EEVPRTIIVT TRSQYGLPED
     AIVYCNFNQL YKIDPSTLQM WANILKRVPN SVLWLLRFPA VGEPNIQQYA QNMGLPQNRI
     IFSPVAPKEE HVRRGQLADV CLDTPLCNGH TTGMDVLWAG TPMVTMPGET LASRVAASQL
     TCLGCLELIA KSRQEYEDIA VKLGTDLEYL KKIRGKVWKQ RISSPLFNTK QYTMELERLY
     LQMWEHYAAG NKPDHMIKPV EVTESA
//
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   SYNJ1_MOUSE             Reviewed;        1574 AA.
AC   Q8CHC4;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 3.
DT   08-FEB-2011, entry version 79.
DE   RecName: Full=Synaptojanin-1;
DE            EC=3.1.3.36;
DE   AltName: Full=Synaptic inositol-1,4,5-trisphosphate 5-phosphatase 1;
GN   Name=Synj1; Synonyms=Kiaa0910;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; 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   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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-784 AND TYR-786, 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-1053; SER-1084 AND
RP   SER-1147, 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-1048; SER-1350 AND
RP   THR-1354, 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: Inositol 5-phosphatase which has a role in clathrin-
CC       mediated endocytosis (By similarity).
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   -!- SUBUNIT: Binds AMPH, SH3GL1, SH3GL2 and SH3GL3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- DOMAIN: Binds to EPS15 (a clathrin coat-associated protein) via a
CC       C-terminal domain containing three Asn-Pro-Phe (NPF) repeats (By
CC       similarity).
CC   -!- DOMAIN: The C-terminal proline-rich region mediates binding to a
CC       variety of SH3 domain-containing proteins including AMPH, SH3GL1,
CC       SH3GL2, SH3GL3 and GRB2.
CC   -!- SIMILARITY: Belongs to the synaptojanin family.
CC   -!- SIMILARITY: In the central section; belongs to the inositol-1,4,5-
CC       trisphosphate 5-phosphatase family.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -!- SIMILARITY: Contains 1 SAC domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC41456.2; Type=Erroneous initiation;
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DR   EMBL; AB093272; BAC41456.2; ALT_INIT; Transcribed_RNA.
DR   IPI; IPI00881540; -.
DR   UniGene; Mm.187079; -.
DR   ProteinModelPortal; Q8CHC4; -.
DR   SMR; Q8CHC4; 54-444, 530-873, 895-971.
DR   MINT; MINT-268854; -.
DR   STRING; Q8CHC4; -.
DR   PhosphoSite; Q8CHC4; -.
DR   PRIDE; Q8CHC4; -.
DR   Ensembl; ENSMUST00000023696; ENSMUSP00000023696; ENSMUSG00000022973.
DR   UCSC; uc007zww.1; mouse.
DR   MGI; MGI:1354961; Synj1.
DR   eggNOG; roNOG05346; -.
DR   GeneTree; ENSGT00600000084387; -.
DR   HOVERGEN; HBG079225; -.
DR   OMA; HSVLKPQ; -.
DR   PhylomeDB; Q8CHC4; -.
DR   BRENDA; 3.1.3.36; 244.
DR   ArrayExpress; Q8CHC4; -.
DR   Bgee; Q8CHC4; -.
DR   CleanEx; MM_SYNJ1; -.
DR   Genevestigator; Q8CHC4; -.
DR   GermOnline; ENSMUSG00000022973; Mus musculus.
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:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Cytoplasm; Endocytosis; Hydrolase; Phosphoprotein; Repeat;
KW   RNA-binding.
FT   CHAIN         1   1574       Synaptojanin-1.
FT                                /FTId=PRO_0000209731.
FT   DOMAIN      119    442       SAC.
FT   DOMAIN      894    971       RRM.
FT   COMPBIAS   1042   1286       Pro-rich.
FT   COMPBIAS   1533   1566       Pro-rich.
FT   MOD_RES     784    784       Phosphotyrosine.
FT   MOD_RES     786    786       Phosphotyrosine.
FT   MOD_RES     830    830       Phosphoserine (By similarity).
FT   MOD_RES    1048   1048       Phosphothreonine.
FT   MOD_RES    1053   1053       Phosphoserine.
FT   MOD_RES    1084   1084       Phosphoserine.
FT   MOD_RES    1147   1147       Phosphoserine.
FT   MOD_RES    1217   1217       Phosphothreonine (By similarity).
FT   MOD_RES    1350   1350       Phosphoserine.
FT   MOD_RES    1354   1354       Phosphothreonine.
FT   MOD_RES    1399   1399       Phosphoserine (By similarity).
SQ   SEQUENCE   1574 AA;  172617 MW;  F791EE3AD6A37B82 CRC64;
     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 QLQQEQPTGQ VKINGISGVK
     QEPTLKSDPF EDLSLSVLAV SKAQPSVQIS PVLTPDPKML IQLPSASQSQ VNPLSSVSCM
     PTRPPGPEES KSQESMGSSA NPFPSLPCRN PFTDRTAAPG NPFRVQSQES EATSWLSKEE
     PVPNSPFPPL MPLSHDTSKA SSSLGGFEDN FDLQSQSTVK TSNPKGWVTF DEDDNFPTTG
     KSKSVCPDLV GNAPASFDDD WSKGASVSFC VLPARRPPPP PPPVPLLPPG TTSSAGPSTT
     LPSKAPSTLD FTER
//
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   PHC3_MOUSE              Reviewed;         981 AA.
AC   Q8CHP6; Q3TLV5;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 61.
DE   RecName: Full=Polyhomeotic-like protein 3;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=22271642; PubMed=12384788; DOI=10.1007/s00439-002-0814-3;
RA   Tonkin E., Hagan D.-M., Li W., Strachan T.;
RT   "Identification and characterisation of novel mammalian homologues of
RT   Drosophila polyhomeotic permits new insights into relationships
RT   between members of the polyhomeotic family.";
RL   Hum. Genet. 111:435-442(2002).
RN   [2]
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; THR-607 AND
RP   SER-614, 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-269; THR-607 AND
RP   SER-614, 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 Polycomb group (PcG) multiprotein PRC1
CC       complex, a complex required to maintain the transcriptionally
CC       repressive state of many genes, including Hox genes, throughout
CC       development. PcG PRC1 complex acts via chromatin remodeling and
CC       modification of histones; it mediates monoubiquitination of
CC       histone H2A 'Lys-119', rendering chromatin heritably changed in
CC       its expressibility (By similarity).
CC   -!- SUBUNIT: Component of chromatin-associated class II polycomb
CC       repressive complex 1 (PRC1/hPRC-H) at least composed of
CC       PCGF2/RNF110, BMI1/PCGF4, CBX2/M33, CBX4/PC2, CBX8/PC3, PHC1,
CC       PHC2, PHC3, SCMH1, RING1 and RNF2/RING2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CHP6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CHP6-2; Sequence=VSP_016772, VSP_016773, VSP_016774,
CC                                  VSP_016775;
CC   -!- TISSUE SPECIFICITY: Ubiquitous expression.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 FCS-type zinc finger.
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; AJ414610; CAC93885.1; -; mRNA.
DR   EMBL; AK166296; BAE38687.1; -; mRNA.
DR   IPI; IPI00652286; -.
DR   IPI; IPI00857563; -.
DR   RefSeq; NP_700470.2; NM_153421.2.
DR   UniGene; Mm.233173; -.
DR   ProteinModelPortal; Q8CHP6; -.
DR   SMR; Q8CHP6; 915-979.
DR   PhosphoSite; Q8CHP6; -.
DR   PRIDE; Q8CHP6; -.
DR   Ensembl; ENSMUST00000046624; ENSMUSP00000037862; ENSMUSG00000037652.
DR   Ensembl; ENSMUST00000099163; ENSMUSP00000096767; ENSMUSG00000037652.
DR   GeneID; 241915; -.
DR   KEGG; mmu:241915; -.
DR   UCSC; uc008ovl.1; mouse.
DR   UCSC; uc008ovr.1; mouse.
DR   CTD; 241915; -.
DR   MGI; MGI:2181434; Phc3.
DR   GeneTree; ENSGT00550000074459; -.
DR   HOGENOM; HBG506159; -.
DR   HOVERGEN; HBG106650; -.
DR   InParanoid; Q8CHP6; -.
DR   NextBio; 385174; -.
DR   ArrayExpress; Q8CHP6; -.
DR   Bgee; Q8CHP6; -.
DR   CleanEx; MM_PHC3; -.
DR   Genevestigator; Q8CHP6; -.
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:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Alternative splicing; Developmental protein; DNA-binding;
KW   Metal-binding; Nucleus; Phosphoprotein; Zinc; Zinc-finger.
FT   CHAIN         1    981       Polyhomeotic-like protein 3.
FT                                /FTId=PRO_0000076291.
FT   DOMAIN      917    981       SAM.
FT   ZN_FING     774    808       FCS-type.
FT   MOTIF       689    718       HD1.
FT   COMPBIAS     18     25       Poly-Thr.
FT   COMPBIAS     31     99       Gln-rich.
FT   COMPBIAS    321    537       Gln-rich.
FT   COMPBIAS    339    615       Pro-rich.
FT   MOD_RES     227    227       Phosphoserine (By similarity).
FT   MOD_RES     231    231       Phosphoserine.
FT   MOD_RES     261    261       Phosphoserine (By similarity).
FT   MOD_RES     269    269       Phosphoserine.
FT   MOD_RES     312    312       Phosphoserine (By similarity).
FT   MOD_RES     607    607       Phosphothreonine.
FT   MOD_RES     612    612       Phosphothreonine (By similarity).
FT   MOD_RES     614    614       Phosphoserine.
FT   MOD_RES     759    759       Phosphoserine (By similarity).
FT   MOD_RES     760    760       Phosphoserine (By similarity).
FT   VAR_SEQ       1      1       M -> MAEAEFKDHSTAM (in isoform 2).
FT                                /FTId=VSP_016772.
FT   VAR_SEQ     178    210       Missing (in isoform 2).
FT                                /FTId=VSP_016773.
FT   VAR_SEQ     720    736       RSSLLIEQPVKKRPLLD -> QKLICVFKIIFSDTTLS
FT                                (in isoform 2).
FT                                /FTId=VSP_016774.
FT   VAR_SEQ     737    981       Missing (in isoform 2).
FT                                /FTId=VSP_016775.
FT   CONFLICT    147    147       I -> S (in Ref. 2; BAE38687).
FT   CONFLICT    384    384       N -> T (in Ref. 2; BAE38687).
FT   CONFLICT    437    437       A -> T (in Ref. 2; BAE38687).
FT   CONFLICT    534    534       V -> G (in Ref. 2; BAE38687).
SQ   SEQUENCE   981 AA;  105439 MW;  CCC3CF42C1EE06B9 CRC64;
     MDSEPSSGTS VSTTASSTTT TTITTSSSRM QQPQISVYSG SDRHAVQVIQ QALHRPPSSA
     AQYLQQMYAA QQQHLMLHTA ALQQQHLSSS QLQSLAAVQA SLSSGRPSTS PTGSVTQQSS
     MSQTSILSAS PAPAQLMNRS QTSSSTIGSI TQQTMLLGST SPTLTASQAQ MYLRAQMLIF
     TPATTVAAVQ SDIPVVSSSP SPSCQSAAAQ VQNLTLRSQK LGVLSSSQNG SPKSAGQTQS
     LTICHNKTTV TSSKISQRDP SPESKKGGSP GLESRSTAVT RTSSIHQLIA PASYSPIQPH
     SLIKHQQIPL HSPPPKVSHH QLLLQQQQQQ IQPITLQSPS QDPPPSQHCI PLPNHGLSPA
     PSNAQPQHCS PVQSHPPPLT VSPNQAQSAQ QSVVVSPPPP HSPSQSPTII IHPQALIQPH
     PLVSSALQTG PNLQQAAADQ VQSTAQLNLP SHLPLPASPV VHIGPVQQSA LVSPGQQMVS
     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 AEEDVAFHED PVPSAMTTRL RRQSERERER ELRDVRIRKM
     PENSDLLPVA QTEPSIWTVD DVWAFIHSLP GCQDVADEFR AQEIDGQALL LLKEDHLMSA
     MNMKLGPALK ICARINSLKD S
//
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   -----------------------------------------------------------------------
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   PDLI5_MOUSE             Reviewed;         591 AA.
AC   Q8CI51; Q9QYN0; Q9QYN1; Q9QYN2;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=PDZ and LIM domain protein 5;
DE   AltName: Full=Enigma homolog;
DE   AltName: Full=Enigma-like PDZ and LIM domains protein;
GN   Name=Pdlim5; Synonyms=Enh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=129/SvJ;
RX   MEDLINE=20294871; PubMed=10833443; DOI=10.1006/bbrc.2000.2787;
RA   Nakagawa N., Hoshijima M., Oyasu M., Saito N., Tanizawa K., Kuroda S.;
RT   "ENH, containing PDZ and LIM domains, heart/skeletal muscle-specific
RT   protein, associates with cytoskeletal proteins through the PDZ
RT   domain.";
RL   Biochem. Biophys. Res. Commun. 272:505-512(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   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).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., 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-228, 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   STRUCTURE BY NMR OF 5-94.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the PDZ domain of enigma homologue protein.";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- FUNCTION: May play an important role in the heart development by
CC       scaffolding PKC to the Z-disk region. Isoform 2 and isoform 3 may
CC       negatively modulate the scaffolding activity of isoform 1. May
CC       play a role in the regulation of cardiomyocyte expansion.
CC       Overexpression promotes the development of heart hypertrophy.
CC       Contributes to the regulation of dendritic spine morphogenesis in
CC       neurons. May restrain postsynaptic growth of excitatory synapses
CC       (By similarity).
CC   -!- SUBUNIT: Interacts with various PKC isoforms through the LIM
CC       domains. Interacts (via LIM domains) with SIPA1L1. Interacts (via
CC       PDZ domain) with actin and ACTN1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane, postsynaptic density (By similarity). Cell junction,
CC       synapse, synaptosome (By similarity). Cytoplasm (By similarity).
CC       Note=Detected both at presynaptic and postsynaptic sites (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=ENH1;
CC         IsoId=Q8CI51-1; Sequence=Displayed;
CC       Name=2; Synonyms=ENH2;
CC         IsoId=Q8CI51-2; Sequence=VSP_010469, VSP_010470;
CC       Name=3; Synonyms=ENH3;
CC         IsoId=Q8CI51-3; Sequence=VSP_010467, VSP_010468, VSP_010469,
CC                                  VSP_010470;
CC   -!- SIMILARITY: Contains 3 LIM zinc-binding domains.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AB016586; BAA88827.1; -; mRNA.
DR   EMBL; AB016587; BAA88828.1; -; mRNA.
DR   EMBL; AB016588; BAA88829.1; -; mRNA.
DR   EMBL; BC037476; AAH37476.1; -; mRNA.
DR   IPI; IPI00415684; -.
DR   IPI; IPI00415685; -.
DR   IPI; IPI00828969; -.
DR   UniGene; Mm.117709; -.
DR   PDB; 1WF7; NMR; -; A=5-94.
DR   PDBsum; 1WF7; -.
DR   ProteinModelPortal; Q8CI51; -.
DR   SMR; Q8CI51; 11-94, 395-589.
DR   STRING; Q8CI51; -.
DR   PhosphoSite; Q8CI51; -.
DR   PRIDE; Q8CI51; -.
DR   Ensembl; ENSMUST00000029941; ENSMUSP00000029941; ENSMUSG00000028273.
DR   Ensembl; ENSMUST00000058626; ENSMUSP00000059267; ENSMUSG00000028273.
DR   Ensembl; ENSMUST00000084039; ENSMUSP00000081052; ENSMUSG00000028273.
DR   UCSC; uc008rom.1; mouse.
DR   UCSC; uc008ron.1; mouse.
DR   MGI; MGI:1927489; Pdlim5.
DR   GeneTree; ENSGT00600000084390; -.
DR   HOGENOM; HBG505271; -.
DR   HOVERGEN; HBG051478; -.
DR   InParanoid; Q8CI51; -.
DR   OrthoDB; EOG4FTW06; -.
DR   ArrayExpress; Q8CI51; -.
DR   Bgee; Q8CI51; -.
DR   CleanEx; MM_PDLIM5; -.
DR   Genevestigator; Q8CI51; -.
DR   GermOnline; ENSMUSG00000028273; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; 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; IEA:UniProtKB-SubCell.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR   GO; GO:0051963; P:regulation of synaptogenesis; ISS:UniProtKB.
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   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cell junction;
KW   Cell membrane; Cytoplasm; LIM domain; Membrane; Metal-binding;
KW   Phosphoprotein; Postsynaptic cell membrane; Repeat; Synapse;
KW   Synaptosome; Zinc.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    591       PDZ and LIM domain protein 5.
FT                                /FTId=PRO_0000075878.
FT   DOMAIN        2     85       PDZ.
FT   DOMAIN      413    472       LIM zinc-binding 1.
FT   DOMAIN      472    531       LIM zinc-binding 2.
FT   DOMAIN      531    591       LIM zinc-binding 3.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES     110    110       Phosphothreonine (By similarity).
FT   MOD_RES     111    111       Phosphoserine (By similarity).
FT   MOD_RES     134    134       Phosphoserine (By similarity).
FT   MOD_RES     136    136       Phosphoserine (By similarity).
FT   MOD_RES     137    137       Phosphoserine (By similarity).
FT   MOD_RES     228    228       Phosphoserine.
FT   MOD_RES     251    251       Phosphotyrosine (By similarity).
FT   MOD_RES     313    313       Phosphoserine (By similarity).
FT   MOD_RES     335    335       Phosphoserine.
FT   VAR_SEQ      98    206       Missing (in isoform 3).
FT                                /FTId=VSP_010467.
FT   VAR_SEQ     237    237       G -> GNPGTVKISPKR (in isoform 3).
FT                                /FTId=VSP_010468.
FT   VAR_SEQ     307    337       NSTQEPSQQPASSGASPLSASEGPESPGSSR -> KEKIPL
FT                                HVFSPKYTKLRDWHHEVSARALNVQ (in isoform 2
FT                                and isoform 3).
FT                                /FTId=VSP_010469.
FT   VAR_SEQ     338    591       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_010470.
FT   CONFLICT     74     74       M -> T (in Ref. 1; BAA88827/BAA88828/
FT                                BAA88829).
FT   CONFLICT     84     84       A -> T (in Ref. 1; BAA88827/BAA88829).
FT   CONFLICT    215    215       E -> D (in Ref. 1; BAA88827/BAA88829).
FT   CONFLICT    222    222       E -> K (in Ref. 1; BAA88827/BAA88829).
FT   CONFLICT    226    226       R -> K (in Ref. 1; BAA88827/BAA88829).
FT   CONFLICT    329    329       G -> R (in Ref. 1; BAA88827).
FT   CONFLICT    433    433       S -> P (in Ref. 1; BAA88827).
FT   CONFLICT    546    546       F -> Y (in Ref. 1; BAA88827).
FT   STRAND        5     12
FT   STRAND       18     21
FT   TURN         22     25
FT   STRAND       26     30
FT   HELIX        38     41
FT   STRAND       49     53
FT   HELIX        63     72
FT   STRAND       74     81
SQ   SEQUENCE   591 AA;  63329 MW;  CC2B9EE1A3DFA32C CRC64;
     MSNYSVSLVG PAPWGFRLQG GKDFNMPLTI SSLKDGGKAS QAHVRIGDVV LSIDGISAQG
     MTHLEAQNKI KACMGSLNMT LQRASAAAKS EPVSVQKGEP KEVVKPVPIT SPAVSKVTST
     TNMAYNKAPR PFGSVSSPKV TSIPSPSSAF TPAHAATSSH ASPTPVAAAT PLHLSASGLH
     VSANLSADQC SSPPNTGKPA VNVPRQPTVT SVCSESAQEL AEGQRRGSQG DIKQQNGPPR
     KHIVERNTEF YHIPTHSDAS KKRLIEDTED WRPRTGTTQS RSFRILAQIT GTEHLTESEN
     DNTKKANSTQ EPSQQPASSG ASPLSASEGP ESPGSSRPSV AGLRSAAAFK PVGSTSVKSP
     SWQRPNQAAP STGRISNNAR SSGTGASVGP PQPSDQDTLV QRAEHIPAGK RTPMCAHCNQ
     VIRGPFLVAL GKSWHPEEFN CAHCKNTMAY IGFVEEKGAL YCELCYEKFF APECGRCQRK
     ILGEVINALK QTWHVSCFVC VACGKPIRNN VFHLEDGEPY CETDYYALFG TICRGCEFPI
     EAGDMFLEAL GYTWHDTCFV CSVCCESLEG QTFFSKKDKP LCKKHAHSVN F
//
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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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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   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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
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   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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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   R4RL1_MOUSE             Reviewed;         445 AA.
AC   Q8K0S5;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Reticulon-4 receptor-like 1;
DE   AltName: Full=Nogo receptor-like 2;
DE   AltName: Full=Nogo-66 receptor homolog 2;
DE   AltName: Full=Nogo-66 receptor-related protein 3;
DE            Short=NgR3;
DE   Flags: Precursor;
GN   Name=Rtn4rl1; Synonyms=Ngrl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=Brain;
RX   PubMed=14664809; DOI=10.1016/S1044-7431(03)00199-4;
RA   Lauren J., Airaksinen M.S., Saarma M., Timmusk T.;
RT   "Two novel mammalian nogo receptor homologs differentially expressed
RT   in the central and peripheral nervous systems.";
RL   Mol. Cell. Neurosci. 24:581-594(2003).
RN   [2]
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   [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=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   IDENTIFICATION.
RX   MEDLINE=22723697; PubMed=12839991; DOI=10.1093/emboj/cdg325;
RA   Barton W.A., Liu B.P., Tzvetkova D., Jeffrey P.D., Fournier A.E.,
RA   Sah D., Cate R., Strittmatter S.M., Nikolov D.B.;
RT   "Structure and axon outgrowth inhibitor binding of the Nogo-66
RT   receptor and related proteins.";
RL   EMBO J. 22:3291-3302(2003).
CC   -!- FUNCTION: May play a role in regulating axonal regeneration and
CC       plasticity in the adult central nervous system (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor
CC       (Potential). Note=Localized to the surface of neurons, including
CC       axons.
CC   -!- DEVELOPMENTAL STAGE: At E13.5, strongly expressed in PNS ganglia
CC       and developing heart, and weakly expressed in brain and spinal
CC       cord. By postnatal day 1, strongly expressed in dorsal root
CC       ganglia and in dorsal and gray matter areas of spinal cord.
CC       Expressed in various adult brain structures including the
CC       amygdala, caudate putamen, cerebellum, cerebral cortex,
CC       hippocampus, olfactory bulb and thalamus.
CC   -!- SIMILARITY: Belongs to the Nogo receptor family.
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; AY250218; AAP82835.1; -; mRNA.
DR   EMBL; AK033286; BAC28223.1; -; mRNA.
DR   EMBL; AK140456; BAE24396.1; -; mRNA.
DR   EMBL; AL603905; CAI35092.1; -; Genomic_DNA.
DR   EMBL; BC030471; AAH30471.1; -; mRNA.
DR   EMBL; BK001304; DAA01387.1; -; mRNA.
DR   IPI; IPI00169628; -.
DR   RefSeq; NP_808376.1; NM_177708.5.
DR   UniGene; Mm.82661; -.
DR   ProteinModelPortal; Q8K0S5; -.
DR   SMR; Q8K0S5; 25-343.
DR   STRING; Q8K0S5; -.
DR   PRIDE; Q8K0S5; -.
DR   Ensembl; ENSMUST00000102514; ENSMUSP00000099572; ENSMUSG00000045287.
DR   GeneID; 237847; -.
DR   KEGG; mmu:237847; -.
DR   UCSC; uc007kdh.1; mouse.
DR   CTD; 237847; -.
DR   MGI; MGI:2661375; Rtn4rl1.
DR   eggNOG; roNOG09059; -.
DR   GeneTree; ENSGT00600000084136; -.
DR   HOGENOM; HBG715367; -.
DR   HOVERGEN; HBG063707; -.
DR   InParanoid; Q8K0S5; -.
DR   OMA; WDCGCRA; -.
DR   OrthoDB; EOG4FXR7G; -.
DR   NextBio; 383518; -.
DR   ArrayExpress; Q8K0S5; -.
DR   Bgee; Q8K0S5; -.
DR   CleanEx; MM_RTN4RL1; -.
DR   Genevestigator; Q8K0S5; -.
DR   GermOnline; ENSMUSG00000045287; Mus musculus.
DR   GO; GO:0046658; C:anchored to plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004872; F:receptor activity; ISS:UniProtKB.
DR   GO; GO:0031103; P:axon regeneration; TAS:UniProtKB.
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; 1.
DR   SMART; SM00013; LRRNT; 1.
DR   PROSITE; PS51450; LRR; 6.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; GPI-anchor; Leucine-rich repeat;
KW   Lipoprotein; Membrane; Receptor; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25    424       Reticulon-4 receptor-like 1.
FT                                /FTId=PRO_0000046044.
FT   PROPEP      425    445       Removed in mature form (Potential).
FT                                /FTId=PRO_0000046045.
FT   TRANSMEM    424    444       Helical; (Potential).
FT   REPEAT       53     75       LRR 1.
FT   REPEAT       76     98       LRR 2.
FT   REPEAT       99    123       LRR 3.
FT   REPEAT      124    147       LRR 4.
FT   REPEAT      148    171       LRR 5.
FT   REPEAT      173    195       LRR 6.
FT   REPEAT      197    219       LRR 7.
FT   REPEAT      221    243       LRR 8.
FT   LIPID       424    424       GPI-anchor amidated serine (Potential).
SQ   SEQUENCE   445 AA;  49836 MW;  8285A01C1250D18A CRC64;
     MLRKGCCVEL LLLLLAGELP LGGGCPRDCV CYPAPMTVSC QAHNFAAIPE GIPEDSERIF
     LQNNRITFLQ QGHFSPAMVT LWIYSNNITF IAPNTFEGFV HLEELDLGDN RQLRTLAPET
     FQGLVKLHAL YLYKCGLSAL PAGIFGGLHS LQYLYLQDNH IEYLQDDIFV DLVNLSHLFL
     HGNKLWSLGQ GIFRGLVNLD RLLLHENQLQ WVHHKAFHDL HRLTTLFLFN NSLTELQGDC
     LAPLVALEFL RLNGNAWDCG CRARSLWEWL RRFRGSSSAV PCATPELRQG QDLKLLRVED
     FRNCTGPVSP HQIKSHTLTT SDRAARKEHH PSHGASRDKG HPHGHPPGSR SGYKKAGKNC
     TSHRNRNQIS KVSSGKELTE LQDYAPDYQH KFSFDIMPTA RPKRKGKCAR RTPIRAPSGV
     QQASSGTALG APLLAWILGL AVTLR
//
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;
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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   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;
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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   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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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   PAF1_MOUSE              Reviewed;         535 AA.
AC   Q8K2T8; Q3UY97; Q9CS63; Q9JJ99;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=RNA polymerase II-associated factor 1 homolog;
GN   Name=Paf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; 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   NUCLEOTIDEQUENCE [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, 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).
CC   -!- FUNCTION: The mammalian PAF1 complex is a multifunctional complex.
CC       The PAF1 complex interacts with RNA polymerase II and may be
CC       involved in both initiation and elongation, and in histone
CC       methylation and RNA processing (By similarity).
CC   -!- SUBUNIT: Component of the mammalian PAF1 complex, which consists
CC       of, at least, CDC73, PAF1, LEO1 and CTR9. Interacts directly with
CC       POLR2A/RNA polymerase II and CDC73 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Punctuate distribution
CC       throughout the nucleus except in nucleoli and the perinuclear
CC       chromatin (By similarity).
CC   -!- SIMILARITY: Belongs to the PAF1 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB041615; BAA95098.1; -; mRNA.
DR   EMBL; AK017762; BAB30913.1; -; mRNA.
DR   EMBL; AK134857; BAE22315.1; -; mRNA.
DR   EMBL; AK148538; BAE28608.1; -; mRNA.
DR   EMBL; BC029843; AAH29843.1; -; mRNA.
DR   EMBL; BC083337; AAH83337.1; -; mRNA.
DR   IPI; IPI00331654; -.
DR   RefSeq; NP_062331.2; NM_019458.3.
DR   UniGene; Mm.7916; -.
DR   ProteinModelPortal; Q8K2T8; -.
DR   IntAct; Q8K2T8; 3.
DR   STRING; Q8K2T8; -.
DR   PhosphoSite; Q8K2T8; -.
DR   PRIDE; Q8K2T8; -.
DR   Ensembl; ENSMUST00000003529; ENSMUSP00000003529; ENSMUSG00000003437.
DR   GeneID; 54624; -.
DR   KEGG; mmu:54624; -.
DR   UCSC; uc009fyu.1; mouse.
DR   CTD; 54624; -.
DR   MGI; MGI:1923988; Paf1.
DR   eggNOG; roNOG08987; -.
DR   GeneTree; ENSGT00390000001474; -.
DR   HOGENOM; HBG320593; -.
DR   HOVERGEN; HBG053131; -.
DR   InParanoid; Q8K2T8; -.
DR   OMA; DRDSQIS; -.
DR   OrthoDB; EOG46HG9T; -.
DR   NextBio; 311440; -.
DR   ArrayExpress; Q8K2T8; -.
DR   Bgee; Q8K2T8; -.
DR   Genevestigator; Q8K2T8; -.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007133; RNA_pol_II-assoc_Paf1.
DR   PANTHER; PTHR23188; Paf1; 1.
DR   Pfam; PF03985; Paf1; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    535       RNA polymerase II-associated factor 1
FT                                homolog.
FT                                /FTId=PRO_0000326401.
FT   COILED      352    400       Potential.
FT   COMPBIAS    358    452       Glu-rich.
FT   COMPBIAS    478    534       Ser-rich.
FT   MOD_RES     456    456       Phosphoserine (By similarity).
FT   MOD_RES     460    460       Phosphoserine (By similarity).
FT   MOD_RES     466    466       Phosphoserine (By similarity).
FT   CONFLICT    227    227       P -> L (in Ref. 1; BAA95098).
FT   CONFLICT    336    336       R -> Q (in Ref. 1; BAE22315).
FT   CONFLICT    505    505       Missing (in Ref. 1; BAE22315).
SQ   SEQUENCE   535 AA;  60518 MW;  7A5EAB1284988070 CRC64;
     MAPTIQTQAQ REDGHRPNSH RTLPERSGVV CRVKYCNSLP DIPFDPKFIT YPFDQNRFVQ
     YKATSLEKQH KHDLLTEPDL GVTIDLINPD TYRIDPNVLL DPADEKLLEE EIQAPTSSKR
     SQQHAKVVPW MRKTEYISTE FNRYGISNEK PEVKIGVSVK QQFTEEEIYK DRDSQITAIE
     KTFEDAQKSI SQHYSKPRVT PVEVMPVFPD FKMWINPCAQ VIFDSDPAPK DTSGAAALEM
     MSQAMIRGMM DEEGNQFVAY FLPVEETLKK RKRDQEEEMD YAPDDVYDYK IAREYNWNVK
     NKASKGYEEN YFFIFREGDG VYYNELETRV RLSKRRAKAG VQSGTNALLV VKHRDMNEKE
     LEAQEARKAQ LENHEPEEEE EEEMEAEEKE AGGSDEEQEK GSSSEKEGSE DEHSGSESDR
     EEGDRDEASD KSGSGEDESS EDEARAARDK EEIFGSDADS EDDADSDDED RGQAHRGSDN
     DSDSGSDGGG QRSRSQSRSR SRSASPFPSG SEHSAQEDGS EAAASDSSEA DSDSD
//
ID   TXD11_MOUSE             Reviewed;         948 AA.
AC   Q8K2W3; Q8BMR8; Q8VCK9;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Thioredoxin domain-containing protein 11;
GN   Name=Txndc11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; 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=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=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 act as a redox regulator involved in DUOX proteins
CC       folding. The interaction with DUOX1 and DUOX2 suggest that it
CC       belongs to a multiprotein complex constituting the thyroid
CC       H(2)O(2) generating system. It is however not sufficient to assist
CC       DUOX1 and DUOX2 in H(2)O(2) generation (By similarity).
CC   -!- SUBUNIT: Interacts with the cytoplasmic part of DUOX1 and DUOX2.
CC       Interacts with TPO and CYBA (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=Q8K2W3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K2W3-2; Sequence=VSP_014338, VSP_014339;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC   -!- SIMILARITY: Contains 2 thioredoxin domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH19564.1; Type=Erroneous initiation;
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DR   EMBL; AK029166; BAC26333.1; -; mRNA.
DR   EMBL; BC019564; AAH19564.1; ALT_INIT; mRNA.
DR   EMBL; BC029643; AAH29643.1; -; mRNA.
DR   IPI; IPI00170006; -.
DR   IPI; IPI00468313; -.
DR   RefSeq; NP_083858.1; NM_029582.2.
DR   RefSeq; NP_598866.1; NM_134105.2.
DR   UniGene; Mm.291015; -.
DR   ProteinModelPortal; Q8K2W3; -.
DR   SMR; Q8K2W3; 91-279, 661-770.
DR   STRING; Q8K2W3; -.
DR   PhosphoSite; Q8K2W3; -.
DR   PRIDE; Q8K2W3; -.
DR   Ensembl; ENSMUST00000038424; ENSMUSP00000041113; ENSMUSG00000022498.
DR   Ensembl; ENSMUST00000115818; ENSMUSP00000111485; ENSMUSG00000022498.
DR   GeneID; 106200; -.
DR   KEGG; mmu:106200; -.
DR   UCSC; uc007yet.1; mouse.
DR   UCSC; uc007yew.1; mouse.
DR   CTD; 106200; -.
DR   MGI; MGI:1923620; Txndc11.
DR   GeneTree; ENSGT00390000016020; -.
DR   HOGENOM; HBG445121; -.
DR   HOVERGEN; HBG082866; -.
DR   InParanoid; Q8K2W3; -.
DR   OMA; VLYSPLK; -.
DR   OrthoDB; EOG4PZJ69; -.
DR   NextBio; 358090; -.
DR   ArrayExpress; Q8K2W3; -.
DR   Bgee; Q8K2W3; -.
DR   CleanEx; MM_TXNDC11; -.
DR   Genevestigator; Q8K2W3; -.
DR   GermOnline; ENSMUSG00000022498; 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   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; 2.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 2.
DR   PROSITE; PS00194; THIOREDOXIN_1; FALSE_NEG.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Disulfide bond;
KW   Endoplasmic reticulum; Membrane; Phosphoprotein; Redox-active center;
KW   Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN         1    948       Thioredoxin domain-containing protein 11.
FT                                /FTId=PRO_0000120174.
FT   TRANSMEM     61     81       Helical; (Potential).
FT   DOMAIN       88    214       Thioredoxin 1.
FT   DOMAIN      618    768       Thioredoxin 2.
FT   COILED      793    874       Potential.
FT   MOD_RES     798    798       Phosphoserine (By similarity).
FT   DISULFID    438    441       Redox-active (By similarity).
FT   DISULFID    688    691       Redox-active (By similarity).
FT   VAR_SEQ     230    236       PGVLGYF -> KQQATQY (in isoform 2).
FT                                /FTId=VSP_014338.
FT   VAR_SEQ     237    948       Missing (in isoform 2).
FT                                /FTId=VSP_014339.
SQ   SEQUENCE   948 AA;  105959 MW;  23AAC6C544919DC1 CRC64;
     MSECGGRGGG GGNNSEDAED EGGGPKGSGS LSPAGAAASL EGRIRRGLRG ASLMARQRPE
     LLCGAVALGC ALLFALKFTC SRAKDVIIPA KPPVSFFSSR SPVLDLFQGQ LDYADHVRQD
     SEVVVLFFYA PWCGQSIAAR AEIEQAASRL SDQVLFVAIN CWWNQGKCRK QKHFFYFPVI
     HLYHRSFGPI EYKGPMSAVY IEKFVRRAMK PLLYIPSQSA LLDFLSSYEP GVLGYFEFSG
     SPQPPGYLTF FTSALHSLKK DYLGTVRFGV ITDKHLARLV SLVHSGSVYL HRHFNTSLVF
     PREVMNFTAE NIYKWASENQ ETLFRWLQPH GGKSLLLNNE LKKGPALFLF IPFDPLAERH
     PLLDEITEVA LEYNNCHGDQ VVERLLQHLR RVEAPVLQSL APELPASLPD TQLMAASPCC
     NTVVLPQGPA LSRTHNVCEL CVNQTVGGTR PSSVSVPQCS FFEMAAALDS FYLKEQTFYH
     VVSGSIECSN FLTSYSPFSY YTACCRTISR GMASFTGSEQ NVLTAPAIEF SSLEKSCEAT
     APSSIPHIEE NRYRFPQVGL TSTAFTGLSC RTNKTLNIYL LDSNLFWLYA ERLGAPSSAP
     VKEFATIVDV KEESHYILDP KQALMKFTLE SFIQNFSVLY SPLKRHLTGS DSAQFPTQHL
     ITEVTTDTFW EVTLRKQDVL LLYYTQWCGF CPSLNHIFIQ LARLLPEDTF TVARIDVSQN
     DLPWEFMVDR LPTVLFFPCN RKDLSVKYPG DLPITLPNLL RFILHHSDAA SAPQDPGISP
     PTQDCVQSKA VLQREHISHV ENAMQKLRSE MSSLRRTQEQ VEGRLLSARR DGHRLLRRQR
     TLEQQHRLLR RHSQKLQALY LKKARELQEL ARASGTPLPE HTWLKILVAT MERELEGQGG
     AKEPAPLGKA RPNHSKSMGT TQLPGDTPPP STTSSTLASE TKHENRTD
//
ID   Q8K303_MOUSE            Unreviewed;       552 AA.
AC   Q8K303;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   08-FEB-2011, entry version 33.
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=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; BC029089; AAH29089.1; -; mRNA.
DR   IPI; IPI00662408; -.
DR   UniGene; Mm.142607; -.
DR   Ensembl; ENSMUST00000160023; ENSMUSP00000125015; ENSMUSG00000026090.
DR   MGI; MGI:1919347; 2010300C02Rik.
DR   GeneTree; ENSGT00530000064039; -.
DR   HOVERGEN; HBG071624; -.
DR   ArrayExpress; Q8K303; -.
DR   Bgee; Q8K303; -.
DR   Genevestigator; Q8K303; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   552 AA;  58855 MW;  75559E069CF147FE CRC64;
     MAPPERDMSP FKGDMAPPKG IMEPPNRDTS LPKGDTPPPE TITDTNLETA SDTERQDQSV
     QKEEELTLVV VPRPEGVGTE SSTAPAPSPP VPKSCLKHKA LVTSGSPAES 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 ILKTETGKQA KVAERAQESV KQGDFVRSKS FLMTPAKPAV
     TQRQGSKLNL KEGLQRGISL SHQNLAAQAA ATTEKELHQL KRASYASTDQ PSWMELARKK
     SQAWSDMPQI IK
//
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   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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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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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   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   ABLM1_MOUSE             Reviewed;         861 AA.
AC   Q8K4G5; Q80U86; Q8BIR9; Q8K4G3; Q8K4G4;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Actin-binding LIM protein 1;
DE            Short=abLIM-1;
DE   AltName: Full=Actin-binding LIM protein family member 1;
GN   Name=Ablim1; Synonyms=Ablim, Kiaa0059;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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   DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RC   STRAIN=C57BL/6;
RX   MEDLINE=97392688; PubMed=9245787; DOI=10.1083/jcb.138.3.575;
RA   Roof D.J., Hayes A., Adamian M., Chishti A.H., Li T.;
RT   "Molecular characterization of abLIM, a novel actin-binding and double
RT   zinc finger protein.";
RL   J. Cell Biol. 138:575-588(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
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 TISSUE SPECIFICITY.
RX   MEDLINE=21094484; PubMed=11163266; DOI=10.1016/S0896-6273(00)00153-7;
RA   Erkman L., Yates P.A., McLaughlin T., McEvilly R.J., Whisenhunt T.,
RA   O'Connell S.M., Krones A.I., Kirby M.A., Rapaport D.H.,
RA   Bermingham J.R. Jr., O'Leary D.D.M., Rosenfeld M.G.;
RT   "A POU domain transcription factor-dependent program regulates axon
RT   pathfinding in the vertebrate visual system.";
RL   Neuron 28:779-792(2000).
RN   [5]
RP   FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND ALTERNATIVE
RP   SPLICING (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6;
RX   MEDLINE=22735641; PubMed=12849746; DOI=10.1016/S0306-4522(03)00263-X;
RA   Lu C., Huang X., Ma H.F., Gooley J.J., Aparacio J., Roof D.J.,
RA   Chen C., Chen D.F., Li T.;
RT   "Normal retinal development and retinofugal projections in mice
RT   lacking the retina-specific variant of actin-binding LIM domain
RT   protein.";
RL   Neuroscience 120:121-131(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475 AND SER-479, 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-475, 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475 AND SER-671, 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 SER-475 AND SER-494, 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 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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-475 AND
RP   SER-502, 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-397; SER-411 AND
RP   SER-496, 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 scaffold protein (By similarity). May play a
CC       role in the development of the retina. Has been suggested to play
CC       a role in axon guidance.
CC   -!- SUBUNIT: Binds F-actin. Interacts with ABRA (By similarity).
CC   -!- INTERACTION:
CC       Q62108:Dlg4; NbExp=1; IntAct=EBI-2307994, EBI-300895;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Note=In
CC       a striped pattern along the myofibril axis in cardiac myocytes.
CC       Associated with the cytoskeleton.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1; Synonyms=AbLIM-L;
CC         IsoId=Q8K4G5-1; Sequence=Displayed;
CC       Name=2; Synonyms=AbLIM-M;
CC         IsoId=Q8K4G5-2; Sequence=VSP_012104, VSP_012108, VSP_012110;
CC       Name=3; Synonyms=AbLIM-S;
CC         IsoId=Q8K4G5-3; Sequence=VSP_012103;
CC       Name=4;
CC         IsoId=Q8K4G5-4; Sequence=VSP_012104, VSP_012108, VSP_012110,
CC                                  VSP_012111;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q8K4G5-5; Sequence=VSP_012105, VSP_012106, VSP_012107,
CC                                  VSP_012109;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is detected in adult retina, where
CC       it is highly expressed in the ganglion layer. Detected in rod
CC       inner segment. Isoform 2 is highly expressed in adult retina,
CC       brain, kidney and heart. Isoform 3 is highly expressed in adult
CC       retina, brain, kidney, liver, skeletal muscle, spleen and heart.
CC       Detected in embryonic retina, brain, spinal cord, peripheral
CC       sensory ganglia and thymus.
CC   -!- DEVELOPMENTAL STAGE: Isoform 1 is detected at low levels starting
CC       from E12 and remains constant until birth. After this levels
CC       increase strongly and expression remains high in adults. Isoform 2
CC       and isoform 3 are expressed at a constant high level throughout
CC       development.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- MISCELLANEOUS: Isoform 1 is not necessary for normal axon
CC       guidance.
CC   -!- SIMILARITY: Contains 1 HP (headpiece) domain.
CC   -!- SIMILARITY: Contains 4 LIM zinc-binding domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65478.1; Type=Erroneous initiation;
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DR   EMBL; AF404774; AAM73705.1; -; mRNA.
DR   EMBL; AF404775; AAM73706.1; -; mRNA.
DR   EMBL; AF404776; AAM73707.1; -; mRNA.
DR   EMBL; AK122196; BAC65478.1; ALT_INIT; mRNA.
DR   EMBL; AK029371; BAC26424.1; -; mRNA.
DR   IPI; IPI00356147; -.
DR   IPI; IPI00403221; -.
DR   IPI; IPI00463138; -.
DR   IPI; IPI00467530; -.
DR   IPI; IPI00480399; -.
DR   RefSeq; NP_001096647.1; NM_001103177.1.
DR   RefSeq; NP_001096648.1; NM_001103178.1.
DR   RefSeq; NP_848803.3; NM_178688.3.
DR   UniGene; Mm.217161; -.
DR   UniGene; Mm.446592; -.
DR   ProteinModelPortal; Q8K4G5; -.
DR   SMR; Q8K4G5; 62-344, 793-861.
DR   IntAct; Q8K4G5; 4.
DR   STRING; Q8K4G5; -.
DR   PhosphoSite; Q8K4G5; -.
DR   PRIDE; Q8K4G5; -.
DR   Ensembl; ENSMUST00000079360; ENSMUSP00000078336; ENSMUSG00000025085.
DR   GeneID; 226251; -.
DR   KEGG; mmu:226251; -.
DR   UCSC; uc008hzr.2; mouse.
DR   UCSC; uc008hzs.2; mouse.
DR   UCSC; uc008hzt.2; mouse.
DR   UCSC; uc008hzz.1; mouse.
DR   UCSC; uc009vbz.1; mouse.
DR   CTD; 226251; -.
DR   MGI; MGI:1194500; Ablim1.
DR   HOGENOM; HBG443863; -.
DR   HOVERGEN; HBG031499; -.
DR   InParanoid; Q8K4G5; -.
DR   NextBio; 378072; -.
DR   ArrayExpress; Q8K4G5; -.
DR   Bgee; Q8K4G5; -.
DR   CleanEx; MM_ABLIM1; -.
DR   Genevestigator; Q8K4G5; -.
DR   GermOnline; ENSMUSG00000025085; 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; 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   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Coiled coil; Cytoplasm;
KW   Cytoskeleton; LIM domain; Metal-binding; Phosphoprotein; Repeat; Zinc.
FT   CHAIN         1    861       Actin-binding LIM protein 1.
FT                                /FTId=PRO_0000075698.
FT   DOMAIN       97    156       LIM zinc-binding 1.
FT   DOMAIN      156    216       LIM zinc-binding 2.
FT   DOMAIN      224    283       LIM zinc-binding 3.
FT   DOMAIN      283    343       LIM zinc-binding 4.
FT   DOMAIN      793    861       HP.
FT   COILED      673    723       Potential.
FT   MOD_RES     216    216       Phosphoserine.
FT   MOD_RES     397    397       Phosphoserine.
FT   MOD_RES     401    401       Phosphotyrosine (By similarity).
FT   MOD_RES     411    411       Phosphoserine.
FT   MOD_RES     417    417       Phosphotyrosine (By similarity).
FT   MOD_RES     440    440       Phosphotyrosine.
FT   MOD_RES     450    450       Phosphotyrosine (By similarity).
FT   MOD_RES     454    454       Phosphotyrosine (By similarity).
FT   MOD_RES     470    470       Phosphoserine (By similarity).
FT   MOD_RES     473    473       Phosphothreonine (By similarity).
FT   MOD_RES     475    475       Phosphoserine.
FT   MOD_RES     477    477       Phosphothreonine (By similarity).
FT   MOD_RES     479    479       Phosphoserine.
FT   MOD_RES     483    483       Phosphotyrosine (By similarity).
FT   MOD_RES     494    494       Phosphoserine.
FT   MOD_RES     495    495       Phosphothreonine (By similarity).
FT   MOD_RES     496    496       Phosphoserine.
FT   MOD_RES     499    499       Phosphoserine (By similarity).
FT   MOD_RES     502    502       Phosphoserine.
FT   MOD_RES     505    505       Phosphotyrosine (By similarity).
FT   MOD_RES     517    517       Phosphoserine (By similarity).
FT   MOD_RES     671    671       Phosphoserine.
FT   MOD_RES     723    723       Phosphoserine (By similarity).
FT   MOD_RES     738    738       Phosphoserine (By similarity).
FT   MOD_RES     789    789       Phosphoserine (By similarity).
FT   VAR_SEQ       1    316       Missing (in isoform 3).
FT                                /FTId=VSP_012103.
FT   VAR_SEQ       1     81       MPSLLGLKCLGKLCSSEIGKVPSPERASLRNSHRRLLIEDL
FT                                SVPETPDPAHRRRGTVIHLVYLYSAGCGPPELRFSSYDPS
FT                                -> MVKEK (in isoform 2 and isoform 4).
FT                                /FTId=VSP_012104.
FT   VAR_SEQ       1     77       Missing (in isoform 5).
FT                                /FTId=VSP_012105.
FT   VAR_SEQ      78     81       YDPS -> MSTR (in isoform 5).
FT                                /FTId=VSP_012106.
FT   VAR_SEQ     301    345       DKHYHPSCARCSRCNQMFTEGEEMYLQGSTVWHPDCKQSTK
FT                                TEEK -> VTEASRTWSHIDLRWQGRSEELRAWRHSIQSLR
FT                                HQSAREWFALSA (in isoform 5).
FT                                /FTId=VSP_012107.
FT   VAR_SEQ     346    861       Missing (in isoform 5).
FT                                /FTId=VSP_012109.
FT   VAR_SEQ     348    391       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_012108.
FT   VAR_SEQ     525    564       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_012110.
FT   VAR_SEQ     616    662       Missing (in isoform 4).
FT                                /FTId=VSP_012111.
SQ   SEQUENCE   861 AA;  96805 MW;  5E045F7CEF1D91EF CRC64;
     MPSLLGLKCL GKLCSSEIGK 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 KTEEKLRPPN IPRSSSDFFY
     PKSLIRRTGR SPALQLLSPP CLTNSNKNPR QPTRTSSESI YSRPGSSIPG SPGHTIYAKV
     DNEILDYKDL AAIPKVKAIY DIERPDLITY EPFYTSGYED KQERQSLGES PRTLSPTPSA
     EGYQDVRDRM IHRSTSQGSI NSPVYSRHSY TPTTSRSPQH FHRPELLSPG VHRWSPLRTS
     SFSSTHSDSR PNPPFRHHFL PHVKGNEPSS GRNSPLPYRP DSRPLTPTYA QAPKHFHVPD
     QGINIYRKPP IYKQHAALAA QSKASEDIIK FSKFPAAQAP DPNEIPKIET DHWPGPPSLA
     AVGTDPRRRS SGREEDEEEL LRRRQLQEEQ LMKLNSGLGQ LILKEEMEKE SRERASLASR
     YDSPLHSASH APSSKTSSLP GYGKNGLHRP VSTDFAQYNS YGDISGGVRD YQTLPDGHMP
     AVRMDRGVSM PNMLEPKIFP YEMLMVTNRG RNKILRDVDR TRLERHLAPE VFWEIFGMSI
     QEFDKLPLWR RNDMKKKAKL F
//
ID   PLCE1_MOUSE             Reviewed;        2282 AA.
AC   Q8K4S1; B9EHS1; Q3TS68; Q80TC4; Q8BZF3; Q9JKM2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase epsilon-1;
DE            EC=3.1.4.11;
DE   AltName: Full=Phosphoinositide phospholipase C-epsilon-1;
DE   AltName: Full=Phospholipase C-epsilon-1;
DE            Short=PLC-epsilon-1;
GN   Name=Plce1; Synonyms=Kiaa1516, Plce;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY,
RP   DEVELOPMENTAL STAGE, AND INDUCTION.
RC   TISSUE=Embryo;
RX   MEDLINE=22637746; PubMed=12752375;
RX   DOI=10.1046/j.1460-9568.2003.02591.x;
RA   Wu D., Tadano M., Edamatsu H., Masago-Toda M., Yamawaki-Kataoka Y.,
RA   Terashima T., Mizoguchi A., Minami Y., Satoh T., Kataoka T.;
RT   "Neuronal lineage-specific induction of phospholipase Cepsilon
RT   expression in the developing mouse brain.";
RL   Eur. J. Neurosci. 17:1571-1580(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Egg, 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   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and 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 919-2282 (ISOFORMS 1/2).
RX   MEDLINE=20581708; PubMed=11146508;
RX   DOI=10.1002/1097-0177(2000)9999:9999<::AID-DVDY1089>3.3.CO;2-O;
RA   Tidhar A., Reichenstein M., Cohen D., Faerman A., Copeland N.G.,
RA   Gilbert D.J., Jenkins N.A., Shani M.;
RT   "A novel transgenic marker for migrating limb muscle precursors and
RT   for vascular smooth muscle cells.";
RL   Dev. Dyn. 220:60-73(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 919-2282 (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   [6]
RP   FUNCTION.
RX   PubMed=12721365; DOI=10.1073/pnas.1031494100;
RA   Czyzyk J., Brogdon J.L., Badou A., Henegariu O., Preston Hurlburt P.,
RA   Flavell R., Bottomly K.;
RT   "Activation of CD4 T cells by Raf-independent effectors of Ras.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:6003-6008(2003).
RN   [7]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=15604236; DOI=10.1158/0008-5472.CAN-04-3143;
RA   Bai Y., Edamatsu H., Maeda S., Saito H., Suzuki N., Satoh T.,
RA   Kataoka T.;
RT   "Crucial role of phospholipase Cepsilon in chemical carcinogen-induced
RT   skin tumor development.";
RL   Cancer Res. 64:8808-8810(2004).
RN   [8]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=16293787; DOI=10.1161/01.RES.0000196578.15385.bb;
RA   Wang H., Oestreich E.A., Maekawa N., Bullard T.A., Vikstrom K.L.,
RA   Dirksen R.T., Kelley G.G., Blaxall B.C., Smrcka A.V.;
RT   "Phospholipase C epsilon modulates beta-adrenergic receptor-dependent
RT   cardiac contraction and inhibits cardiac hypertrophy.";
RL   Circ. Res. 97:1305-1313(2005).
RN   [9]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=15743817; DOI=10.1128/MCB.25.6.2191-2199.2005;
RA   Tadano M., Edamatsu H., Minamisawa S., Yokoyama U., Ishikawa Y.,
RA   Suzuki N., Saito H., Wu D., Masago-Toda M., Yamawaki-Kataoka Y.,
RA   Setsu T., Terashima T., Maeda S., Satoh T., Kataoka T.;
RT   "Congenital semilunar valvulogenesis defect in mice deficient in
RT   phospholipase C epsilon.";
RL   Mol. Cell. Biol. 25:2191-2199(2005).
RN   [10]
RP   INTERACTION WITH IQGAP1.
RX   PubMed=17086182; DOI=10.1038/ng1918;
RA   Hinkes B., Wiggins R.C., Gbadegesin R., Vlangos C.N., Seelow D.,
RA   Nuernberg G., Garg P., Verma R., Chaib H., Hoskins B.E., Ashraf S.,
RA   Becker C., Hennies H.C., Goyal M., Wharram B.L., Schachter A.D.,
RA   Mudumana S., Drummond I., Kerjaschki D., Waldherr R., Dietrich A.,
RA   Ozaltin F., Bakkaloglu A., Cleper R., Basel-Vanagaite L., Pohl M.,
RA   Griebel M., Tsygin A.N., Soylu A., Mueller D., Sorli C.S.,
RA   Bunney T.D., Katan M., Liu J., Attanasio M., O'toole J.F.,
RA   Hasselbacher K., Mucha B., Otto E.A., Airik R., Kispert A.,
RA   Kelley G.G., Smrcka A.V., Gudermann T., Holzman L.B., Nuernberg P.,
RA   Hildebrandt F.;
RT   "Positional cloning uncovers mutations in PLCE1 responsible for a
RT   nephrotic syndrome variant that may be reversible.";
RL   Nat. Genet. 38:1397-1405(2006).
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. PLCE1 is a bifunctional enzyme which also regulates
CC       small GTPases of the Ras superfamily through its Ras guanine-
CC       exchange factor (RasGEF) activity. As an effector of
CC       heterotrimeric and small G-protein, it may play a role in cell
CC       survival, cell growth, actin organization and T-cell activation.
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   -!- ENZYME REGULATION: Activated by the heterotrimeric G-protein
CC       subunits GNA12, GNA13 and GNB1-GNG2. Activated by HRAS, RAP1A,
CC       RHOA, RHOB, RHOC, RRAS and RRAS2. Activated by the G(s)-coupled
CC       GPCRs ADRB2, PTGER1 and CHRM3 through cyclic-AMP formation and
CC       RAP2B activation. Inhibited by G(i)-coupled GPCRs (By similarity).
CC   -!- SUBUNIT: Interacts with GTP-bound HRAS, RAP1A, RAP2A, RAP2B and
CC       RHOA (By similarity). Interacts with IQGAP1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity). Cell
CC       membrane (By similarity). Golgi apparatus membrane (By
CC       similarity). Note=Recruited to plasma membrane by activated HRAS
CC       and RAP2. Recruited to perinuclear membrane by activated RAP1A.
CC       Associates with Golgi membranes (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K4S1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K4S1-2; Sequence=VSP_021337, VSP_021338;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in neurons and to a lower
CC       extent in skin, skeletal muscle and heart (at protein level).
CC       Expressed in the epidermis.
CC   -!- DEVELOPMENTAL STAGE: Specifically expressed in cells committed to
CC       the neuronal lineage (at protein level). Weakly expressed at E7,
CC       expression strongly increases at later embryonic stages. Expressed
CC       abundantly in almost all neural tissues at E12.5 and also detected
CC       in tongue muscles, genital tubercle and hand plate. At E15.5 a
CC       strong expression in skeletal muscles is detected together with
CC       the strong expression in neural tissues.
CC   -!- INDUCTION: Up-regulated during the differentiation of neural
CC       precursor cells into neurons and not glial cells. Up-regulated in
CC       heart upon induced hypertrophy.
CC   -!- DOMAIN: The Ras-associating domain 1 is degenerated and may not
CC       bind HRAS. The Ras-associating domain 2 mediates interaction with
CC       GTP-bound HRAS, RAP1A, RAP2A and RAP2B and recruitment of HRAS to
CC       the cell membrane (By similarity).
CC   -!- DOMAIN: The Ras-GEF domain has a GEF activity towards HRAS and
CC       RAP1A. Mediates activation of the mitogen-activated protein kinase
CC       pathway (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice exhibit delayed onset and markedly
CC       reduced incidence of chemically induced skin squamous tumors. They
CC       also display cardiac malformations which mainly affects aortic and
CC       pulmonary valves and enhanced susceptibility to cardiac
CC       hypertrophy and fibrosis in response to chronic stress.
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   -!- SIMILARITY: Contains 2 Ras-associating domains.
CC   -!- SIMILARITY: Contains 1 Ras-GEF domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF40208.1; Type=Erroneous initiation;
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DR   EMBL; AB076247; BAC00906.1; -; mRNA.
DR   EMBL; AK035546; BAC29099.1; -; mRNA.
DR   EMBL; AK162236; BAE36807.1; -; mRNA.
DR   EMBL; BC138349; AAI38350.1; -; mRNA.
DR   EMBL; BC138350; AAI38351.1; -; mRNA.
DR   EMBL; AF233885; AAF40208.1; ALT_INIT; mRNA.
DR   EMBL; AK122521; BAC65803.1; -; mRNA.
DR   IPI; IPI00170268; -.
DR   IPI; IPI00798586; -.
DR   RefSeq; NP_062534.2; NM_019588.2.
DR   UniGene; Mm.34031; -.
DR   HSSP; Q9UHV3; 2C5L.
DR   ProteinModelPortal; Q8K4S1; -.
DR   SMR; Q8K4S1; 1849-1940, 1986-2094, 2111-2226.
DR   STRING; Q8K4S1; -.
DR   PhosphoSite; Q8K4S1; -.
DR   PRIDE; Q8K4S1; -.
DR   Ensembl; ENSMUST00000025962; ENSMUSP00000025962; ENSMUSG00000024998.
DR   GeneID; 74055; -.
DR   KEGG; mmu:74055; -.
DR   UCSC; uc008hjp.1; mouse.
DR   UCSC; uc008hjq.1; mouse.
DR   CTD; 74055; -.
DR   MGI; MGI:1921305; Plce1.
DR   eggNOG; roNOG11704; -.
DR   GeneTree; ENSGT00600000084213; -.
DR   HOVERGEN; HBG059220; -.
DR   InParanoid; Q8K4S1; -.
DR   OrthoDB; EOG4BG8V4; -.
DR   PhylomeDB; Q8K4S1; -.
DR   BRENDA; 3.1.4.11; 244.
DR   NextBio; 339656; -.
DR   ArrayExpress; Q8K4S1; -.
DR   Bgee; Q8K4S1; -.
DR   CleanEx; MM_PLCE1; -.
DR   Genevestigator; Q8K4S1; -.
DR   GermOnline; ENSMUSG00000024998; Mus musculus.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005624; C:membrane fraction; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; ISS:UniProtKB.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0000187; P:activation of MAPK activity; ISS:UniProtKB.
DR   GO; GO:0007200; P:activation of phospholipase C activity by G-protein coupled receptor protein signaling pathway coupled to IP3 second messenger; ISS:UniProtKB.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0008277; P:regulation of G-protein coupled receptor protein signaling pathway; ISS:UniProtKB.
DR   GO; GO:0046578; P:regulation of Ras protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0007264; P:small GTPase mediated 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; 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; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   InterPro; IPR000159; Ras-assoc.
DR   InterPro; IPR001895; RasGRF_CDC25.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Gene3D; G3DSA:3.20.20.190; PLC-like_Pdiesterase_TIM-brl; 3.
DR   Gene3D; G3DSA:1.10.840.10; RasGRF_CDC25; 1.
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   Pfam; PF00788; RA; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00149; PLCYc; 1.
DR   SMART; SM00314; RA; 1.
DR   SMART; SM00147; RasGEF; 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.
DR   PROSITE; PS50200; RA; 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; Golgi apparatus;
KW   Guanine-nucleotide releasing factor; Hydrolase; Lipid degradation;
KW   Membrane; Repeat; Transducer.
FT   CHAIN         1   2282       1-phosphatidylinositol-4,5-bisphosphate
FT                                phosphodiesterase epsilon-1.
FT                                /FTId=PRO_0000256239.
FT   DOMAIN      528    781       Ras-GEF.
FT   DOMAIN     1373   1521       PI-PLC X-box.
FT   DOMAIN     1710   1826       PI-PLC Y-box.
FT   DOMAIN     1836   1936       C2.
FT   DOMAIN     1992   2094       Ras-associating 1.
FT   DOMAIN     2115   2218       Ras-associating 2.
FT   REGION     1667   1744       Required for activation by RHOA, RHOB,
FT                                GNA12, GNA13 and G-beta gamma (By
FT                                similarity).
FT   ACT_SITE   1388   1388       By similarity.
FT   ACT_SITE   1433   1433       By similarity.
FT   VAR_SEQ       1   1150       Missing (in isoform 2).
FT                                /FTId=VSP_021337.
FT   VAR_SEQ    1151   1165       TAGSPNLATGMSSPI -> MAWGLHLPVTAMFLC (in
FT                                isoform 2).
FT                                /FTId=VSP_021338.
FT   CONFLICT   1798   1798       T -> A (in Ref. 4; AAF40208).
FT   CONFLICT   1829   1829       S -> N (in Ref. 4; AAF40208).
FT   CONFLICT   2215   2217       LKE -> VKD (in Ref. 2; BAC29099).
FT   CONFLICT   2233   2233       A -> G (in Ref. 2; BAC29099).
FT   CONFLICT   2236   2236       L -> V (in Ref. 2; BAC29099).
FT   CONFLICT   2239   2239       L -> V (in Ref. 2; BAC29099).
FT   CONFLICT   2275   2275       S -> T (in Ref. 2; BAC29099).
SQ   SEQUENCE   2282 AA;  255020 MW;  1E694A07ADADFFB3 CRC64;
     MTSEEMAASV LIPVTQRKVA SAQSVAEERS VKVSDAGIPR ARAGRQGALI PPTISQWNKH
     KEESSRSDLS KVFSIARGEL VCDENSNEEG WEENAPDSPE NHAMNGNSLV QSHQHQFPRS
     QLCEARDSVT EDPCLQPGIP SPLERKVLPG IQLEMEDSPM DVSPAGSQPR IMESSGPHSD
     RNTAVFHFHY EADRTMSDAF HTLSENLILD DCANCVTLPG GQQNKNCMAY ACKLVELTRT
     CGSKNGQVQC EHCTSLRDEY LCFESSCSKA DEVCSGGGFC EDGFAHGPAA KTFLSPLEDF
     SDNCEDVDDF FKSKKERSTL LVRRFCKNDR EVKKSVYTGT RAIMRTLPSG CIGPAAWNYV
     DQKKAGLLWP CGNVMGTLSA MDIRQSGSQR LSEAQWCLIY SAVRRGEEIE DTVGSLLHCS
     TQLPNSETAH GRIEDGPCLK QCVRDTECEF RATLQRTSIA QYITGSLLEA TTSLGARSGL
     LSSFGGSTGR IMLKERQLGT SMANSNPVPS SSAGISKELI DLQPLIQFPE EVASILTEQE
     QNIYRRVLPM DYLCFLTRDL SSPECQRSLP RLKASISESI LTSQSGEHNA LEDLVMRFNE
     VSSWVTWLIL TAGSMEEKRE VFSYLVHVAK CCWNMGNYNA VMEFLAGLRS RKVLKMWQFM
     DQSDIETMRS LKDAMAQHES SVEYKKVVTR ALHIPGCKVV PFCGVFLKEL CEVLDGASGL
     LKLCPRYSSQ EEALEFVADY SGQDNFLQRV GQNGLKNSEK ELTVNSIFQV IRSCSRSLEM
     EEEDSASEGS GSRKNSLKDK ARWQFIIGDL LDSENDIFEK SKECDPHGSE ESQKAFDHGT
     ELIPWYVLSI QADVHQFLLQ GATVIHYDQD THLSARCFLQ LQPDNSTLTW MKPPTASPAG
     ARPKLGVLSN MAEPGKFPSP GNAGVSGLAE GILDLFSVKA VYMGHPGIDI HTVCVQNKLS
     SMLLSETGVT LLYGLQTTDN RLLHFVAPKH TAEMLFSGLL ELTTAVRKIR RFPDQRQQWL
     RKQYVSLYQE DGRYEGPTLA HAVELFGGRR WSTRNPSPGM SAKNAEKPNM QRNNTLGIST
     TKKKKKMLMR GESGEVTDDE MATRKAKMYR ECRSRSGSDP QDVNEQEESE ANVITNPPNP
     LHSRRAYSLT TAGSPNLATG MSSPISAWSS SSWHGRIRGG MQGFQSFMVS DSNMSFVEFV
     ELFKSFSIRS RKDLKDIFDI YSVPCNRSAS ESAPLYTNLT IEENTSDLQP DLDLLTRNVS
     DLGLFIKSKQ QLSDNQRQIS DAIAAASIVT NGTGIESTSL GIFGVGILQL NDFLVNCQGE
     HCTYDEILSI IQKFEPSVSM CHQGLLSFEG FARFLMDKDN FASKNDESRE NKKELQLPLS
     YYYIESSHNT YLTGHQLKGE SSVELYSQVL LQGCRSIELD CWDGDDGMPI IYHGHTLTTK
     IPFKEVVEAI DRSAFITSDL PIIISIENHC SLPQQRKMAE IFKSVFGEKL VAKFLFETDF
     SDDPMLPSPD QLRRKVLLKN KKLKAHQTPV DILKQKAHQL ASMQAQAFTG GNANPPPASN
     EEEEDEEDEY DYDYESLSDD NILEDRPENK SCADKLQFEY NEEVPKRIKK ADNSSGNKGK
     VYDMELGEEF YLPQNKKESR QIAPELSDLV IYCQAVKFPG LSTLNSSGSS RGKERKSRKS
     IFGNNPGRMS PGETAPFNRT SGKGSCEGMR HTWEESSPLS PSTSLSAIIR TPKCYHISSL
     NENAAKRLCR RGSQKLIQHT AYQLLRTYPA ATRIDSSNPN PIMFWLHGIQ LVALNYQTDD
     LPLHLNAAMF EANGGCGYVL KPPVLWDKSC PMYQKFSPLE RDLDNLDPAI YSLTIISGQN
     VCPSNSTGSP CIEVDVLGMP LDSCHFRTKP IHRNTLNPMW NEQFLFRVHF EDLVFLRFAV
     VENNSSAITA QRIIPLRALK RGYRHLQLRN LHNEILEISS LFINSRRMEE NPSGSSMPAS
     LMFNTEERKC SQTHKVTVHG VPGPEPFAVF TINEGTKAKQ LLQQVLAVDQ DTKCTATDYF
     LMEEKHFISK EKNECRKQPF QRAVGPEEDI VQILNSWFPE EGYVGRIVLK PQQETLEEKS
     IVFDDKEVIL SSEEESFFVQ VHDVSPEQPR TVIKAPRVST AQDVIQQTLC KAKYSYSILN
     NPNPCDYVLL EEVLKDAANK KSSTPKSSQR ILLDQECVFQ AQSKWKGAGK FILKLKEQVQ
     ASREDKRRGI SFASELKKLT KSTKQSRGLP SPPQLVASES VQSKEEKPVG ALSSSDTVGY
     QQ
//
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   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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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
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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   MTSS1_MOUSE             Reviewed;         759 AA.
AC   Q8R1S4; Q8BMM3; Q99LB3;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-FEB-2011, entry version 73.
DE   RecName: Full=Metastasis suppressor protein 1;
DE   AltName: Full=Missing in metastasis protein;
GN   Name=Mtss1; Synonyms=Mim;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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   MUTAGENESIS OF LYS-746 AND LYS-747, AND INTERACTION OF WH2 DOMAIN WITH
RP   ACTIN.
RC   STRAIN=FVB/N;
RX   MEDLINE=22499581; PubMed=12482861; DOI=10.1074/jbc.M212113200;
RA   Mattila P.K., Salminen M., Yamashiro T., Lappalainen P.;
RT   "Mouse MIM, a tissue-specific regulator of cytoskeletal dynamics,
RT   interacts with ATP-actin monomers through its C-terminal WH2 domain.";
RL   J. Biol. Chem. 278:8452-8459(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and 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 [LARGE SCALE MRNA] OF 82-759 (ISOFORM 1).
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-530, 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 THR-262; SER-276; SER-319;
RP   SER-320 AND SER-573, 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-607, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., 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: Inhibits the nucleation of actin filaments in vitro.
CC   -!- SUBUNIT: Binds to actin.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Long;
CC         IsoId=Q8R1S4-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=Q8R1S4-2; Sequence=VSP_050527, VSP_050528, VSP_050529;
CC   -!- TISSUE SPECIFICITY: Strongly expressed in the developing neurons
CC       and skeletal and cardiac muscles in embryos. Strongly expressed
CC       also in liver, outer layers of the kidney, and in the Purkinje
CC       cells of the brain.
CC   -!- DOMAIN: The WH2 motif at the C-terminus binds to actin monomers.
CC   -!- SIMILARITY: Belongs to the MTSS1 family.
CC   -!- SIMILARITY: Contains 1 IMD (IRSp53/MIM homology) domain.
CC   -!- SIMILARITY: Contains 1 WH2 domain.
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DR   EMBL; AY214918; AAO52743.1; -; mRNA.
DR   EMBL; BC003483; AAH03483.1; -; mRNA.
DR   EMBL; BC024131; AAH24131.1; -; mRNA.
DR   EMBL; BC042632; AAH42632.1; -; mRNA.
DR   EMBL; AK030533; BAC27008.1; -; mRNA.
DR   IPI; IPI00153439; -.
DR   IPI; IPI00278134; -.
DR   RefSeq; NP_659049.2; NM_144800.2.
DR   UniGene; Mm.215481; -.
DR   UniGene; Mm.394414; -.
DR   PDB; 2D1L; X-ray; 1.85 A; A/B=1-250.
DR   PDBsum; 2D1L; -.
DR   ProteinModelPortal; Q8R1S4; -.
DR   SMR; Q8R1S4; 1-246, 729-757.
DR   DIP; DIP-29271N; -.
DR   STRING; Q8R1S4; -.
DR   PhosphoSite; Q8R1S4; -.
DR   PRIDE; Q8R1S4; -.
DR   Ensembl; ENSMUST00000080371; ENSMUSP00000079239; ENSMUSG00000022353.
DR   Ensembl; ENSMUST00000110150; ENSMUSP00000105777; ENSMUSG00000022353.
DR   GeneID; 211401; -.
DR   KEGG; mmu:211401; -.
DR   UCSC; uc007vtx.1; mouse.
DR   CTD; 211401; -.
DR   MGI; MGI:2384818; Mtss1.
DR   GeneTree; ENSGT00390000002637; -.
DR   HOVERGEN; HBG052530; -.
DR   NextBio; 373226; -.
DR   ArrayExpress; Q8R1S4; -.
DR   Bgee; Q8R1S4; -.
DR   CleanEx; MM_MTSS1; -.
DR   Genevestigator; Q8R1S4; -.
DR   GermOnline; ENSMUSG00000022353; Mus musculus.
DR   GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0003785; F:actin monomer binding; ISS:UniProtKB.
DR   GO; GO:0008093; F:cytoskeletal adaptor activity; IEA:InterPro.
DR   GO; GO:0005102; F:receptor binding; ISS:UniProtKB.
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:0007517; P:muscle organ development; NAS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; NAS:UniProtKB.
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   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Alternative splicing; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Phosphoprotein.
FT   CHAIN         1    759       Metastasis suppressor protein 1.
FT                                /FTId=PRO_0000096640.
FT   DOMAIN        1    254       IMD.
FT   DOMAIN      731    748       WH2.
FT   COILED      108    157       Potential.
FT   COMPBIAS    242    363       Ser-rich.
FT   COMPBIAS    612    730       Pro-rich.
FT   MOD_RES     262    262       Phosphothreonine.
FT   MOD_RES     265    265       Phosphoserine (By similarity).
FT   MOD_RES     276    276       Phosphoserine.
FT   MOD_RES     319    319       Phosphoserine.
FT   MOD_RES     320    320       Phosphoserine.
FT   MOD_RES     530    530       Phosphotyrosine.
FT   MOD_RES     573    573       Phosphoserine.
FT   MOD_RES     607    607       Phosphothreonine.
FT   VAR_SEQ     483    483       L -> P (in isoform 2).
FT                                /FTId=VSP_050527.
FT   VAR_SEQ     487    487       L -> P (in isoform 2).
FT                                /FTId=VSP_050528.
FT   VAR_SEQ     646    681       Missing (in isoform 2).
FT                                /FTId=VSP_050529.
FT   MUTAGEN     746    746       K->A: Loss of actin-binding.
FT   MUTAGEN     747    747       K->A: Loss of actin-binding.
FT   CONFLICT    139    139       N -> K (in Ref. 3; BAC27008).
FT   CONFLICT    758    758       F -> L (in Ref. 3; BAC27008).
FT   HELIX         1     24
FT   HELIX        27     66
FT   HELIX        71    103
FT   HELIX       105    150
FT   HELIX       154    156
FT   TURN        157    159
FT   HELIX       162    214
FT   HELIX       215    219
FT   HELIX       220    233
FT   HELIX       242    244
SQ   SEQUENCE   759 AA;  82408 MW;  3E9008065FF78439 CRC64;
     MEAVIEKECS ALGGLFQTII SDMKGSYPVW EDFINKAGKL QSQLRTTVVA AAAFLDAFQK
     VADMATNTRG GTREIGSALT RMCMRHRSIE AKLRQFSSAL IDCLINPLQE QMEEWKKVAN
     QLDKDHAKEY KKARQEIKNK SSDTLKLQKK AKKVDAQGRG DIQPQLDSAL QDVNDKYLLL
     EETEKQAVRK ALIEERGRFC TFISMLRPVI EEEISMLGEI THLQTISEDL KSLTMDPHKL
     PSSSEQVILD LKGSDYSWSY QTPPSSPSTT MSRKSSVCSS LNSVNSSDSR SSGSHSHSPS
     SHYRYRSSNL AQQAPVRLSS VSSHDSGFIS QDAFQSKSPS PMPPEAANQL SNGFSHCSLS
     SESHAGPVGA GPFPHCLPAS RLLPRVTSVH LPDYAHYYTI GPGMFPSSQI PSWKDWAKPG
     PYDQPLVNTL QRRKEKREPD SNGGGPTTTG GPPAGAEEAQ RPRSMTVSAA TRPGEEMAAC
     EELTLALSRG LQLDVQRSSR DSLQCSSGYS TQTTTPCCSE DTIPSQVSDY DYFSVSGDQE
     AEQQEFDKSS TIPRNSDISQ SYRRMFQAKR PASTAGLPTT LGPAMVTPGV ATIRRTPSTK
     PSVRRGTIGA GPIPIKTPVI PVKTPTVPDL PGVLPSPPDG PEERGEHSPE SPSAGEGPQG
     VSNIPSSLWS GQAPVNPPLP GPKPSIPEEH RQAIPESEAE DQERDPPSAT VSPGPIPESD
     PADLSPRESP QGEDMLNAIR RGVKLKKTTT NDRSAPRFS
//
ID   SPG20_MOUSE             Reviewed;         671 AA.
AC   Q8R1X6; Q6ZQ87; Q8BJD3; Q8BM37; Q8BZ63;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Spartin;
GN   Name=Spg20; Synonyms=Kiaa0610;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; 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=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 11-671 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Bone, 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).
CC   -!- FUNCTION: May be implicated in endosomal trafficking, or
CC       microtubule dynamics, or both.
CC   -!- SUBUNIT: Interacts with ITCH and WWP1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=Transiently
CC       associated with endosomes (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R1X6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R1X6-2; Sequence=VSP_010934;
CC   -!- PTM: Ubiquinated; ubiquitination does not require ITCH and WWP1
CC       (By similarity).
CC   -!- SIMILARITY: Contains 1 MIT domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC39856.1; Type=Erroneous initiation;
CC       Sequence=BAC97981.1; Type=Erroneous initiation;
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DR   EMBL; AK129171; BAC97981.1; ALT_INIT; mRNA.
DR   EMBL; BC022921; AAH22921.1; -; mRNA.
DR   EMBL; AK035081; BAC28937.1; -; mRNA.
DR   EMBL; AK036569; BAC29482.1; -; mRNA.
DR   EMBL; AK087388; BAC39856.1; ALT_INIT; mRNA.
DR   IPI; IPI00153501; -.
DR   IPI; IPI00453929; -.
DR   RefSeq; NP_001138459.1; NM_001144987.1.
DR   RefSeq; NP_001138460.1; NM_001144988.1.
DR   RefSeq; NP_659144.1; NM_144895.2.
DR   UniGene; Mm.235523; -.
DR   ProteinModelPortal; Q8R1X6; -.
DR   SMR; Q8R1X6; 7-111.
DR   STRING; Q8R1X6; -.
DR   PhosphoSite; Q8R1X6; -.
DR   PRIDE; Q8R1X6; -.
DR   Ensembl; ENSMUST00000044116; ENSMUSP00000042367; ENSMUSG00000036580.
DR   Ensembl; ENSMUST00000107971; ENSMUSP00000103605; ENSMUSG00000036580.
DR   Ensembl; ENSMUST00000118118; ENSMUSP00000113621; ENSMUSG00000036580.
DR   GeneID; 229285; -.
DR   KEGG; mmu:229285; -.
DR   UCSC; uc008pgb.1; mouse.
DR   UCSC; uc008pgc.1; mouse.
DR   CTD; 229285; -.
DR   MGI; MGI:2139806; Spg20.
DR   GeneTree; ENSGT00390000012235; -.
DR   HOGENOM; HBG443605; -.
DR   HOVERGEN; HBG079206; -.
DR   InParanoid; Q8R1X6; -.
DR   OMA; LRLQANW; -.
DR   OrthoDB; EOG4BZN29; -.
DR   PhylomeDB; Q8R1X6; -.
DR   NextBio; 379384; -.
DR   ArrayExpress; Q8R1X6; -.
DR   Bgee; Q8R1X6; -.
DR   Genevestigator; Q8R1X6; -.
DR   GermOnline; ENSMUSG00000036580; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR007330; MIT.
DR   InterPro; IPR009686; Senescence/spartin.
DR   Pfam; PF04212; MIT; 1.
DR   Pfam; PF06911; Senescence; 1.
DR   SMART; SM00745; MIT; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Cytoplasm; Isopeptide bond;
KW   Phosphoprotein; Ubl conjugation.
FT   CHAIN         1    671       Spartin.
FT                                /FTId=PRO_0000072120.
FT   DOMAIN       16     94       MIT.
FT   COMPBIAS    370    376       Poly-Ser.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     474    474       Phosphoserine (By similarity).
FT   CROSSLNK    360    360       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   VAR_SEQ     337    393       Missing (in isoform 2).
FT                                /FTId=VSP_010934.
FT   CONFLICT    157    157       S -> F (in Ref. 3; BAC28937).
FT   CONFLICT    264    264       R -> P (in Ref. 3; BAC39856).
FT   CONFLICT    297    297       D -> N (in Ref. 3; BAC39856).
FT   CONFLICT    344    353       DEFQIPGRSS -> MNSKSLGDQA (in Ref. 3;
FT                                BAC39856).
SQ   SEQUENCE   671 AA;  72655 MW;  5C17F0268E420B26 CRC64;
     MEREPENGEP AEIKIIKEAY EKAFMFVNKG LNTDELGQKE EAKNYYKQGI GHLLRGISIA
     AAEPGHTGPA WEAARQMQQK MKETLQNVRT RLEILEKGLA TSLRNDLQDV PKLYPEFPPK
     DACKKSPEQE SVSTAPQRAE VDGSASAACA GPSGAPSALP VPSPSCPAEA PPAYSPQAAE
     GHYTVSYGTD SGEFSSVGED FYRNRSQPPP LETLGLDADE LILIPNGVQI FFVNPAGEVS
     APSYPGYLRI VRFLDNSLDT VLNRPPGFLQ VCDWLYPLVP DRSPVLKCTV GAYMFPDTML
     QAAGCFVGVV LSSELPEDDR ELFEDLLRQM SDLRLQANWN REEDEFQIPG RSSHPSEPPK
     EASGTDVRQS SSSGSSIDQG SKDARHKGKR GKKTKDSSEE VNLSQIVPCE PSSEEKSKEL
     PEWSEKVAHN ILSGASWVSW GLVKGAEFTG KAIQKGASKL RERIQPEEKP VEVSPAVTRG
     LYIAKQATGG AAKVSQLLVD GVCTVANCVG KELAPHVKKH GSKLVPESLK RDKDGKSALD
     GAMVVAASSV QGFSTVWQGL ECAAKCIVNN VSAETVQTVR YKYGHNAGEA THNAVDSAIN
     VGLTAYNIDN IGIKAMVKKT AKQTGHTLLE DYQIVERPQR ESQGGATSTE GRRDIGKQVE
     EEKPGAGKKD K
//
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.
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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   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.
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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   BRD8_MOUSE              Reviewed;         951 AA.
AC   Q8R3B7; Q3TSZ2; Q8C049; Q8R583; Q8VDP0;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Bromodomain-containing protein 8;
GN   Name=Brd8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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 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=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and 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-710 AND SER-714, 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 coactivator during transcriptional
CC       activation by hormone-activated nuclear receptors (NR). Stimulates
CC       transcriptional activation by AR/DHTR, ESR1/NR3A1, RXRA/NR2B1 and
CC       THRB/ERBA2. Component of the NuA4 histone acetyltransferase (HAT)
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. NuA4 may also
CC       play a direct role in DNA repair when recruited to sites of DNA
CC       damage.
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. Component of a NuA4-
CC       related complex which contains EP400, TRRAP/PAF400, SRCAP,
CC       BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin,
CC       ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. BRD8 isoform 2 interacts
CC       with RXRA/NR2B1 and THRB/ERBA2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R3B7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R3B7-2; Sequence=VSP_038218;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 bromo domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH23160.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC       Sequence=AAH25644.1; Type=Erroneous initiation;
CC       Sequence=BAC27812.1; Type=Erroneous initiation;
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DR   EMBL; AK032320; BAC27812.1; ALT_INIT; mRNA.
DR   EMBL; AK161689; BAE36533.1; -; mRNA.
DR   EMBL; BC023160; AAH23160.1; ALT_SEQ; mRNA.
DR   EMBL; BC025644; AAH25644.1; ALT_INIT; mRNA.
DR   IPI; IPI00153722; -.
DR   IPI; IPI00653134; -.
DR   RefSeq; NP_084423.2; NM_030147.2.
DR   UniGene; Mm.411740; -.
DR   UniGene; Mm.45602; -.
DR   ProteinModelPortal; Q8R3B7; -.
DR   SMR; Q8R3B7; 786-884.
DR   STRING; Q8R3B7; -.
DR   PhosphoSite; Q8R3B7; -.
DR   PRIDE; Q8R3B7; -.
DR   Ensembl; ENSMUST00000003876; ENSMUSP00000003876; ENSMUSG00000003778.
DR   GeneID; 78656; -.
DR   KEGG; mmu:78656; -.
DR   UCSC; uc008ekv.1; mouse.
DR   CTD; 78656; -.
DR   MGI; MGI:1925906; Brd8.
DR   GeneTree; ENSGT00530000064262; -.
DR   HOVERGEN; HBG050732; -.
DR   OrthoDB; EOG470THC; -.
DR   PhylomeDB; Q8R3B7; -.
DR   NextBio; 349290; -.
DR   ArrayExpress; Q8R3B7; -.
DR   Bgee; Q8R3B7; -.
DR   CleanEx; MM_BRD8; -.
DR   Genevestigator; Q8R3B7; -.
DR   GermOnline; ENSMUSG00000003778; Mus musculus.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
DR   GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR   GO; GO:0040008; P:regulation of growth; 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; IPR001487; Bromodomain.
DR   Gene3D; G3DSA:1.20.920.10; Bromodomain; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; FALSE_NEG.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Bromodomain; Chromatin regulator;
KW   Coiled coil; Growth regulation; Nucleus; Phosphoprotein;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    951       Bromodomain-containing protein 8.
FT                                /FTId=PRO_0000211186.
FT   DOMAIN      797    867       Bromo.
FT   COILED       97    171       Potential.
FT   MOD_RES     264    264       Phosphothreonine (By similarity).
FT   MOD_RES     268    268       Phosphoserine (By similarity).
FT   MOD_RES     284    284       Phosphoserine (By similarity).
FT   MOD_RES     460    460       Phosphoserine (By similarity).
FT   MOD_RES     554    554       N6-acetyllysine (By similarity).
FT   MOD_RES     710    710       Phosphoserine.
FT   MOD_RES     714    714       Phosphoserine.
FT   VAR_SEQ     215    287       Missing (in isoform 2).
FT                                /FTId=VSP_038218.
FT   CONFLICT    811    811       D -> G (in Ref. 1; BAC27812).
SQ   SEQUENCE   951 AA;  102610 MW;  133859691F7CCEFB CRC64;
     MATGTGKHKL LSTGPTEPWS IREKLCLASS VMRSGDQNWV SVSRAIKPFA EPGRPPDWFS
     QKHCASQYSE LLETTETPKR KRGEKGEVVE TVEDVIVRKL TAERVEELKK VIKETQERYR
     RLKRDAELIQ AGHMDSRLDE LCNDIAMKKK LEEEEAEVKR KATDAAYQAR QAVKTPPRRL
     PTVMVRSPVD SASPGGDYPL GDLTPTTMEE ATSGVTPGTL PSTPVTSFPG IPDTLPPGSA
     PLEAPMTPIT DDSPQKKMLG QKATPPPSPL LSELLKKGSL LPTSPRLVNE SEMPVPPGHL
     NSTGVLLEVG GVLPMIHGGE IQPTTSAVAA SPAASGAPTL SRLLEAGPTQ FTTPLPSFTT
     VASEPPVKLV PPPVESVSQA TIVMMPALPA PSSAAAVSTS ESGAPVSQPE PCVPLEAVGD
     PHTVTVSMDS NEISMIINSI KEECFRSGVA EAPGGSKAPS IDGKEDLDLA EKMDIAVSYT
     GEELDFETVG DIIAIIEDKV DDHPEVLDVA AVEAALSFCE ENDDPQSLPG PWEHPIQQER
     DKPVPLPAPE MTVKQERLDF EESENKGLHD LVDIRDSGVE IKVEPTEPEP GMSGAEIVAG
     VGPVPSMEPP ELRSQDSDEE PRSSAAGDIG EADGSSGKGD ERPLSAVKTE ASPESMLSPS
     HGSNLIEDPL EAETQHKFEM SDSLKEESGT IFGSQIKDAP GDDEEEDGVS EAASLEEPKE
     EDQGEGYLSE MDNEPPVSES DDGFSIHNAT LQSHTLADSI PSSPASSQFS VCSEDQEAIQ
     AQKIWKKAIM LVWRAAANHR YANVFLQPVT DDIAPGYHSI VQRPMDLSTI KKNIENGLIR
     STAEFQRDIM LMFQNAVMYN SSDHDVYHMA VEMQRDVLEQ IQQFLATQLI MQTSESGISA
     KSLRGRDSTR KQDASEKDSV PMGSPAFLLS LFDGGTRGRR CAIEADMKMK K
//
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.
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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   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).
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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   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.
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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   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   GRAN_MOUSE              Reviewed;         220 AA.
AC   Q8VC88; Q8BL53; Q8K3Z6;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Grancalcin;
GN   Name=Gca;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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 DISRUPTION PHENOTYPE.
RX   MEDLINE=22417474; PubMed=12529388; DOI=10.1128/MCB.23.3.826-830.2003;
RA   Roes J., Choi B.K., Power D., Xu P., Segal A.W.;
RT   "Granulocyte function in grancalcin-deficient mice.";
RL   Mol. Cell. Biol. 23:826-830(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15118320; DOI=10.1271/bbb.68.894;
RA   Liu F., Shinomiya H., Kirikae T., Hirata H., Asano Y.;
RT   "Characterization of murine grancalcin specifically expressed in
RT   leukocytes and its possible role in host defense against bacterial
RT   infection.";
RL   Biosci. Biotechnol. Biochem. 68:894-902(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cecum, Corpora quadrigemina, 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=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   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=16934789; DOI=10.1016/j.cellimm.2006.07.004;
RA   Xu P., Roes J., Segal A.W., Radulovic M.;
RT   "The role of grancalcin in adhesion of neutrophils.";
RL   Cell. Immunol. 240:116-121(2006).
CC   -!- FUNCTION: Calcium-binding protein that may play a role in the
CC       adhesion of neutrophils to fibronectin. May play a role in the
CC       formation of focal adhesions.
CC   -!- SUBUNIT: Homodimer. Interacts with SRI and LCP1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasmic
CC       granule membrane; Peripheral membrane protein; Cytoplasmic side
CC       (By similarity). Note=Primarily cytosolic in the absence of
CC       calcium or magnesium ions. Relocates to granules and other
CC       membranes in response to elevated calcium and magnesium levels (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Not essential for
CC       normal resistance to microbial infections. Grancalcin-deficient
CC       neutrophils exhibit decreased adhesion to fibronectin, and a
CC       strongly reduced number of focal adhesion complexes.
CC   -!- MISCELLANEOUS: This protein has been shown to bind calcium with
CC       high affinity (By similarity).
CC   -!- SIMILARITY: Contains 4 EF-hand domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF518325; AAM66720.1; -; mRNA.
DR   EMBL; AB088388; BAC07231.1; -; mRNA.
DR   EMBL; AK033740; BAC28458.1; -; mRNA.
DR   EMBL; AK046347; BAC32686.1; -; mRNA.
DR   EMBL; AK049317; BAC33679.1; -; mRNA.
DR   EMBL; AK050540; BAC34315.1; -; mRNA.
DR   EMBL; AK078915; BAC37457.1; -; mRNA.
DR   EMBL; BC021450; AAH21450.1; -; mRNA.
DR   IPI; IPI00308789; -.
DR   RefSeq; NP_663498.1; NM_145523.3.
DR   UniGene; Mm.219877; -.
DR   ProteinModelPortal; Q8VC88; -.
DR   SMR; Q8VC88; 56-220.
DR   STRING; Q8VC88; -.
DR   REPRODUCTION-2DPAGE; IPI00308789; -.
DR   PRIDE; Q8VC88; -.
DR   Ensembl; ENSMUST00000028257; ENSMUSP00000028257; ENSMUSG00000026893.
DR   GeneID; 227960; -.
DR   KEGG; mmu:227960; -.
DR   UCSC; uc008jvp.1; mouse.
DR   CTD; 227960; -.
DR   MGI; MGI:1918521; Gca.
DR   GeneTree; ENSGT00580000081418; -.
DR   HOGENOM; HBG747897; -.
DR   HOVERGEN; HBG004492; -.
DR   InParanoid; Q8VC88; -.
DR   OMA; KCLTQSG; -.
DR   OrthoDB; EOG4ZS949; -.
DR   PhylomeDB; Q8VC88; -.
DR   NextBio; 378876; -.
DR   ArrayExpress; Q8VC88; -.
DR   Bgee; Q8VC88; -.
DR   CleanEx; MM_GCA; -.
DR   Genevestigator; Q8VC88; -.
DR   GermOnline; ENSMUSG00000026893; Mus musculus.
DR   GO; GO:0005829; C:cytosol; TAS:MGI.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; 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   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; Membrane; Repeat.
FT   CHAIN         1    220       Grancalcin.
FT                                /FTId=PRO_0000073722.
FT   DOMAIN       51     86       EF-hand 1.
FT   DOMAIN       92    127       EF-hand 2.
FT   DOMAIN      122    157       EF-hand 3.
FT   DOMAIN      158    193       EF-hand 4.
FT   CA_BIND     105    116       1 (Potential).
FT   CA_BIND     135    146       2 (Potential).
FT   CONFLICT    187    188       KL -> NV (in Ref. 1; AAM66720).
FT   CONFLICT    217    217       T -> P (in Ref. 3; BAC32686).
SQ   SEQUENCE   220 AA;  24663 MW;  694DCA7D6ADF8279 CRC64;
     MAYPGYGGAF GNFSGQIPGM QMQMGQPMPG AGPNMFSGGY PGYLGYSDSY SPADDSMWTY
     FTAVAGQDGE VDAEELQRCL TQSGISGTYA PFSLETCRIM IAMLDRDYTG KMGFNEFKEL
     WAALNAWKQN FMTIDQDQSG TVEHHELSQA IALMGYRLSP QTLAAIVRRY SKNGRIFFDD
     YVACCVKLRA LTDFFRRRDH LQQGIVNFMY EDFLQGTMTI
//
ID   MAVS_MOUSE              Reviewed;         503 AA.
AC   Q8VCF0;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Mitochondrial antiviral-signaling protein;
DE   AltName: Full=CARD adapter inducing interferon beta;
DE            Short=Cardif;
DE   AltName: Full=Interferon beta promoter stimulator protein 1;
DE            Short=IPS-1;
DE   AltName: Full=Virus-induced-signaling adapter;
GN   Name=Mavs; Synonyms=Ips1, Visa;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=16125763; DOI=10.1016/j.cell.2005.08.012;
RA   Seth R.B., Sun L., Ea C.-K., Chen Z.J.;
RT   "Identification and characterization of MAVS, a mitochondrial
RT   antiviral signaling protein that activates NF-kappaB and IRF 3.";
RL   Cell 122:669-682(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16153868; DOI=10.1016/j.molcel.2005.08.014;
RA   Xu L.-G., Wang Y.-Y., Han K.-J., Li L.-Y., Zhai Z., Shu H.-B.;
RT   "VISA is an adapter protein required for virus-triggered IFN-beta
RT   Signaling.";
RL   Mol. Cell 19:727-740(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16177806; DOI=10.1038/nature04193;
RA   Meylan E., Curran J., Hofmann K., Moradpour D., Binder M.,
RA   Bartenschlager R., Tschopp J.;
RT   "Cardif is an adaptor protein in the RIG-I antiviral pathway and is
RT   targeted by hepatitis C virus.";
RL   Nature 437:1167-1172(2005).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Eye, 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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147; SER-152; SER-157;
RP   SER-309 AND THR-310, 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   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).
CC   -!- FUNCTION: Required for innate immune defense against viruses. Acts
CC       downstream of DDX58 and IFIH1/MDA5, which detect intracellular
CC       dsRNA produced during viral replication, to coordinate pathways
CC       leading to the activation of NF-kappa-B, IRF3 and IRF7, and to the
CC       subsequent induction of antiviral cytokines such as IFN-beta and
CC       RANTES (CCL5). May activate the same pathways following detection
CC       of extracellular dsRNA by TLR3. May protect cells from apoptosis
CC       (By similarity).
CC   -!- SUBUNIT: Interacts with DDX58, IFIH1, TRAF2 and TRAF6. May
CC       interact with IRF3, FADD, RIPK1, IKBKE, CHUK and IKBKB. Does not
CC       interact with TBK1. Interacts with NLRX1. Interaction with NLRX1
CC       requires the CARD domain (By similarity). Interacts with PSMA7 (By
CC       similarity). Interacts with TRAFD1. Interacts (via C-terminus)
CC       with PCBP2 in a complex containing MAVS, PCBP2 and ITCH. Interacts
CC       with CYLD (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane (By
CC       similarity).
CC   -!- DOMAIN: Both CARD and transmembrane domains are essential for
CC       antiviral function. The CARD domain is responsible for interaction
CC       with DDX58 and IFIH1 (By similarity).
CC   -!- PTM: Ubiquitinated; undergoes 'Lys-48'-linked polyubiquitination
CC       catalyzed by ITCH; ITCH-dependent polyubiquitination is mediated
CC       by the interaction with PCBP2 and leads to MAVS proteosomal
CC       degradation (By similarity).
CC   -!- SIMILARITY: Contains 1 CARD domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; DQ174271; AAZ80418.1; -; mRNA.
DR   EMBL; DQ167127; ABA54891.1; -; mRNA.
DR   EMBL; AK028421; BAC25940.1; -; mRNA.
DR   EMBL; BC020006; AAH20006.1; -; mRNA.
DR   EMBL; BC025825; AAH25825.1; -; mRNA.
DR   EMBL; BC031352; AAH31352.1; -; mRNA.
DR   EMBL; BC037391; AAH37391.1; -; mRNA.
DR   IPI; IPI00122075; -.
DR   RefSeq; NP_659137.1; NM_144888.1.
DR   UniGene; Mm.287226; -.
DR   ProteinModelPortal; Q8VCF0; -.
DR   SMR; Q8VCF0; 1-93.
DR   MINT; MINT-2839937; -.
DR   STRING; Q8VCF0; -.
DR   PhosphoSite; Q8VCF0; -.
DR   PRIDE; Q8VCF0; -.
DR   Ensembl; ENSMUST00000041362; ENSMUSP00000038339; ENSMUSG00000037523.
DR   Ensembl; ENSMUST00000110199; ENSMUSP00000105828; ENSMUSG00000037523.
DR   GeneID; 228607; -.
DR   KEGG; mmu:228607; -.
DR   UCSC; uc008mle.1; mouse.
DR   CTD; 228607; -.
DR   MGI; MGI:2444773; Mavs.
DR   GeneTree; ENSGT00510000049120; -.
DR   HOGENOM; HBG126010; -.
DR   HOVERGEN; HBG079638; -.
DR   InParanoid; Q8VCF0; -.
DR   OMA; PINSTRA; -.
DR   OrthoDB; EOG42BX8F; -.
DR   PhylomeDB; Q8VCF0; -.
DR   NextBio; 379056; -.
DR   ArrayExpress; Q8VCF0; -.
DR   Bgee; Q8VCF0; -.
DR   CleanEx; MM_D430028G21RIK; -.
DR   Genevestigator; Q8VCF0; -.
DR   GermOnline; ENSMUSG00000037523; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; EXP:Reactome.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR   GO; GO:0002230; P:positive regulation of defense response to virus by host; ISS:UniProtKB.
DR   GO; GO:0032727; P:positive regulation of interferon-alpha production; ISS:UniProtKB.
DR   GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:UniProtKB.
DR   GO; GO:0009615; P:response to virus; IEA:UniProtKB-KW.
DR   PROSITE; PS50209; CARD; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Antiviral defense; Immunity; Innate immunity; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix; Ubl conjugation.
FT   CHAIN         1    503       Mitochondrial antiviral-signaling
FT                                protein.
FT                                /FTId=PRO_0000144097.
FT   TOPO_DOM      1    478       Cytoplasmic (By similarity).
FT   TRANSMEM    479    496       Helical; (Potential).
FT   TOPO_DOM    497    503       Mitochondrial intermembrane (By
FT                                similarity).
FT   DOMAIN       10     77       CARD.
FT   REGION       10     77       Required for interaction with NLRX1 (By
FT                                similarity).
FT   REGION      143    147       Interaction with TRAF2 (By similarity).
FT   REGION      153    158       Interaction with TRAF6 1 (By similarity).
FT   REGION      431    436       Interaction with TRAF6 2 (By similarity).
FT   MOD_RES     147    147       Phosphothreonine.
FT   MOD_RES     152    152       Phosphoserine.
FT   MOD_RES     157    157       Phosphoserine.
FT   MOD_RES     163    163       Phosphothreonine (By similarity).
FT   MOD_RES     220    220       Phosphoserine (By similarity).
FT   MOD_RES     251    251       Phosphoserine (By similarity).
FT   MOD_RES     256    256       Phosphoserine (By similarity).
FT   MOD_RES     309    309       Phosphoserine.
FT   MOD_RES     310    310       Phosphothreonine.
FT   MOD_RES     332    332       Phosphotyrosine (By similarity).
FT   MOD_RES     343    343       Phosphoserine (By similarity).
FT   MOD_RES     370    370       Phosphothreonine (By similarity).
FT   MOD_RES     374    374       Phosphothreonine (By similarity).
FT   MOD_RES     379    379       Phosphothreonine (By similarity).
SQ   SEQUENCE   503 AA;  53399 MW;  FE4CA1920772BF3E CRC64;
     MTFAEDKTYK YIRDNHSKFC CVDVLEILPY LSCLTASDQD RLRASYRQIG NRDTLWGLFN
     NLQRRPGWVE VFIRALQICE LPGLADQVTR VYQSYLPPGT SLRSLEPLQL PDFPAAVSGP
     SAFAPGHNIP DHGLRETPSC PKPVQDTQPP ESPVENSEQL LQTNSGAVAR MSGGSLIPSP
     NQQALSPQPS REHQEQEPEL GGAHAANVAS VPIATYGPVS PTVSFQPLPR TALRTNLLSG
     VTVSALSADT SLSSSSTGSA FAKGAGDQAK AATCFSTTLT NSVTTSSVPS PRLVPVKTMS
     SKLPLSSKST AAMTSTVLTN TAPSKLPSNS VYAGTVPSRV PASVAKAPAN TIPPERNSKQ
     AKETPEGPAT KVTTGGNQTG PNSSIRSLHS GPEMSKPGVL VSQLDEPFSA CSVDLAISPS
     SSLVSEPNHG PEENEYSSFR IQVDESPSAD LLGSPEPLAT QQPQEEEEHC ASSMPWAKWL
     GATSALLAVF LAVMLYRSRR LAQ
//
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.
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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   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;
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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   CCD71_MOUSE             Reviewed;         433 AA.
AC   Q8VEG0; Q3UDX1;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Coiled-coil domain-containing protein 71;
GN   Name=Ccdc71;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; 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, Head, 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].
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).
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DR   EMBL; AK044601; BAC31997.1; -; mRNA.
DR   EMBL; AK086560; BAC39691.1; -; mRNA.
DR   EMBL; AK149878; BAE29140.1; -; mRNA.
DR   EMBL; AK161396; BAE36372.1; -; mRNA.
DR   EMBL; BC018518; AAH18518.1; -; mRNA.
DR   IPI; IPI00124561; -.
DR   RefSeq; NP_598505.1; NM_133744.4.
DR   UniGene; Mm.479964; -.
DR   ProteinModelPortal; Q8VEG0; -.
DR   PRIDE; Q8VEG0; -.
DR   Ensembl; ENSMUST00000061209; ENSMUSP00000057891; ENSMUSG00000049305.
DR   GeneID; 72454; -.
DR   KEGG; mmu:72454; -.
DR   UCSC; uc009rpq.1; mouse.
DR   CTD; 72454; -.
DR   MGI; MGI:1919704; Ccdc71.
DR   eggNOG; roNOG16279; -.
DR   GeneTree; ENSGT00510000049135; -.
DR   HOGENOM; HBG277984; -.
DR   HOVERGEN; HBG061228; -.
DR   InParanoid; Q8VEG0; -.
DR   OMA; AKVARTQ; -.
DR   OrthoDB; EOG41RPVS; -.
DR   PhylomeDB; Q8VEG0; -.
DR   NextBio; 336270; -.
DR   ArrayExpress; Q8VEG0; -.
DR   Bgee; Q8VEG0; -.
DR   CleanEx; MM_CCDC71; -.
DR   Genevestigator; Q8VEG0; -.
DR   GermOnline; ENSMUSG00000049305; Mus musculus.
PE   2: Evidence at transcript level;
KW   Coiled coil.
FT   CHAIN         1    433       Coiled-coil domain-containing protein 71.
FT                                /FTId=PRO_0000234422.
FT   COILED      260    330       Potential.
FT   COMPBIAS    293    372       Lys-rich.
FT   CONFLICT    312    312       R -> W (in Ref. 1; BAE29140).
SQ   SEQUENCE   433 AA;  46010 MW;  0DB9C0883F256315 CRC64;
     MSMVVQPVEE KAVHSWSRIS TAGKKALEEA LLVFNPMSQD LSATEAQLVA FLQGLRDDGF
     QPTILRSGDV YGYSSCTASP PSQTKLQART INPPATSLPK TAVSVPAGRT TLLPVPLSGR
     LAKGSTAALA KHATTNLLLS SLKQSSASNS SGTTVGFPAH LYPGVYPAMR LSVVLEALVP
     LKTPCLDVKH GAQSLQLSLA KSPLKVRKAS GNPKSKAPRK ITSKGLKHLT SKGPGAGLRR
     GAGTQSNGAQ RKGCSALGPK TVQAQASQTL IKAARAHASV AQTQTKTVRV RAKAKQAKPK
     AARAKAKAAV VRDKAKDKVI QAKAKAAQTK HKGKPKGSVQ TRTGRANRKN SSETVGRKRK
     KAEETKGLPP KKRARCVPRP PKVWLGPGTA KPRKSQTIKV DRKCSDDEVR QCAQQILRVN
     LSPVVWLQPL LPF
//
ID   CC50A_MOUSE             Reviewed;         364 AA.
AC   Q8VEK0; Q3TCJ5; Q3UDH8; Q8R0X6; Q8VEH1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Cell cycle control protein 50A;
DE   AltName: Full=Transmembrane protein 30A;
GN   Name=Tmem30a; Synonyms=Cdc50a, D9Wsu20e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; 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 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, 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 TYR-5, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.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 CDC50/LEM3 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH26136.1; Type=Erroneous initiation;
CC       Sequence=BAE41961.1; Type=Frameshift; Positions=33;
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DR   EMBL; AK077065; BAC36588.1; -; mRNA.
DR   EMBL; AK150071; BAE29283.1; -; mRNA.
DR   EMBL; AK159364; BAE35022.1; -; mRNA.
DR   EMBL; AK170697; BAE41961.1; ALT_FRAME; mRNA.
DR   EMBL; AK170171; BAE41615.1; -; mRNA.
DR   EMBL; BC018367; AAH18367.1; -; mRNA.
DR   EMBL; BC018491; AAH18491.1; -; mRNA.
DR   EMBL; BC026136; AAH26136.1; ALT_INIT; mRNA.
DR   IPI; IPI00387318; -.
DR   RefSeq; NP_598479.1; NM_133718.4.
DR   UniGene; Mm.355034; -.
DR   ProteinModelPortal; Q8VEK0; -.
DR   STRING; Q8VEK0; -.
DR   PRIDE; Q8VEK0; -.
DR   Ensembl; ENSMUST00000034878; ENSMUSP00000034878; ENSMUSG00000032328.
DR   GeneID; 69981; -.
DR   KEGG; mmu:69981; -.
DR   UCSC; uc009quw.1; mouse.
DR   CTD; 69981; -.
DR   MGI; MGI:106402; Tmem30a.
DR   eggNOG; roNOG15985; -.
DR   GeneTree; ENSGT00390000004660; -.
DR   HOGENOM; HBG525157; -.
DR   HOVERGEN; HBG055537; -.
DR   InParanoid; Q8VEK0; -.
DR   OMA; VTPCICT; -.
DR   OrthoDB; EOG473PRQ; -.
DR   PhylomeDB; Q8VEK0; -.
DR   NextBio; 330725; -.
DR   ArrayExpress; Q8VEK0; -.
DR   Bgee; Q8VEK0; -.
DR   CleanEx; MM_TMEM30A; -.
DR   Genevestigator; Q8VEK0; -.
DR   GermOnline; ENSMUSG00000032328; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR005045; DUF284_TM_euk.
DR   PANTHER; PTHR10926; DUF284_TM_euk; 1.
DR   Pfam; PF03381; CDC50; 1.
DR   PIRSF; PIRSF015840; DUF284_TM_euk; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Glycoprotein; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    364       Cell cycle control protein 50A.
FT                                /FTId=PRO_0000244470.
FT   TRANSMEM     50     70       Helical; (Potential).
FT   TRANSMEM    329    349       Helical; (Potential).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       5      5       Phosphotyrosine.
FT   CARBOHYD      4      4       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     98     98       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    297    297       N-linked (GlcNAc...) (Potential).
FT   CONFLICT     90     90       P -> H (in Ref. 1; BAE29283).
FT   CONFLICT    198    198       P -> L (in Ref. 2; AAH18491).
SQ   SEQUENCE   364 AA;  41061 MW;  F662D38B5B1E7E8F CRC64;
     MAMNYSAKDE VDGGPAGPPG GAAKTRRPDN TAFKQQRLPA WQPILTAGTV LPTFFIIGLI
     FIPIGIGIFV TSNNIREIEI DYTGTEPSSP CNKCLSPNVT SCACTINFTL KQSFEGNVFM
     YYGLSNFYQN HRRYVKSRDD SQLNGDPSAL LNPSKECEPY RRNEDRPIAP CGAIANSMFN
     DTLELYLVAN ESDPKPIPIP LKKKGIAWWT DKNVKFRNPP GKESLEEKFK DTIKPVNWHK
     AVYELDPEDE SNNGFINEDF IVWMRTAALP TFRKLYRLIE RRDDLHPTLP AGQYFLNITY
     NYPVHSFDGR KRMILSTISW MGGKNPFLGI AYITIGSISF LLGVVLLVIN HKYRNSSNTA
     DITI
//
ID   Q8VGJ7_MOUSE            Unreviewed;       309 AA.
AC   Q8VGJ7;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   SubName: Full=MCG142304;
DE   SubName: Full=Olfactory receptor 346;
DE   SubName: Full=Olfactory receptor MOR136-11;
DE   SubName: Full=Olfactory receptor Olfr346;
GN   Name=Olfr346; ORFNames=RP23-409M4.2-001, mCG_142304;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; 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   Leongamornlert D.;
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.
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   [8]
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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DR   EMBL; AY073150; AAL60813.1; -; Genomic_DNA.
DR   EMBL; AY317440; AAP70879.1; -; Genomic_DNA.
DR   EMBL; AL935058; CAM23576.1; -; Genomic_DNA.
DR   EMBL; CH466542; EDL08683.1; -; Genomic_DNA.
DR   IPI; IPI00127218; -.
DR   RefSeq; NP_667149.1; NM_146938.1.
DR   UniGene; Mm.223338; -.
DR   ProteinModelPortal; Q8VGJ7; -.
DR   PRIDE; Q8VGJ7; -.
DR   Ensembl; ENSMUST00000078854; ENSMUSP00000077897; ENSMUSG00000063915.
DR   GeneID; 258940; -.
DR   KEGG; mmu:258940; -.
DR   UCSC; uc008jlu.1; mouse.
DR   CTD; 258940; -.
DR   MGI; MGI:3030180; Olfr346.
DR   eggNOG; NOG46978; -.
DR   GeneTree; ENSGT00560000076842; -.
DR   HOGENOM; HBG755317; -.
DR   HOVERGEN; HBG017625; -.
DR   InParanoid; Q8VGJ7; -.
DR   OMA; LPIRAKD; -.
DR   OrthoDB; EOG40VVQG; -.
DR   PhylomeDB; Q8VGJ7; -.
DR   NextBio; 391241; -.
DR   ArrayExpress; Q8VGJ7; -.
DR   Bgee; Q8VGJ7; -.
DR   Genevestigator; Q8VGJ7; -.
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   309 AA;  34559 MW;  07A5756936C7612E CRC64;
     MRMDNESTVS EFILLGLPIR AKDQAVYSAL ILAMYLTTVL GNLLIILLIR LDPHLHTPMY
     FFLSHLALTD ISFSSVTVPR MLVNMLTQSQ SISYTGCISQ VYFFIVFGSI DSFLLPSMAY
     DRYVAICHPL HYTLIMNLNL CVLLVVVSWA LSLVNALVHT LLLARLSHFR NNIIPHYFCD
     LSALLKLSSS DTSINELVIL VLGNVVITLP FICILVSYGY IGVTILKTPS TKGIRKALST
     CGSHLCVVSL YYGSVIGLYC VPSSNNTNDK DAIVAMMYTV VTPMLNPFIY SLRNRDMKRA
     LRNILSRKK
//
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;
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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   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   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   -----------------------------------------------------------------------
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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   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   ZCH14_MOUSE             Reviewed;         956 AA.
AC   Q8VIG0; Q80TX3; Q91VU4;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Zinc finger CCHC domain-containing protein 14;
DE   AltName: Full=BDG-29;
GN   Name=Zcchc14; Synonyms=Kiaa0579;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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   Kawasoe T., Furukawa Y., Daigo Y., Ishiguro H., Nishiwaki T.,
RA   Fujita M., Nagasawa Y., Miyoshi Y., Nakamura Y.;
RT   "Isolation and characterization of a novel downstream gene of beta-
RT   catenin.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 704-944 (ISOFORM 2).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 790-956 (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=Q8VIG0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VIG0-2; Sequence=VSP_013844;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8VIG0-3; Sequence=VSP_013845;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 CCHC-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH09020.1; Type=Erroneous initiation;
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DR   EMBL; AB030244; BAB83130.1; -; mRNA.
DR   EMBL; BC009020; AAH09020.1; ALT_INIT; mRNA.
DR   EMBL; AK122315; BAC65597.1; -; mRNA.
DR   IPI; IPI00129314; -.
DR   IPI; IPI00403334; -.
DR   IPI; IPI00606457; -.
DR   RefSeq; NP_543131.1; NM_080855.2.
DR   UniGene; Mm.103202; -.
DR   UniGene; Mm.475749; -.
DR   ProteinModelPortal; Q8VIG0; -.
DR   SMR; Q8VIG0; 100-208, 305-362.
DR   PhosphoSite; Q8VIG0; -.
DR   PRIDE; Q8VIG0; -.
DR   Ensembl; ENSMUST00000046386; ENSMUSP00000040360; ENSMUSG00000061410.
DR   Ensembl; ENSMUST00000108906; ENSMUSP00000104534; ENSMUSG00000061410.
DR   GeneID; 142682; -.
DR   KEGG; mmu:142682; -.
DR   UCSC; uc009nrx.1; mouse.
DR   CTD; 142682; -.
DR   MGI; MGI:2159407; Zcchc14.
DR   GeneTree; ENSGT00520000055637; -.
DR   HOVERGEN; HBG080706; -.
DR   OrthoDB; EOG4CJVGJ; -.
DR   PhylomeDB; Q8VIG0; -.
DR   NextBio; 370053; -.
DR   ArrayExpress; Q8VIG0; -.
DR   Bgee; Q8VIG0; -.
DR   CleanEx; MM_ZCCHC14; -.
DR   Genevestigator; Q8VIG0; -.
DR   GermOnline; ENSMUSG00000061410; Mus musculus.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   InterPro; IPR001683; Phox.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   InterPro; IPR013084; Znf_CCH_retrovir.
DR   InterPro; IPR001878; Znf_CCHC.
DR   Gene3D; G3DSA:3.30.1520.10; PX; 1.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Gene3D; G3DSA:4.10.60.10; Znf_CCH_retrovir; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF64268; PX; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Metal-binding; Phosphoprotein; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    956       Zinc finger CCHC domain-containing
FT                                protein 14.
FT                                /FTId=PRO_0000150976.
FT   ZN_FING     913    930       CCHC-type.
FT   COMPBIAS     30     49       Gly-rich.
FT   COMPBIAS    206    211       Poly-Ser.
FT   COMPBIAS    427    432       Poly-Ser.
FT   COMPBIAS    693    769       Ser-rich.
FT   COMPBIAS    770    776       His-rich.
FT   COMPBIAS    779    790       Poly-Pro.
FT   MOD_RES       3      3       Phosphoserine (By similarity).
FT   MOD_RES     333    333       Phosphoserine (By similarity).
FT   VAR_SEQ     939    956       GTFRLKYAPPAESLDSTD -> EHFIKP (in isoform
FT                                2).
FT                                /FTId=VSP_013844.
FT   VAR_SEQ     940    956       TFRLKYAPPAESLDSTD -> KQVRGSHVLLALWLVAPERR
FT                                KQETCFVLFFKMIFIHTVFFFFFFKIYLFIIICTYTEAVFR
FT                                CTRRGCQTSSRVVVSHHVVAGI (in isoform 3).
FT                                /FTId=VSP_013845.
SQ   SEQUENCE   956 AA;  99835 MW;  9B02F53EFBD5AC6F CRC64;
     MASNHPAFSF HQKQVLRQEL TQIQSSLNSG GGGGGGGGGG GKSAPGPSGA LPTCSACHKM
     APRTETPVSS ISNSLENALH TSAHSTEESL PKRPLGKHGK VSVEKIDLKG LSHTKNDRSV
     ECSFEVLWSD SSITSVTKSS SEVTEFISKL SQLCPEENLD KLIPCLAGPD SFYVERNHVD
     LEAGLRFLAS APSHTLKHDH VRKFFSSSSP SQQLQSPSPG NPSLPKVGAV MGVSGRPVCG
     VAGIPSSQSS AQHHLQHSAS TSASLPHCSH TGGTGSALAY RTQVDNSPTI LMPSSLQTPQ
     PQEQNGILDW LRKLRLHKYY PVFKQLTMEK FLSLTEEDLN KFESLTMGAK KKLKTQLELE
     KEKSERRCLN SSAPSLVTSS GVARVTPTSH VGPVQPGRSS SHASELRVEV EPPAHQLPRE
     GSSSEYSSSS SSPMGVQVRE ESSDSAEESD RRVDIHVEGT EKEKPVMLLA HFPSSSARPT
     AQVLPVQNET GSSPAAHHPL PPQLMPAASH LAPVRMLNSV HKSDRGGADV KLLSSSVHSL
     LSLEERNKGP GPRSGTKVDK SFGGAVLDPL PSAAPHPPGQ GLSGLVENNA VSPTVSFGPR
     AKVVHAATLD RVLKTAQQPA LTVESSSATT GTPSTVLHVA RPPIKLLLAS SVPADAAIAG
     QTSCPNNGQI SVPPAIMNPR TALYTANTKV AFSAVSSVPV GPLQGSFCAN SNTASPSSHP
     STSFASMASL PSCPAPSSSP ALSSVPESSF YSGGAGSSSP GNIPASSQSH HHHHHHQQPP
     APPQPAPPPP GCIVCTSCGC SGSCGSNGLT VSYANYFQHP FSGPSVLTFP FLPFSPMCGN
     GYVSTQQYGG GSAFPVVHTP YNGSVTPDPV LGGQSTFAVP PMQNFMAGTA GVYQAQGLVG
     STNGSSHKKS GNLSCYNCGA TGHRAQDCKQ PSMDFNRQGT FRLKYAPPAE SLDSTD
//
ID   SFPQ_MOUSE              Reviewed;         699 AA.
AC   Q8VIJ6; A2A7U6; Q9ERW2;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Splicing factor, proline- and glutamine-rich;
DE   AltName: Full=DNA-binding p52/p100 complex, 100 kDa subunit;
DE   AltName: Full=Polypyrimidine tract-binding protein-associated-splicing factor;
DE            Short=PSF;
DE            Short=PTB-associated-splicing factor;
GN   Name=Sfpq;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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=Bone marrow;
RX   MEDLINE=21406000; PubMed=11514619;
RA   Shav-Tal Y., Cohen M., Lapter S., Dye B., Patton J.G.,
RA   Vandekerckhove J., Zipori D.;
RT   "Nuclear relocalization of the pre-mRNA splicing factor PSF during
RT   apoptosis involves hyperphosphorylation, masking of antigenic
RT   epitopes, and changes in protein interactions.";
RL   Mol. Biol. Cell 12:2328-2340(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 [MRNA] OF 198-580, AND PROTEIN SEQUENCE OF 20-30;
RP   47-55 AND 210-238.
RC   TISSUE=Bone marrow;
RX   MEDLINE=20465090; PubMed=11008015; DOI=10.1016/S0301-472X(00)00510-5;
RA   Shav-Tal Y., Lee B., Bar-Haim S., Vandekerckhove J., Zipori D.;
RT   "Enhanced proteolysis of pre-mRNA splicing factors in myeloid cells.";
RL   Exp. Hematol. 28:1029-1038(2000).
RN   [5]
RP   PROTEIN SEQUENCE OF 291-306; 312-322; 358-368 AND 472-485, 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 PSPC1.
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   [7]
RP   INTERACTION WITH PITX3 AND 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: DNA- and RNA binding protein, involved in several
CC       nuclear processes. Essential pre-mRNA splicing factor required
CC       early in spliceosome formation and for splicing catalytic step II,
CC       probably as an heteromer with NONO. Binds to pre-mRNA in
CC       spliceosome C complex, and specifically binds to intronic
CC       polypyrimidine tracts. Interacts with U5 snRNA, probably by
CC       binding to a purine-rich sequence located on the 3' side of U5
CC       snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and
CC       polyadenylation process as component of a snRNP-free complex with
CC       SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play
CC       a role in nuclear retention of defective RNAs. SFPQ may be
CC       involved in homologous DNA pairing; in vitro, promotes the
CC       invasion of ssDNA between a duplex DNA and produces a D-loop
CC       formation. The SFPQ-NONO heteromer may be involved in DNA
CC       unwinding by modulating the function of topoisomerase I/TOP1; in
CC       vitro, stimulates dissociation of TOP1 from DNA after cleavage and
CC       enhances its jumping between separate DNA helices. The SFPQ-NONO
CC       heteromer may be involved in DNA nonhomologous end joining (NHEJ)
CC       required for double-strand break repair and V(D)J recombination
CC       and may stabilize paired DNA ends; in vitro, the complex strongly
CC       stimulates DNA end joining, binds directly to the DNA substrates
CC       and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to
CC       establish a functional preligation complex. SFPQ is involved in
CC       transcriptional regulation. Transcriptional repression is probably
CC       mediated by an interaction of SFPQ with SIN3A and subsequent
CC       recruitment of histone deacetylases (HDACs). The SFPQ-NONO-NR5A1
CC       complex binds to the CYP17 promoter and regulates basal and cAMP-
CC       dependent transcriptional avtivity. SFPQ isoform Long binds to the
CC       DNA binding domains (DBD) of nuclear hormone receptors, like RXRA
CC       and probably THRA, and acts as transcriptional corepressor in
CC       absence of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3'
CC       in the insulin-like growth factor response element (IGFRE) and
CC       inhibits IGF-I-stimulated transcriptional activity (By
CC       similarity).
CC   -!- SUBUNIT: Monomer and component of the SFPQ-NONO complex, which is
CC       probably a heterotetramer of two 52 kDa (NONO) and two 100 kDa
CC       (SFPQ) subunits. SFPQ is a component of spliceosome and U5.4/6
CC       snRNP complexes. Interacts with SNRPA/U1A. Component of a snRNP-
CC       free complex with SNRPA/U1A. Part of complex consisting of SFPQ,
CC       NONO and MATR3. Interacts with polypyrimidine tract-binding
CC       protein 1/PTB. Part of a complex consisting of SFPQ, NONO and
CC       NR5A1. Interacts with RXRA, probably THRA, and SIN3A. Interacts
CC       with TOP1. Part of a complex consisting of SFPQ, NONO and TOP1.
CC       Interacts with SNRNP70 in apoptotic cells (By similarity).
CC       Interacts with PSPC1. Interacts with RNF43 (By similarity).
CC       Interacts with PITX3 and NR4A2/NURR1.
CC   -!- SUBCELLULAR LOCATION: Nucleus matrix (By similarity).
CC       Note=Predominantly in nuclear matrix (By similarity).
CC   -!- PTM: Phosphorylated on multiple serine and threonine residues
CC       during apoptosis (By similarity).
CC   -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
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DR   EMBL; AY034062; AAK60397.1; -; mRNA.
DR   EMBL; AL606985; CAM15587.1; -; Genomic_DNA.
DR   EMBL; BC089305; AAH89305.1; -; mRNA.
DR   EMBL; AF272847; AAG17365.1; -; mRNA.
DR   IPI; IPI00129430; -.
DR   RefSeq; NP_076092.1; NM_023603.3.
DR   UniGene; Mm.257276; -.
DR   ProteinModelPortal; Q8VIJ6; -.
DR   SMR; Q8VIJ6; 282-441.
DR   STRING; Q8VIJ6; -.
DR   PhosphoSite; Q8VIJ6; -.
DR   REPRODUCTION-2DPAGE; Q8VIJ6; -.
DR   PRIDE; Q8VIJ6; -.
DR   Ensembl; ENSMUST00000030623; ENSMUSP00000030623; ENSMUSG00000028820.
DR   GeneID; 71514; -.
DR   KEGG; mmu:71514; -.
DR   UCSC; uc008utz.1; mouse.
DR   CTD; 71514; -.
DR   MGI; MGI:1918764; Sfpq.
DR   HOGENOM; HBG126336; -.
DR   HOVERGEN; HBG009801; -.
DR   InParanoid; Q8VIJ6; -.
DR   OMA; APGGHPK; -.
DR   OrthoDB; EOG4RNB8S; -.
DR   PhylomeDB; Q8VIJ6; -.
DR   NextBio; 333919; -.
DR   ArrayExpress; Q8VIJ6; -.
DR   Bgee; Q8VIJ6; -.
DR   Genevestigator; Q8VIJ6; -.
DR   GermOnline; ENSMUSG00000028820; Mus musculus.
DR   GO; GO:0016363; C:nuclear matrix; 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:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; 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; 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; Direct protein sequencing; DNA damage;
KW   DNA repair; DNA-binding; Methylation; mRNA processing; mRNA splicing;
KW   Nucleus; Phosphoprotein; Repeat; Repressor; RNA-binding;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    699       Splicing factor, proline- and glutamine-
FT                                rich.
FT                                /FTId=PRO_0000081910.
FT   REPEAT        9     11       1.
FT   REPEAT       19     21       2.
FT   REPEAT       25     27       3.
FT   DOMAIN      289    361       RRM 1.
FT   DOMAIN      363    444       RRM 2.
FT   REGION        9     27       3 X 3 AA repeats of R-G-G.
FT   COMPBIAS     10    258       Gln/Glu/Pro-rich.
FT   COMPBIAS     10     15       Poly-Gly.
FT   COMPBIAS     20     27       Poly-Gly.
FT   COMPBIAS     54     63       Poly-Pro.
FT   COMPBIAS     65     69       Poly-Gln.
FT   COMPBIAS     96    100       Poly-Pro.
FT   COMPBIAS    158    161       Poly-Pro.
FT   COMPBIAS    178    182       Poly-Pro.
FT   COMPBIAS    563    566       Poly-Arg.
FT   COMPBIAS    605    608       Poly-Gly.
FT   COMPBIAS    627    633       Poly-Gly.
FT   MOD_RES       7      7       Omega-N-methylated arginine (By
FT                                similarity).
FT   MOD_RES       9      9       Omega-N-methylated arginine (By
FT                                similarity).
FT   MOD_RES      19     19       Omega-N-methylated arginine (By
FT                                similarity).
FT   MOD_RES      25     25       Omega-N-methylated arginine (By
FT                                similarity).
FT   MOD_RES      33     33       Phosphoserine (By similarity).
FT   MOD_RES     265    265       Phosphoserine (By similarity).
FT   MOD_RES     275    275       Phosphoserine (By similarity).
FT   MOD_RES     306    306       N6,N6-dimethyllysine (By similarity).
FT   MOD_RES     311    311       N6-acetyllysine (By similarity).
FT   MOD_RES     330    330       N6-acetyllysine (By similarity).
FT   MOD_RES     371    371       Phosphoserine (By similarity).
FT   MOD_RES     413    413       N6-acetyllysine (By similarity).
FT   MOD_RES     464    464       N6-acetyllysine (By similarity).
FT   MOD_RES     563    563       Dimethylated arginine (By similarity).
FT   MOD_RES     673    673       Omega-N-methylarginine (By similarity).
FT   MOD_RES     679    679       Phosphothreonine (By similarity).
FT   MOD_RES     685    685       Dimethylated arginine (By similarity).
FT   CONFLICT     47     47       M -> Q (in Ref. 4; AA sequence).
FT   CONFLICT    546    546       S -> N (in Ref. 4; AAG17365).
SQ   SEQUENCE   699 AA;  75442 MW;  714F786264C63AA0 CRC64;
     MSRDRFRSRG GGGGGFHRRG GGGGRGGLHD FRSPPPGMGL NQNRGPMGPG PGGPKPPLPP
     PPPHQQQQQP PPQQPPPQQP PPHQQPPPHQ PPHQQPPPPP QESKPVVPQG PGSAPGVSSA
     PPPAVSAPPA NPPTTGAPPG PGPTPTPPPA VPSTAPGPPP PSTPSSGVST TPPQTGGPPP
     PPAGGAGPGP KPGPGPGGPK GGKMPGGPKP GGGPGMGAPG GHPKPPHRGG GEPRGGRQHH
     APYHQQHHQG PPPGGPGPRT EEKISDSEGF KANLSLLRRP GEKTYTQRCR LFVGNLPADI
     TEDEFKRLFA KYGEPGEVFI NKGKGFGFIK LESRALAEIA KAELDDTPMR GRQLRVRFAT
     HAAALSVRNL SPYVSNELLE EAFSQFGPIE RAVVIVDDRG RSTGKGIVEF ASKPAARKAF
     ERCSEGVFLL TTTPRPVIVE PLEQLDDEDG LPEKLAQKNP MYQKERETPP RFAQHGTFEY
     EYSQRWKSLD EMEKQQREQV EKNMKDAKDK LESEMEDAYH EHQANLLRQD LMRRQEELRR
     MEELHSQEMQ KRKEMQLRQE EERRRREEEM MIRQREMEEQ MRRQREESYS RMGYMDPRER
     DMRMGGGGTM NMGDPYGSGG QKFPPLGGGG GIGYEANPGV PPATMSGSMM GSDMRTERFG
     QGGAGPVGGQ GPRGMGPGTP AGYGRGREEY EGPNKKPRF
//
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;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   ABCA7_MOUSE             Reviewed;        2159 AA.
AC   Q91V24; Q9JL36;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=ATP-binding cassette sub-family A member 7;
GN   Name=Abca7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; 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=DBA/2; TISSUE=Lymphoma;
RX   MEDLINE=21328888; PubMed=11435699;
RA   Broccardo C., Osorio J., Luciani M.-F., Schriml L.M., Prades C.,
RA   Shulenin S., Arnould I., Naudin L., Lafargue C., Rosier M., Jordan B.,
RA   Mattei M.-G., Dean M., Denefle P., Chimini G.;
RT   "Comparative analysis of the promoter structure and genomic
RT   organization of the human and mouse ABCA7 gene encoding a novel ABCA
RT   transporter.";
RL   Cytogenet. Cell Genet. 92:264-270(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1920-2159.
RC   STRAIN=C57BL/6J;
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   [3]
RP   FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=12917409; DOI=10.1074/jbc.M307831200;
RA   Wang N., Lan D., Gerbod-Giannone M., Linsel-Nitschke P., Jehle A.W.,
RA   Chen W., Martinez L.O., Tall A.R.;
RT   "ATP-binding cassette transporter A7 (ABCA7) binds apolipoprotein A-I
RT   and mediates cellular phospholipid but not cholesterol efflux.";
RL   J. Biol. Chem. 278:42906-42912(2003).
RN   [4]
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).
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=15550377; DOI=10.1074/jbc.M412602200;
RA   Kim W.S., Fitzgerald M.L., Kang K., Okuhira K., Bell S.A.,
RA   Manning J.J., Koehn S.L., Lu N., Moore K.J., Freeman M.W.;
RT   "Abca7 null mice retain normal macrophage phosphatidylcholine and
RT   cholesterol efflux activity despite alterations in adipose mass and
RT   serum cholesterol levels.";
RL   J. Biol. Chem. 280:3989-3995(2005).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16908670; DOI=10.1083/jcb.200601030;
RA   Jehle A.W., Gardai S.J., Li S., Linsel-Nitschke P., Morimoto K.,
RA   Janssen W.J., Vandivier R.W., Wang N., Greenberg S., Dale B.M.,
RA   Qin C., Henson P.M., Tall A.R.;
RT   "ATP-binding cassette transporter A7 enhances phagocytosis of
RT   apoptotic cells and associated ERK signaling in macrophages.";
RL   J. Cell Biol. 174:547-556(2006).
CC   -!- FUNCTION: Plays a role in phagocytosis by macrophages of apoptotic
CC       cells. Binds APOA1 and may function in apolipoprotein-mediated
CC       phospholipid efflux from cells. May also mediate cholesterol
CC       efflux. May regulate cellular ceramide homeostasis during
CC       keratinocytes differentiation.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Golgi apparatus membrane; Multi-pass membrane protein. Endosome
CC       membrane; Multi-pass membrane protein. Note=Localizes to cell
CC       membrane ruffles and phagocytic cups of macrophages stimulated
CC       with C1q or apoptotic cells. Localizes to the cytoplasm of resting
CC       macrophages, probably in Golgi and endosomes. Localizes to the
CC       apical brush border of cells in the proximal tubules of kidney.
CC   -!- TISSUE SPECIFICITY: Widely expressed with higher expression in
CC       brain, lung, adrenal gland and spleen (at protein level). Highly
CC       expressed in spleen and hematopoietic tissues.
CC   -!- DEVELOPMENTAL STAGE: Widely expressed during embryogenesis.
CC   -!- INDUCTION: Down-regulated by digoxin.
CC   -!- DISRUPTION PHENOTYPE: According to PubMed:16908670, mice are not
CC       viable and heterozygous knockout mice display impaired
CC       phagocytosis of apoptotic cells. Depletion of Abca7 in macrophages
CC       by RNAi reduces phagocytosis of apoptotic cells. According to
CC       PubMed:15550377, mice are viable and females have less visceral
CC       fat and lower total serum and high density lipoprotein cholesterol
CC       level.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA
CC       family.
CC   -!- SIMILARITY: Contains 2 ABC transporter domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF31434.1; Type=Frameshift; Positions=Several;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF287141; AAK56862.1; -; mRNA.
DR   EMBL; AF287142; AAK56863.1; -; Genomic_DNA.
DR   EMBL; AF213395; AAF31434.1; ALT_FRAME; mRNA.
DR   IPI; IPI00125970; -.
DR   RefSeq; NP_038878.1; NM_013850.1.
DR   UniGene; Mm.103351; -.
DR   ProteinModelPortal; Q91V24; -.
DR   SMR; Q91V24; 803-1029, 1806-2033.
DR   STRING; Q91V24; -.
DR   PhosphoSite; Q91V24; -.
DR   PRIDE; Q91V24; -.
DR   Ensembl; ENSMUST00000043866; ENSMUSP00000043090; ENSMUSG00000035722.
DR   GeneID; 27403; -.
DR   KEGG; mmu:27403; -.
DR   UCSC; uc007gba.1; mouse.
DR   CTD; 27403; -.
DR   MGI; MGI:1351646; Abca7.
DR   GeneTree; ENSGT00560000076613; -.
DR   HOVERGEN; HBG050436; -.
DR   InParanoid; Q91V24; -.
DR   OMA; CHFPNKP; -.
DR   PhylomeDB; Q91V24; -.
DR   NextBio; 305402; -.
DR   ArrayExpress; Q91V24; -.
DR   Bgee; Q91V24; -.
DR   Genevestigator; Q91V24; -.
DR   GermOnline; ENSMUSG00000035722; Mus musculus.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0010008; C:endosome 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0005548; F:phospholipid transporter activity; IDA:MGI.
DR   GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0033700; P:phospholipid efflux; IDA:MGI.
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; Cell membrane; Disulfide bond; Endosome; Glycoprotein;
KW   Golgi apparatus; Membrane; Nucleotide-binding; Phagocytosis; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1   2159       ATP-binding cassette sub-family A member
FT                                7.
FT                                /FTId=PRO_0000250675.
FT   TRANSMEM     22     42       Helical; (Potential).
FT   TOPO_DOM     43    546       Extracellular (By similarity).
FT   TRANSMEM    547    567       Helical; (Potential).
FT   TRANSMEM    590    610       Helical; (Potential).
FT   TRANSMEM    623    643       Helical; (Potential).
FT   TRANSMEM    652    672       Helical; (Potential).
FT   TRANSMEM    678    698       Helical; (Potential).
FT   TRANSMEM    732    752       Helical; (Potential).
FT   TRANSMEM    846    866       Helical; (Potential).
FT   TRANSMEM   1246   1266       Helical; (Potential).
FT   TOPO_DOM   1267   1551       Extracellular (By similarity).
FT   TRANSMEM   1552   1572       Helical; (Potential).
FT   TRANSMEM   1598   1618       Helical; (Potential).
FT   TRANSMEM   1635   1655       Helical; (Potential).
FT   TRANSMEM   1663   1683       Helical; (Potential).
FT   TRANSMEM   1743   1763       Helical; (Potential).
FT   DOMAIN      804   1035       ABC transporter 1.
FT   DOMAIN     1807   2039       ABC transporter 2.
FT   NP_BIND     838    845       ATP 1 (Potential).
FT   NP_BIND    1841   1848       ATP 2 (Potential).
FT   CARBOHYD    309    309       N-linked (GlcNAc...) (Potential).
FT   DISULFID     75    222       By similarity.
FT   DISULFID   1359   1373       By similarity.
FT   CONFLICT   1944   1944       N -> D (in Ref. 2; AAF31434).
FT   CONFLICT   2004   2004       A -> R (in Ref. 2; AAF31434).
FT   CONFLICT   2069   2069       L -> M (in Ref. 2; AAF31434).
SQ   SEQUENCE   2159 AA;  236884 MW;  CD2BE3FE0D8B822B CRC64;
     MALGTQLMLL LWKNYTYRRR QPIQLLVELL WPLFLFFILV AVRHSHPPLE HHECHFPNKP
     LPSAGTVPWL QGLVCNVNNS CFQHPTPGEK PGVLSNFKDS LISRLLADTR TVLGGHSIQD
     MLDALGKLIP VLRAVGGGAR PQESDQPTSQ GSVTKLLEKI LQRASLDPVL GQAQDSMRKF
     SDAIRDLAQE LLTLPSLMEL RALLRRPRGS AGSLELVSEA LCSTKGPSSP GGLSLNWYEA
     NQLNEFMGPE VAPALPDNSL SPACSEFVGT LDDHPVSRLL WRRLKPLILG KILFAPDTNF
     TRKLMAQVNQ TFEELALLRD LHELWGVLGP QIFNFMNDST NVAMLQRLLD VGGTGQRQQT
     PRAQKKLEAI KDFLDPSRGG YSWREAHADM GRLAGILGQM MECVSLDKLE AVPSEEALVS
     RALELLGERR LWAGIVFLSP EHPLDPSELS SPALSPGHLR FKIRMDIDDV TRTNKIRDKF
     WDPGPSADPF MDLRYVWGGF VYLQDLLEQA AVRVLGGGNS RTGLYLQQMP HPCYVDDVFL
     RVLSRSLPLF LTLAWIYSVA LTVKAVVREK ETRLRETMRA MGLSRAVLWL GWFLSCLGPF
     LVSAALLVLV LKLGNILPYS HPVVIFLFLA AFAVATVAQS FLLSAFFSRA NLAAACGGLA
     YFALYLPYVL CVAWRERLHL GGLLAASLLS PVAFGFGCES LALLEEQGDG AQWHNLGTGP
     AEDVFSLAQV SAFLLLDAVI YGLALWYLEA VCPGQYGIPE PWNFPFRRSY WCGPGPPKSS
     VLAPAPQDPK VLVEEPPLGL VPGVSIRGLK KHFRGCPQPA LQGLNLDFYE GHITAFLGHN
     GAGKTTTLSI LSGLFPPSSG SASILGHDVQ TNMAAIRPHL GICPQYNVLF DMLTVEEHVW
     FYGRLKGVSA AAMGPERERL IRDVGLTLKR DTQTRHLSGG MQRKLSVAIA FVGGSRVVIM
     DEPTAGVDPA SRRGIWELLL KYREGRTLIL STHHLDEAEL LGDRVAMVAG GSLCCCGSPL
     FLRRHLGCGY YLTLVKSSQS LVTHDAKGDS EDPRREKKSD GNGRTSDTAF TRGTSDKSNQ
     APAPGAVPIT PSTARILELV QQHVPGAQLV EDLPHELLLV LPYAGALDGS FAMVFQELDQ
     QLELLGLTGY GISDTNLEEI FLKVVEDAHR EGGDSRPQLH LRTCTPQPPT GPEASVLENG
     ELAPQGLAPN AAQVQGWTLT CQQLRALLHK RFLLARRSRR GLFAQVVLPA LFVGLALFFS
     LIVPPFGQYP PLQLSPAMYG PQVSFFSEDA PGDPNRMKLL EALLGEAGLQ EPSMQDKDAR
     GSECTHSLAC YFTVPEVPPD VASILASGNW TPESPSPACQ CSQPGARRLL PDCPAGAGGP
     PPPQAVAGLG EVVQNLTGRN VSDFLVKTYP SLVRRGLKTK KWVDEVRYGG FSLGGRDPDL
     PTGHEVVRTL AEIRALLSPQ PGNALDRILN NLTQWALGLD ARNSLKIWFN NKGWHAMVAF
     VNRANNGLLH ALLPSGPVRH AHSITTLNHP LNLTKEQLSE ATLIASSVDV LVSICVVFAM
     SFVPASFTLV LIEERITRAK HLQLVSGLPQ TLYWLGNFLW DMCNYLVAVC IVVFIFLAFQ
     QRAYVAPENL PALLLLLLLY GWSITPLMYP ASFFFSVPST AYVVLTCINL FIGINSSMAT
     FVLELLSDQN LQEVSRILKQ VFLIFPHFCL GRGLIDMVRN QAMADAFERL GDKQFQSPLR
     WDIIGKNLLA MMAQGPLFLL ITLLLQHRNR LLPQSKPRLL PPLGEEDEDV AQERERVTKG
     ATQGDVLVLR DLTKVYRGQR NPAVDRLCLG IPPGECFGLL GVNGAGKTST FRMVTGDTLP
     SSGEAVLAGH NVAQERSAAH RSMGYCPQSD AIFDLLTGRE HLELFARLRG VPEAQVAQTA
     LSGLVRLGLP SYADRPAGTY SGGNKRKLAT ALALVGDPAV VFLDEPTTGM DPSARRFLWN
     SLLSVVREGR SVVLTSHSME ECEALCTRLA IMVNGRFRCL GSSQHLKGRF GAGHTLTLRV
     PPDQPEPAIA FIRITFPGAE LREVHGSRLR FQLPPGGRCT LTRVFRELAA QGRAHGVEDF
     SVSQTTLEEV FLYFSKDQGE EEESSRQEAE EEEVSKPGRQ HPKRVSRFLE DPSSVETMI
//
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   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   -----------------------------------------------------------------------
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).
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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   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.
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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   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.
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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   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   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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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   Q91XY3_MOUSE            Unreviewed;       932 AA.
AC   Q91XY3;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   SubName: Full=MCG133388, isoform CRA_w;
DE   SubName: Full=Protocadherin gamma A5;
DE   SubName: Full=Protocadherin gamma subfamily A, 5;
GN   Name=Pcdhga5; 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   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, 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; BC057404; AAH57404.1; -; mRNA.
DR   EMBL; AY013799; AAK26088.1; -; mRNA.
DR   EMBL; CH466528; EDL10140.1; -; Genomic_DNA.
DR   IPI; IPI00129672; -.
DR   RefSeq; NP_291066.1; NM_033588.4.
DR   UniGene; Mm.247203; -.
DR   HSSP; P09803; 1FF5.
DR   ProteinModelPortal; Q91XY3; -.
DR   SMR; Q91XY3; 26-137, 140-339, 355-554.
DR   STRING; Q91XY3; -.
DR   PhosphoSite; Q91XY3; -.
DR   PRIDE; Q91XY3; -.
DR   GeneID; 93713; -.
DR   KEGG; mmu:93713; -.
DR   UCSC; uc008eqr.1; mouse.
DR   CTD; 93713; -.
DR   MGI; MGI:1935217; Pcdhga5.
DR   HOVERGEN; HBG054878; -.
DR   NextBio; 351519; -.
DR   Genevestigator; Q91XY3; -.
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-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;  101406 MW;  5D3193C182801643 CRC64;
     MADPPRRWIC NDLLTFFMLL GTLCAPGKGQ IRYSVREELD KGSFVGNISK DLGLEPRELA
     ERGVRIISRG RSQLFSLNPR GGSLVTAGRI DREELCVQSS PCLVSFNILV ENKMKIYGVE
     VEILDINDNF PRFRDEELKV KVNENAAAGT RLVLPFARDG DVGVNSLQGY KLSSNRHFSL
     DVKSGSDGQK HPELVLEQPL DREKESAHDL VLTALDGGNP VLSSTVHISV TVLDANDNAP
     LFTQSEYRVS VPENTPVGTR LLTLTATDAD EGINAKLTFS FRNEEDKISE TFQLDSNLGE
     ISTIQSLDYE ESRFYLMEVV AQDGGALLAS AKVLVTVQDV NDNAPEVILT SLTSSVSEDC
     LPGTIIALFS VHDADSGENG EISCSIPKNL PFKLEKSVDN YYHLLTTRAL DREETSDYNI
     TVTVVDRGTP PLSTENHISL KVADINDNPP TFSRPFYSTS ISENNPRGVS IFSVYAYDAD
     SGDNAQVTYS LAENTFQEVP VSSYVSINSD TGVLYALQSF DYEHLRDLQL LVTAKDSGTP
     PLSSNVSMSL FVLDQNDNIP EILYPTIPTD GSTGVELAPR SAEPGYLVTK VVAVDKDSGQ
     NAWLSYRLLK ASEPGLFSIG LHTGEVCTAR ALLDRDVLKQ SLVVAVQDHG QPPLSATVTL
     TIAVGDSIPD VLTDLGNHNT LAEPQDSDLT LYLVVSVAVV SCVFLGFVTV LLALRLRHWH
     MSRLLQTSTG RLADMPASHF VGMDGVQAYL QTYSHEISLT TDSKKSHLIF PQPNYADRLI
     SEESCEKSEP LLIPHNIHTH KEEPGDAQQA PPNTDWRFSQ AQRPGTSGSQ NGDETGTWPN
     NQFDTEMLQA MILASASEAA DGSSTLGGGA GTMGLSARYG PQFTLQHVPD YRQNVYIPGS
     NATLTNAAGK RDGKAPAGGN GNKKKSGKKE KK
//
ID   Q91XY8_MOUSE            Unreviewed;       933 AA.
AC   Q91XY8;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   SubName: Full=Protocadherin gamma A11;
DE   SubName: Full=Protocadherin gamma subfamily A, 11;
GN   Name=Pcdhga11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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; BC059837; AAH59837.1; -; mRNA.
DR   EMBL; BC064675; AAH64675.1; -; mRNA.
DR   EMBL; AY013794; AAK26083.1; -; mRNA.
DR   IPI; IPI00129686; -.
DR   RefSeq; NP_291072.1; NM_033594.2.
DR   UniGene; Mm.247203; -.
DR   HSSP; P15116; 1NCJ.
DR   ProteinModelPortal; Q91XY8; -.
DR   SMR; Q91XY8; 25-138, 232-345, 354-665.
DR   PhosphoSite; Q91XY8; -.
DR   PRIDE; Q91XY8; -.
DR   Ensembl; ENSMUST00000061279; ENSMUSP00000058362; ENSMUSG00000023036.
DR   GeneID; 93723; -.
DR   KEGG; mmu:93723; -.
DR   UCSC; uc008erb.1; mouse.
DR   CTD; 93723; -.
DR   GeneTree; ENSGT00560000076625; -.
DR   HOVERGEN; HBG054878; -.
DR   NextBio; 351551; -.
DR   ArrayExpress; Q91XY8; -.
DR   Bgee; Q91XY8; -.
DR   Genevestigator; Q91XY8; -.
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   933 AA;  101124 MW;  B6F0736CA125FD11 CRC64;
     MANQSQRLDR RALIPLCIFL GTLLTFGTGQ IRYSVPEETD KGFFVGNISK DLGLEPWEVA
     ERGVRIISRG QSQLFSLNPR GGSLVTAGRI DREELCDTMP SCMLNLEILV EETLKIYGVE
     VEVLDINDNA PSFREEEVEI KVSEHTSPGS RFPLPSARDP DAGMNSLQSY QLSPSSYFSL
     QVRGGTDGDK NPELVLEEGL DREKEASHHL LLTALDGGDP VRKGTVPIRV VVLDVNDHIP
     KFTQPVYRVS IPENLSSGTR VLVVNASDPD EGINGEVIYS FRKMKSKASE IFQLNSQTGE
     VLVGKPLDFE KYRFYEMEIQ GQDGGGLLST TTLLITVEDV NDNAPEITVT SASNSVPENS
     PSGTVIALLN VQDQDSGENG QVSCFIPSGL PFKLEKTYGN YYKLITNSEL DREQVESYNI
     TLIAKDQGSP PLSTETHLLL KVADANDNPP VFSSSSYLAY IPENNPRGSS IFSVTAIDRD
     SRENAQVTYS LAEYTIQGTP LSSYVSINSD TGVLYALQSF DYEQFQTLQL GVTASDNGDP
     PLSSNISLTL FVLDQNDNTP EILYPSLPTD GSTGVELAPR SAEPGYLVTK VVAVDRDSGQ
     NAWLSYRLLK ASEPGLFSVG LHTGEVRTAR AMMDKDALKQ SLVVTVQDHG QPPLSATVKL
     TVAVADSIPE VLEDLVSLES PANPDESGLT LYLVVAITAV SCIFLIFVMV LLALKLRRWH
     SLRLLQAASG LAGVPPSHFV GVDGMRAFLQ TYSHEVSLTA DSRKSHLIFP QPNYADTLIS
     QESCGKSEPL LITEDSTTVL GKCEPTDIQQ APPNTDWRFS QAQRPGTSGS QNGDETGTWP
     NNQFDTEMLQ AMILASASEA ADGSSTLGGG AGTMGLSARY GPQFTLQHVP DYRQNVYIPG
     SNATLTNAAG KRDGKAPAGG NGNKKKSGKK EKK
//
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;
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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   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.
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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   OPT_MOUSE               Reviewed;         328 AA.
AC   Q920A0; Q91ZZ9;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Opticin;
DE   AltName: Full=Oculoglycan;
DE   Flags: Precursor;
GN   Name=Optc; Synonyms=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 [GENOMIC DNA / MRNA].
RC   STRAIN=129/SvJ;
RX   MEDLINE=21419313; PubMed=11527931;
RA   Takanosu M., Boyd T.C., Le Goff M., Henry S.P., Zhang Y., Bishop P.N.,
RA   Mayne R.;
RT   "Structure, chromosomal location, and tissue-specific expression of
RT   the mouse opticin gene.";
RL   Invest. Ophthalmol. Vis. Sci. 42:2202-2210(2001).
CC   -!- FUNCTION: Binds collagen fibrils (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix (By similarity).
CC   -!- TISSUE SPECIFICITY: Present in the presumptive ciliary body during
CC       development and in the nonpigmented ciliary epithelium of the
CC       adult eye.
CC   -!- PTM: O-glycosylated (Probable).
CC   -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC       family. SLRP class III subfamily.
CC   -!- SIMILARITY: Contains 7 LRR (leucine-rich) repeats.
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DR   EMBL; AF333980; AAL12835.1; -; mRNA.
DR   EMBL; AF333981; AAL12836.1; -; Genomic_DNA.
DR   IPI; IPI00120286; -.
DR   UniGene; Mm.59985; -.
DR   ProteinModelPortal; Q920A0; -.
DR   SMR; Q920A0; 38-95, 127-327.
DR   Ensembl; ENSMUST00000010455; ENSMUSP00000010455; ENSMUSG00000010311.
DR   UCSC; uc007cqy.1; mouse.
DR   MGI; MGI:2151113; Optc.
DR   GeneTree; ENSGT00560000076729; -.
DR   HOGENOM; HBG445498; -.
DR   HOVERGEN; HBG006850; -.
DR   InParanoid; Q920A0; -.
DR   NextBio; 392702; -.
DR   ArrayExpress; Q920A0; -.
DR   Bgee; Q920A0; -.
DR   CleanEx; MM_OPTC; -.
DR   Genevestigator; Q920A0; -.
DR   GermOnline; ENSMUSG00000010311; Mus musculus.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
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; 1.
DR   SMART; SM00013; LRRNT; 1.
DR   PROSITE; PS51450; LRR; 4.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Leucine-rich repeat; Repeat; Secreted; Signal; Sulfation.
FT   SIGNAL        1     19       By similarity.
FT   CHAIN        20    328       Opticin.
FT                                /FTId=PRO_0000032766.
FT   REPEAT      142    161       LRR 1.
FT   REPEAT      162    185       LRR 2.
FT   REPEAT      186    209       LRR 3.
FT   REPEAT      210    229       LRR 4.
FT   REPEAT      230    255       LRR 5.
FT   REPEAT      256    276       LRR 6.
FT   REPEAT      277    307       LRR 4.
FT   COMPBIAS     79    110       Ser/Thr-rich.
FT   COMPBIAS    124    136       Cys-rich.
FT   MOD_RES      69     69       Sulfotyrosine (Potential).
FT   CARBOHYD     46     46       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     80     80       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    101    101       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    308    308       N-linked (GlcNAc...) (Potential).
FT   DISULFID    285    318       By similarity.
FT   CONFLICT    285    287       CDT -> SLS (in Ref. 1; AAL12836).
SQ   SEQUENCE   328 AA;  36471 MW;  3E2579C1F1367D1D CRC64;
     MKFLAFLSLL SLVLQKAETA SLLGEREREE QSPEEGDTYA SLYVGNHTLS IEDYNEVIDL
     SNYEELADYG DQIPEAKISN LTLPTRTSPT STVAQKTLSP NLTMAVPTTT GLLNSQSSHG
     LPTCLVCVCL GSSVYCDDAD LENIPPLPQM TTYLYARFNH ISHIQAGYFK GLTKLRRIDL
     SGNSISSIHN DALRLLPALQ DLILPENQLA ALPVLPSGIE FLDVRLNRLQ SSGIQPEAFV
     ALKKLQFLYL ANNMLDSIPG PLPLSLRSLH LQNNMIETME SDTFCDTGEH RHERRQLEDI
     RLDGNPINLS LFPEAYFCLP RLPVGHFT
//
ID   WDR7_MOUSE              Reviewed;        1489 AA.
AC   Q920I9; Q3U440; Q80TY3; Q920J0;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=WD repeat-containing protein 7;
DE   AltName: Full=TGF-beta resistance-associated protein TRAG;
GN   Name=Wdr7; Synonyms=Kiaa0541, Trag;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=129/SvJ; TISSUE=Brain;
RA   Sanders S., Thorgeirsson S.S.;
RT   "TRAG: a novel gene associated with TGF-beta resistance.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 292-1489 (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-1151; SER-1153 AND
RP   SER-1455, 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-1151, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., 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-935, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., 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=Q920I9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q920I9-2; Sequence=VSP_015275;
CC   -!- SIMILARITY: Contains 9 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; AF188123; AAL03981.1; -; mRNA.
DR   EMBL; AF188124; AAL03982.1; -; mRNA.
DR   EMBL; AK154451; BAE32595.1; -; mRNA.
DR   EMBL; AK122304; BAC65586.1; -; mRNA.
DR   IPI; IPI00120637; -.
DR   IPI; IPI00380997; -.
DR   UniGene; Mm.480708; -.
DR   ProteinModelPortal; Q920I9; -.
DR   SMR; Q920I9; 11-144, 405-603, 1357-1426.
DR   PhosphoSite; Q920I9; -.
DR   PRIDE; Q920I9; -.
DR   Ensembl; ENSMUST00000072726; ENSMUSP00000072509; ENSMUSG00000040560.
DR   Ensembl; ENSMUST00000097552; ENSMUSP00000095160; ENSMUSG00000040560.
DR   UCSC; uc008feb.1; mouse.
DR   MGI; MGI:1860197; Wdr7.
DR   GeneTree; ENSGT00520000055590; -.
DR   HOGENOM; HBG716644; -.
DR   HOVERGEN; HBG067501; -.
DR   InParanoid; Q920I9; -.
DR   OrthoDB; EOG4G1MFH; -.
DR   ArrayExpress; Q920I9; -.
DR   Bgee; Q920I9; -.
DR   CleanEx; MM_WDR7; -.
DR   Genevestigator; Q920I9; -.
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; 4.
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   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1   1489       WD repeat-containing protein 7.
FT                                /FTId=PRO_0000051354.
FT   REPEAT       17     56       WD 1.
FT   REPEAT       62    104       WD 2.
FT   REPEAT      156    199       WD 3.
FT   REPEAT      324    366       WD 4.
FT   REPEAT      404    443       WD 5.
FT   REPEAT      462    507       WD 6.
FT   REPEAT      558    597       WD 7.
FT   REPEAT     1350   1389       WD 8.
FT   REPEAT     1391   1431       WD 9.
FT   MOD_RES     935    935       Phosphoserine.
FT   MOD_RES    1151   1151       Phosphoserine.
FT   MOD_RES    1153   1153       Phosphoserine.
FT   MOD_RES    1455   1455       Phosphoserine.
FT   VAR_SEQ     950    981       Missing (in isoform 2).
FT                                /FTId=VSP_015275.
FT   CONFLICT    116    116       F -> L (in Ref. 2; BAE32595).
FT   CONFLICT    168    168       H -> R (in Ref. 2; BAE32595).
FT   CONFLICT    566    566       I -> V (in Ref. 2; BAE32595).
FT   CONFLICT    579    579       C -> S (in Ref. 1; AAL03981/AAL03982).
FT   CONFLICT    938    938       A -> P (in Ref. 2; BAE32595).
SQ   SEQUENCE   1489 AA;  163405 MW;  EA8178E491A28522 CRC64;
     MAGNSLVLPI VLWGRKAPTH CISSILLTDD GGTIVTGCHD GQICLWDVSV ELEVNPRALL
     FGHTASITCL SKACASGDKR YTVSASANGE MCLWDVNDGR CIEFTKLACT HTGIQFYQFS
     VGNQQEGRLL CHGHYPEILV VDATSLEVLY SLVSKISPDW ISSMSIIHSQ 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 KARDSPPASS 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   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   Q921N8_MOUSE            Unreviewed;       327 AA.
AC   Q921N8;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   SubName: Full=G protein pathway suppressor 2;
DE   SubName: Full=MCG22494, isoform CRA_b;
GN   Name=Gps2; ORFNames=RP23-172M21.10-001, mCG_22494;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; 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., 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.
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   Heath P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC011317; AAH11317.1; -; mRNA.
DR   EMBL; BC138879; AAI38880.1; -; mRNA.
DR   EMBL; BC138880; AAI38881.1; -; mRNA.
DR   EMBL; AL596185; CAI35152.1; -; Genomic_DNA.
DR   EMBL; CH466596; EDL12472.1; -; Genomic_DNA.
DR   EMBL; CH466596; EDL12474.1; -; Genomic_DNA.
DR   IPI; IPI00310928; -.
DR   RefSeq; NP_062700.2; NM_019726.3.
DR   UniGene; Mm.477738; -.
DR   ProteinModelPortal; Q921N8; -.
DR   PhosphoSite; Q921N8; -.
DR   PRIDE; Q921N8; -.
DR   Ensembl; ENSMUST00000057884; ENSMUSP00000054072; ENSMUSG00000023170.
DR   Ensembl; ENSMUST00000072581; ENSMUSP00000072389; ENSMUSG00000023170.
DR   Ensembl; ENSMUST00000116358; ENSMUSP00000112062; ENSMUSG00000023170.
DR   GeneID; 56310; -.
DR   KEGG; mmu:56310; -.
DR   UCSC; uc007jsp.1; mouse.
DR   CTD; 56310; -.
DR   MGI; MGI:1891751; Gps2.
DR   eggNOG; maNOG17746; -.
DR   HOGENOM; HBG714815; -.
DR   HOVERGEN; HBG005905; -.
DR   InParanoid; Q921N8; -.
DR   OMA; YAVHSHF; -.
DR   OrthoDB; EOG4F1X3S; -.
DR   PhylomeDB; Q921N8; -.
DR   NextBio; 312252; -.
DR   ArrayExpress; Q921N8; -.
DR   Bgee; Q921N8; -.
DR   Genevestigator; Q921N8; -.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   327 AA;  36738 MW;  3008661CE6579F4B CRC64;
     MPALLERPKL SNAMARALHR HIMMERERKR QEEEEVDKMM EQKMKEEQER RKKKEMEERM
     SLEETKEQIL KLQEKLSALQ EEKHQLFLQL KKVLHEEEKR RRKEQSDLTT LTSAAYQQSL
     TVHTGTHLLS MQGSPGGHNR PGTLMAADRA KQMFGPQVLT TRHYVGSAAA FAGTPEHGQF
     QGSPGGAYGT AQPPPHYGPT QPAYSPSQQL RAPSAFPAVQ YLSQPQPQPY AVHGHFQPTQ
     TGFLQPGSTL SLQKQMEHAN QQTSFSDSSS LRPMHPQALH PAPGLLASPQ LPVQIQAAGK
     SGFATTSQPG PRLPFIQHSQ NPRFYHK
//
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   -----------------------------------------------------------------------
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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   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   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   NRBP_MOUSE              Reviewed;         535 AA.
AC   Q99J45; Q8BL77;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-FEB-2011, entry version 80.
DE   RecName: Full=Nuclear receptor-binding protein;
DE   AltName: Full=HLS7-interacting protein kinase;
DE   AltName: Full=MLF1 adapter molecule;
GN   Name=Nrbp1; Synonyms=Madm, Nrbp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; 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,
RP   PHOSPHORYLATION, HOMODIMERIZATION, AND INTERACTION WITH MLF1.
RC   STRAIN=129, and BDF1;
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   [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=129, 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 THR-441, 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-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: May play a role in subcellular trafficking between the
CC       endoplasmic reticulum and Golgi apparatus through interactions
CC       with the Rho-type GTPases (By similarity).
CC   -!- SUBUNIT: Homodimer. Binds to MLF1, recruiting a serine kinase
CC       which phosphorylates both itself and MLF1. Phosphorylated MLF1
CC       binds to YWHAZ and is retained in the cytoplasm.
CC   -!- INTERACTION:
CC       Self; NbExp=1; IntAct=EBI-767484, EBI-767484;
CC       Q9QWV4:Mlf1; NbExp=3; IntAct=EBI-767484, EBI-354765;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Endomembrane system.
CC       Cell projection, lamellipodium. Note=Colocalizes with activated
CC       RAC3 to endomembranes and at the cell periphery in lamellipodia.
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.
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DR   EMBL; AF302138; AAK97260.1; -; mRNA.
DR   EMBL; AF302139; AAK97261.1; -; Genomic_DNA.
DR   EMBL; AK046142; BAC32612.1; -; mRNA.
DR   EMBL; BC004756; AAH04756.1; -; mRNA.
DR   EMBL; BC018463; AAH18463.1; -; mRNA.
DR   IPI; IPI00222739; -.
DR   RefSeq; NP_671734.1; NM_147201.2.
DR   UniGene; Mm.292040; -.
DR   ProteinModelPortal; Q99J45; -.
DR   SMR; Q99J45; 58-329.
DR   IntAct; Q99J45; 8.
DR   STRING; Q99J45; -.
DR   PhosphoSite; Q99J45; -.
DR   PRIDE; Q99J45; -.
DR   Ensembl; ENSMUST00000031034; ENSMUSP00000031034; ENSMUSG00000029148.
DR   GeneID; 192292; -.
DR   KEGG; mmu:192292; -.
DR   UCSC; uc008wxt.1; mouse.
DR   CTD; 192292; -.
DR   MGI; MGI:2183436; Nrbp1.
DR   GeneTree; ENSGT00550000074385; -.
DR   HOVERGEN; HBG057400; -.
DR   NextBio; 371294; -.
DR   ArrayExpress; Q99J45; -.
DR   Bgee; Q99J45; -.
DR   CleanEx; MM_NRBP1; -.
DR   Genevestigator; Q99J45; -.
DR   GermOnline; ENSMUSG00000029148; Mus musculus.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; 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   1: Evidence at protein level;
KW   Acetylation; Cell projection; Cytoplasm; Membrane; Phosphoprotein.
FT   CHAIN         1    535       Nuclear receptor-binding protein.
FT                                /FTId=PRO_0000086451.
FT   DOMAIN       68    327       Protein kinase.
FT   MOD_RES       2      2       Phosphoserine (By similarity).
FT   MOD_RES     134    134       N6-acetyllysine (By similarity).
FT   MOD_RES     431    431       Phosphothreonine (By similarity).
FT   MOD_RES     433    433       Phosphothreonine.
FT   MOD_RES     441    441       Phosphothreonine.
FT   CONFLICT    220    220       S -> SVFHRIFAN (in Ref. 2; BAC32612).
FT   CONFLICT    494    494       V -> G (in Ref. 2; BAC32612).
FT   CONFLICT    508    510       TSL -> SSV (in Ref. 2; BAC32612).
FT   CONFLICT    521    521       T -> S (in Ref. 2; BAC32612).
FT   CONFLICT    535    535       S -> VVELT (in Ref. 2; BAC32612).
SQ   SEQUENCE   535 AA;  59866 MW;  85DD5F6FC25C5AB7 CRC64;
     MSEGESQTVV SSGSDPKVES SSLAPGLTSV SPPVTSTTSA ASPEEEEESE DESEILEESP
     CGRWQKRREE VNQRNVPGID SAYLAMDTEE GVEVVWNEVQ FSERKNYKLQ EEKVRAVFDN
     LIQLEHLNIV KFHKYWADVK ENKARVIFIT EYMSSGSLKQ FLKKTKKNHK TMNEKAWKRW
     CTQILSALSY LHSCDPPIIH GNLTCDTIFI QHNGLIKIGS VAPDTINNHV KTCREEQKNL
     HFFAPEYGEV TNVTTAVDIY SFGMCALEMA VLEIQGNGES SYVPQEAISS AIQLLEDSLQ
     REFIQKCLQS EPARRPTARE LLFHPALFEV PSLKLLAAHC IVGHQHMIPE NALEEITKNM
     DTSAVLAEIP AGPGREPVQT LYSQSPALEL DKFLEDVRNG IYPLTAFGLP RPQQPQQEEV
     TSPVVPPSVK TPTPEPAEVE TRKVVLMQCN IESVEEGVKH HLTLLLKLED KLNRHLSCDL
     MPNESIPDLA AELVQLGFIS EADQSRLTSL LEETLNKFNF TRNSTLNTAT VTVSS
//
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;
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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   EPN4_MOUSE              Reviewed;         631 AA.
AC   Q99KN9; Q8CFH4;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 2.
DT   08-FEB-2011, entry version 79.
DE   RecName: Full=Clathrin interactor 1;
DE   AltName: Full=Enthoprotin;
DE   AltName: Full=Epsin-4;
DE   AltName: Full=Epsin-related protein;
DE            Short=EpsinR;
GN   Name=Clint1; Synonyms=Enth, Epn4, Epnr, Kiaa0171;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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=Embryonic intestine;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-631 (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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., 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-235; SER-240; SER-242
RP   AND SER-307, 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: Binds to membranes enriched in phosphatidylinositol-4,5-
CC       biphosphate (PtdIns(4,5)P2). May have a role in transport via
CC       clathrin-coated vesicles from the trans-Golgi network to
CC       endosomes. Stimulates clathrin assembly (By similarity).
CC   -!- SUBUNIT: Binds clathrin heavy chain, GGA2, AP-2 and AP1G1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       perinuclear region (By similarity). Membrane; Peripheral membrane
CC       protein (By similarity). Cytoplasmic vesicle, clathrin-coated
CC       vesicle (By similarity). Note=Found throughout the cell, with the
CC       exception of the cell surface. Concentrated in the perinuclear
CC       region and associated with clathrin-coated vesicles close to the
CC       trans-Golgi network (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99KN9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99KN9-2; Sequence=VSP_009162, VSP_009163, VSP_009164;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the epsin family.
CC   -!- SIMILARITY: Contains 1 ENTH (epsin N-terminal homology) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC41396.1; Type=Erroneous initiation;
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DR   EMBL; AB093212; BAC41396.1; ALT_INIT; mRNA.
DR   EMBL; BC004080; AAH04080.1; -; mRNA.
DR   IPI; IPI00400154; -.
DR   IPI; IPI00403139; -.
DR   UniGene; Mm.169673; -.
DR   ProteinModelPortal; Q99KN9; -.
DR   SMR; Q99KN9; 25-160.
DR   STRING; Q99KN9; -.
DR   PhosphoSite; Q99KN9; -.
DR   PRIDE; Q99KN9; -.
DR   Ensembl; ENSMUST00000065062; ENSMUSP00000070982; ENSMUSG00000006169.
DR   Ensembl; ENSMUST00000109260; ENSMUSP00000104883; ENSMUSG00000006169.
DR   UCSC; uc007inr.1; mouse.
DR   MGI; MGI:2144243; Clint1.
DR   GeneTree; ENSGT00600000084490; -.
DR   HOVERGEN; HBG048921; -.
DR   PhylomeDB; Q99KN9; -.
DR   ArrayExpress; Q99KN9; -.
DR   Bgee; Q99KN9; -.
DR   CleanEx; MM_CLINT1; -.
DR   Genevestigator; Q99KN9; -.
DR   GermOnline; ENSMUSG00000006169; Mus musculus.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; 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   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   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   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Cytoplasmic vesicle; Endocytosis;
KW   Lipid-binding; Membrane; Phosphoprotein.
FT   CHAIN         1    631       Clathrin interactor 1.
FT                                /FTId=PRO_0000074522.
FT   DOMAIN       24    157       ENTH.
FT   COMPBIAS    555    611       Met-rich.
FT   BINDING      37     37       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   BINDING      75     75       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   MOD_RES      30     30       Phosphoserine (By similarity).
FT   MOD_RES      34     34       Phosphoserine (By similarity).
FT   MOD_RES     171    171       Phosphoserine.
FT   MOD_RES     174    174       Phosphoserine (By similarity).
FT   MOD_RES     235    235       Phosphoserine.
FT   MOD_RES     240    240       Phosphoserine.
FT   MOD_RES     242    242       Phosphoserine.
FT   MOD_RES     253    253       Phosphoserine (By similarity).
FT   MOD_RES     280    280       Phosphothreonine (By similarity).
FT   MOD_RES     307    307       Phosphoserine.
FT   MOD_RES     313    313       Phosphoserine (By similarity).
FT   MOD_RES     320    320       Phosphoserine (By similarity).
FT   VAR_SEQ     346    370       Missing (in isoform 2).
FT                                /FTId=VSP_009162.
FT   VAR_SEQ     467    489       NTDMVQKSASKTLPSTWSDPSVN -> VSCLFPLGIGAYTS
FT                                TRRSNSMMS (in isoform 2).
FT                                /FTId=VSP_009163.
FT   VAR_SEQ     490    631       Missing (in isoform 2).
FT                                /FTId=VSP_009164.
SQ   SEQUENCE   631 AA;  68513 MW;  370711BBCA59CC17 CRC64;
     MLIFMYLYVC VCTCTCAFSL CSTNVVMNYS EIESKVREAT NDDPWGPSGQ LMGEIAKATF
     MYEQFPELMN MLWSRMLKDN KKNWRRVYKS LLLLAYLIRN GSERVVTSAR EHIYDLRSLE
     NYHFVDEHGK DQGINIRQKV KELVEFAQDD DRLREERKKA KKNKDKYVGV SSDSVGGFRY
     NERYDPEPKS KWDEEWDKNK SAFPFSDKLG ELSDKIGSTI DDTISKFRRK DREDSPERCS
     DSDEEKKARR GRSPKGEFKD EEETVTTKHI HITQATETTT TRHKRTANPS KTIDLGAAAH
     YTGDKASPDQ NASTHTPQSS AKPSVPSSKS SGDLVDLFDG SSQSAGGSAD LFGGFADFGS
     AAASGNFPSQ ATSGNGDFGD WSAFNQAPSG PVASGGELFG SAPQSAVELI SASQPALGPP
     PAASNSADLF DLMGSSQATM TSSQSMNFSL MSTNTVGLGL PMSRSQNTDM VQKSASKTLP
     STWSDPSVNI SLDNLLPGMQ PSKPQQPSLN TMIQQQNMQQ PLNVMTQSFG AVNLSSPSNM
     LPVRPQTNPL LGGPMPMNMP GVMTGTMGMA PLGNSAGMSQ GMVGMNMNMG MSASGMGLSG
     TMGMGMPSMA MPSGTVQPKQ DAFANFANFS K
//
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.
CC   -----------------------------------------------------------------------
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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   EPDR1_MOUSE             Reviewed;         224 AA.
AC   Q99M71; Q06BK9; Q8BQY1; Q8CAI2;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Mammalian ependymin-related protein 1;
DE            Short=MERP-1;
DE   Flags: Precursor;
GN   Name=Epdr1; Synonyms=Epdr2, Merp1, Merp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; 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=C57BL/6J;
RX   MEDLINE=21622606; PubMed=11749721; DOI=10.1089/104454901753340613;
RA   Apostolopoulos J., Sparrow R.L., McLeod J.L., Collier F.M.,
RA   Darcy P.K., Slater H.R., Ngu C., Gregorio-King C.C., Kirkland M.A.;
RT   "Identification and characterization of a novel family of mammalian
RT   ependymin-related proteins (MERPs) in hematopoietic, nonhematopoietic,
RT   and malignant tissues.";
RL   DNA Cell Biol. 20:625-635(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Gregorio-King C.C., Collier F.M., Elliott K.L., Kirkland M.A.;
RT   "Characterization of mammalian ependymin proteins.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Corpora quadrigemina, Diencephalon, and
RC   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] (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: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99M71-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99M71-2; Sequence=VSP_031977;
CC   -!- SIMILARITY: Belongs to the ependymin family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AY028709; AAK29146.1; -; Genomic_DNA.
DR   EMBL; AF353717; AAK51799.1; -; mRNA.
DR   EMBL; DQ914440; ABI84107.1; -; mRNA.
DR   EMBL; AK034083; BAC28576.1; -; mRNA.
DR   EMBL; AK038733; BAC30113.1; -; mRNA.
DR   EMBL; AK046185; BAC32624.1; -; mRNA.
DR   EMBL; AK160413; BAE35778.1; -; mRNA.
DR   EMBL; BC014708; AAH14708.1; -; mRNA.
DR   IPI; IPI00316989; -.
DR   IPI; IPI00889272; -.
DR   RefSeq; NP_598826.3; NM_134065.4.
DR   UniGene; Mm.275054; -.
DR   ProteinModelPortal; Q99M71; -.
DR   STRING; Q99M71; -.
DR   PRIDE; Q99M71; -.
DR   Ensembl; ENSMUST00000002885; ENSMUSP00000002885; ENSMUSG00000002808.
DR   GeneID; 105298; -.
DR   KEGG; mmu:105298; -.
DR   UCSC; uc007ppe.1; mouse.
DR   CTD; 105298; -.
DR   MGI; MGI:2145369; Epdr1.
DR   eggNOG; roNOG08881; -.
DR   GeneTree; ENSGT00530000064036; -.
DR   HOGENOM; HBG279479; -.
DR   HOVERGEN; HBG051490; -.
DR   InParanoid; Q99M71; -.
DR   OMA; PVQETFI; -.
DR   OrthoDB; EOG4WM4VR; -.
DR   PhylomeDB; Q99M71; -.
DR   NextBio; 357600; -.
DR   ArrayExpress; Q99M71; -.
DR   Bgee; Q99M71; -.
DR   CleanEx; MM_EPDR1; -.
DR   Genevestigator; Q99M71; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR   InterPro; IPR001299; Ependymin.
DR   Pfam; PF00811; Ependymin; 1.
DR   PRINTS; PR00317; EPENDYMIN.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Secreted; Signal.
FT   SIGNAL        1     37       Potential.
FT   CHAIN        38    224       Mammalian ependymin-related protein 1.
FT                                /FTId=PRO_0000322976.
FT   CARBOHYD    130    130       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    182    182       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ      91    224       Missing (in isoform 2).
FT                                /FTId=VSP_031977.
FT   CONFLICT    122    122       W -> S (in Ref. 3; BAC32624).
FT   CONFLICT    197    197       G -> S (in Ref. 3; BAC30113).
SQ   SEQUENCE   224 AA;  25485 MW;  D49BAC79CB1C57BB CRC64;
     MPARAPRRLV QGPRGTWLLG SLWVWVLCGL GMAGSLGTPQ PCQAPQQWEG RQVLYQQSSG
     HNNRALVSYD GLNQRVRVLD ERKALIPCKR LFEYILLYKE GVMFQIEQAT KQCAKIPLVE
     SWDPLDIPQN STFEDQYSIG GPQEQILVQE WSDRRTARSY ETWIGVYTAK DCYPVQETFI
     RNYTVVMSTR FFDVQLGIKD PSVFTPPSTC QAAQPEKMSD GCSL
//
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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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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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   Q99NC2_MOUSE            Unreviewed;       804 AA.
AC   Q99NC2;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   11-JAN-2011, entry version 35.
DE   SubName: Full=MAGE-necdin/trophinin complex (Magphinin);
GN   Name=Tro; Synonyms=trophinin/magphinin;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; 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   Saburi S., Hirama K., Yamanouchi K., Naito K., Tojo H., Tachi C.,
RA   Fukuda M.;
RT   "Identification of an Isoform of Trophinin Gene Transcript Coding for
RT   a Novel Protein, Magphinin, Revealed the Compex Genomic Structure of
RT   the Trophinin Gene.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AB032477; BAB40318.1; -; mRNA.
DR   IPI; IPI00621881; -.
DR   UniGene; Mm.3597; -.
DR   ProteinModelPortal; Q99NC2; -.
DR   STRING; Q99NC2; -.
DR   Ensembl; ENSMUST00000087253; ENSMUSP00000084508; ENSMUSG00000025272.
DR   MGI; MGI:1928994; Tro.
DR   HOVERGEN; HBG003714; -.
DR   ArrayExpress; Q99NC2; -.
DR   Bgee; Q99NC2; -.
DR   Genevestigator; Q99NC2; -.
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   804 AA;  85038 MW;  3548B61E33F915AE CRC64;
     MSQLIPWPQQ LSTNPRKLLR GTGAANKTVP SAAEISLASA ATHTATTQGQ AAKETGSIQT
     IAATARSKKN SKGKRTPAKT TNTDNEYVEA SNAIEASSRQ IGASGRQTEA SNRQIEASSR
     QTEAFNRQIE ASSRQIEASS RQTETSYQQI GASNRQIMAS NRQIGASNRQ IEASNRQIGA
     SNRQTEVSSR QIEASNRQIG ASNRQTEASN RQIGASNRQT EASNRQIGAS NRQTDASNRQ
     TEASSRQTEA SSRQTEASSR QTEASSRQIE ASAAAVRPKK PRGKKGNNKG SNSASEPSEA
     PPAIQTVTNH ALSVTVRIRR GSRARKAANK NRATESQAQI AEQGAQASEA SISALETQVA
     AAVQALADDY LAQLSLEPTT RTRGKRNRKS KHPNGEERTG NNYRRIPWGR RLPPPRDVAI
     LQERANKLVK YLLVKDQTKI PIKRSDMLKD VIQEYEDYFP EIIERASYAL EKMFRVNLKE
     IDKQNNLYIL ISTQESSAGI MGTTKDTPKL GLLMVILSVI FMNGNKASEA VIWEVLRKLG
     LHPGVKHSLF GEVKKLITDE FVKQKYLEYK RVPNSRPPEY EFFWGLRSYH ETSKMKVLKF
     ACKVQKKDPK DWAAQYREAV EMDIQAAAVA VAEAKARAEA RAQMGIGEEA VAGPWNWDDM
     DINCLTSGGP STGAGFCSGP STGGFGGGPS TGPGFGGPST GPGFGGPSTG GGFGGPNTGG
     GFGGPSTGGG FGGPSTGGGF GGPSTGGGFG GPSTAAGFGS GLSTSTGFGG GLNTSAGFSG
     GPPSTGTGFG GGASSHGGCG FPYG
//
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   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;
CC   -----------------------------------------------------------------------
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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   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   ZN318_MOUSE             Reviewed;        2064 AA.
AC   Q99PP2; Q3TZL5; Q8BMX9; Q9JJ01;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Zinc finger protein 318;
DE   AltName: Full=Testicular zinc finger protein;
DE   Flags: Fragment;
GN   Name=Znf318; Synonyms=Tzf, Zfp318;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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.
RC   STRAIN=ddY; TISSUE=Testis;
RX   MEDLINE=20334282; PubMed=10873617; DOI=10.1006/bbrc.2000.2953;
RA   Inoue A., Ishiji A., Kasagi S., Ishizuka M., Hirose S., Baba T.,
RA   Hagiwara H.;
RT   "The transcript for a novel protein with a zinc finger motif is
RT   expressed at specific stages of mouse spermatogenesis.";
RL   Biochem. Biophys. Res. Commun. 273:398-403(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=ddY;
RX   MEDLINE=22477853; PubMed=12589823; DOI=10.1016/S0006-291X(03)00085-8;
RA   Ishizuka M., Ohshima H., Tamura N., Nakada T., Inoue A., Hirose S.,
RA   Hagiwara H.;
RT   "Molecular cloning and characteristics of a novel zinc finger protein
RT   and its splice variant whose transcripts are expressed during
RT   spermatogenesis.";
RL   Biochem. Biophys. Res. Commun. 301:1079-1085(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 393-1057 AND 1999-2064
RP   (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   [4]
RP   FUNCTION, AND INTERACTION WITH AR.
RX   PubMed=15882980; DOI=10.1016/j.bbrc.2005.04.024;
RA   Ishizuka M., Kawate H., Takayanagi R., Ohshima H., Tao R.-H.,
RA   Hagiwara H.;
RT   "A zinc finger protein TZF is a novel corepressor of androgen
RT   receptor.";
RL   Biochem. Biophys. Res. Commun. 331:1025-1031(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407 AND SER-2033, 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: Repressed AR-mediated transcriptional activation. May
CC       act as a transcriptional regulator during spermatogenesis and in
CC       particular, during meiotic division.
CC   -!- SUBUNIT: Interacts with the N-terminal domain of AR.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=TZF-L;
CC         IsoId=Q99PP2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99PP2-2; Sequence=VSP_016594, VSP_016595;
CC   -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are highly expressed
CC       in testis, moderately expressed in adrenal gland and uterus and
CC       faintly expressed in brain, kidney and liver. Isoform 1 is
CC       expressed more in adrenal gland, uterus and liver than isoform 2
CC       is. Expression during testicular development of isoform 1 and
CC       isoform 2 is restricted to spermatocytes at the pachytene stage of
CC       meiotic prophase and to round and elongated spermatids.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 2 matrin-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF61636.1; Type=Frameshift; Positions=13, 32;
CC       Sequence=AAK00650.1; Type=Frameshift; Positions=13, 32;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF159455; AAF61636.1; ALT_FRAME; mRNA.
DR   EMBL; AF227194; AAK00650.1; ALT_FRAME; mRNA.
DR   EMBL; AK011661; BAC25342.1; -; mRNA.
DR   EMBL; AK157779; BAE34193.1; -; mRNA.
DR   IPI; IPI00282808; -.
DR   IPI; IPI00410738; -.
DR   PIR; JC7316; JC7316.
DR   RefSeq; NP_997554.2; NM_207671.3.
DR   UniGene; Mm.439916; -.
DR   ProteinModelPortal; Q99PP2; -.
DR   STRING; Q99PP2; -.
DR   PhosphoSite; Q99PP2; -.
DR   PRIDE; Q99PP2; -.
DR   Ensembl; ENSMUST00000047394; ENSMUSP00000049207; ENSMUSG00000015597.
DR   Ensembl; ENSMUST00000113479; ENSMUSP00000109107; ENSMUSG00000015597.
DR   Ensembl; ENSMUST00000113481; ENSMUSP00000109109; ENSMUSG00000015597.
DR   GeneID; 57908; -.
DR   KEGG; mmu:57908; -.
DR   UCSC; uc008csq.1; mouse.
DR   UCSC; uc008csr.1; mouse.
DR   CTD; 57908; -.
DR   MGI; MGI:1889348; Zfp318.
DR   eggNOG; roNOG11651; -.
DR   GeneTree; ENSGT00390000000614; -.
DR   HOVERGEN; HBG107139; -.
DR   InParanoid; Q99PP2; -.
DR   OrthoDB; EOG48KR9B; -.
DR   NextBio; 314073; -.
DR   ArrayExpress; Q99PP2; -.
DR   Bgee; Q99PP2; -.
DR   CleanEx; MM_ZFP318; -.
DR   Genevestigator; Q99PP2; -.
DR   GermOnline; ENSMUSG00000015597; Mus musculus.
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:0007126; P:meiosis; 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; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR003604; Znf_U1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SMART; SM00451; ZnF_U1; 2.
DR   PROSITE; PS50171; ZF_MATRIN; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Meiosis;
KW   Metal-binding; Nucleus; Phosphoprotein; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN        <1   2064       Zinc finger protein 318.
FT                                /FTId=PRO_0000191808.
FT   ZN_FING     912    946       Matrin-type 1.
FT   ZN_FING     985   1007       Matrin-type 2.
FT   COILED      175    203       Potential.
FT   COILED      731    830       Potential.
FT   COILED     1625   1654       Potential.
FT   COMPBIAS   1297   1326       Pro-rich.
FT   MOD_RES      32     32       Phosphoserine (By similarity).
FT   MOD_RES      73     73       Phosphoserine (By similarity).
FT   MOD_RES     166    166       Phosphoserine (By similarity).
FT   MOD_RES     168    168       Phosphoserine (By similarity).
FT   MOD_RES     324    324       Phosphoserine (By similarity).
FT   MOD_RES     407    407       Phosphoserine.
FT   MOD_RES     559    559       Phosphoserine (By similarity).
FT   MOD_RES     886    886       Phosphoserine (By similarity).
FT   MOD_RES    1127   1127       N6-acetyllysine (By similarity).
FT   MOD_RES    1272   1272       Phosphoserine (By similarity).
FT   MOD_RES    1477   1477       Phosphoserine (By similarity).
FT   MOD_RES    1735   1735       Phosphoserine (By similarity).
FT   MOD_RES    1881   1881       Phosphoserine (By similarity).
FT   MOD_RES    1967   1967       Phosphoserine (By similarity).
FT   MOD_RES    1970   1970       Phosphoserine (By similarity).
FT   MOD_RES    2021   2021       Phosphoserine (By similarity).
FT   MOD_RES    2033   2033       Phosphoserine.
FT   VAR_SEQ     942    981       TLDPYNRPWASKTQSEAKQDTVKRTDKITVPAKGSEFLIP
FT                                -> GQFQKSSHFQTEGLKQMFLLQECRDRNHRDYGNNVRPC
FT                                GQ (in isoform 2).
FT                                /FTId=VSP_016594.
FT   VAR_SEQ     982   2064       Missing (in isoform 2).
FT                                /FTId=VSP_016595.
FT   NON_TER       1      1
SQ   SEQUENCE   2064 AA;  228220 MW;  CA64069FFA9D269B CRC64;
     SLEESLRITV GNDHFCVSTP ERRRLSDRLG ISPVDGLQDM DRDDLTDDSD FTRSSQCSRG
     LERYISREEG PLSPFLGQLD EDYRTRETFL HRPEFSPQSS CHDELLRGTE RNRDKLKSSS
     YSIRSEERSR EAKRPRYDDT EKVHSSGGDH SSFTSGTRNY RQRRSSPSPR FLDPEFRELD
     LARRKREEEE EQSRSLSQEL VGVGDDQIGC SIPGLAGVLT TSEPGYSLQR PEEVPMMPKK
     SILKKRIEAD MKPSLQLESF SSGASSGEDH PLYSEHSPLP LSGAIAAFTS EIENKGTTVE
     ADLKEPQSNL YQWGPLREIP KDNSEKFDSF LGFKERLDLK AEGLEQQTDN LLPHERASQD
     GSGFSRILSM LADPTITQEK RRRSFPDIED EEKFLYGDEE EDIKSESPLK SLEDPESAGT
     RQKANSLPST PAVKLESLEE SNPEYAKIHN LLKTIGLDIG VAEIGKLAAR TQERLHGKKP
     SSRPSADRRL SADRHLSGDR HFSADRCSSV EHSFTADWRS SDPHRPESRE THHSNTQSPE
     VSHPHPASPV DPYLRTKNSP PFLKSDHPVC HVSGPEVVGS GFQSSVAVRC MLPSAPSTPI
     RLPHSAALSQ FHIPGASQFA AARIPPNYQG SVIPSASFDA YRHYMAYAAS RWPMYPASQP
     PSHPLSDPHR LLPVTKQAAR SRPNLRVIPT VTPAKPKQEI PVLGSISVKR IPVRVSIPSL
     IKYNPKKISD EKNRASQKQK VIEEREKLKT EQEARQKKMF YLTTELERLH KQQGEMLRKK
     RREKDGHKDP LLMEVSRLQD SIMKDIAELH KETEEAEKKQ SELDKVAQIL GIDIFDKSLK
     SSNDSKESTE KPEKEKSKSP EKELSPSNSS SSNKESKMNE KSCIKSPSST ESLQPTVKQS
     DQPVAAYEYY DAGSHWCKDC NTTCGTMFDF FTHMHNKKHT QTLDPYNRPW ASKTQSEAKQ
     DTVKRTDKIT VPAKGSEFLI PVTGFYCQLC EEFLGDPISG EQHVKGHQHN ENYKKYVEEN
     PLYEERRNLD RQAGLAVVLE TERRRQNELK RKLNEKPKEE KIEKKARIVR EVKEDDKAPG
     ELEEQLSEDG SAPEKGEVKG NASLRPQVKE EVKKEPSVAS IAASFGKFSW KKPEKEEEKG
     SVVTPGAPKE DTVETSKDRD DGKAEVGKAK PIKIKLSGKT VIAHTSPWTP VVTTSTQTKI
     RPNLPIPSTV LRKSGSATVS KPAPLNTFLS IKSSGTSTKP LPVVKESSSD LLLPPDIISK
     AFGGEEVVLK GSPEEKVELA EKNEPSQVPE QMLALLPPPP PPPPPPPPPP PPPPPQAVPQ
     LSAPSPAQAN VVLTPVKSNS VISQTFSLGF QGPNILNPGL PVAFMASEQP TVIPSDETAP
     GVSESDWDQT LISMLVRPPP PLSSVFSEQA KKLEKRNSCL ATANAKDLYD IFYSSGGKGA
     HETKLSSSTL ANGESSSLPR TESSDFSSTC TLNSSMSSED LPQCSALVTA TEISNLENPI
     SKGMESTGKW SVVDQIDPKS RDSTYSFLQP LTRLYQNKPY EIVSPKTDTL VMWTSGSSQN
     DTHKDRPPEG KIRFDLGEPG PPGTDSTSHL SDTHCQTNGP QKLIEINLID NQNKNQEVYQ
     SEGCRESEMK RKTELKGKVA TEEEEEEEEE GANSIEDSNS NHGNRNTWEG EIGQPKLSTV
     DKKGEQSSKL MTGHENTSKV VIELSPSLPS KRTKIDLFPS LLQNPKSMPE LLLLSPAGSG
     LCLKRQEIWE RPEKPGLEDV ELQGTRPELT VTIESKVLEN FDTTHLEVEG FASLRNLGDM
     HANFHNSQTE QTRRSPTALS EKMSEEISVS SVMCNPSSSS DIEPVPSFSG FPLESPKTLV
     LNFETEGAHS SSNSRNGRIT SNSLETGHPV ENVGHDLGGE RTHQALDLLA GGMLSEDVKE
     TSPLQKDLLR MESTTVSPSG LGPSPCLPDL VDFVTRTPGV PKQKPCSPLS EPDAFLKCSS
     LEMGSPPPEI LSVSVSEVAV PQVSEDNDSA LNLVKTPPSG SPSRDQVVGG NVSPREMPEQ
     EAAVDVIPDH TRSNVYNSQD YLNG
//
ID   TRI33_MOUSE             Reviewed;        1142 AA.
AC   Q99PP7; Q6SI71; Q6ZPX5;
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=E3 ubiquitin-protein ligase TRIM33;
DE            EC=6.3.2.-;
DE   AltName: Full=Ectodermin homolog;
DE   AltName: Full=Transcription intermediary factor 1-gamma;
DE            Short=TIF1-gamma;
DE   AltName: Full=Tripartite motif-containing protein 33;
GN   Name=Trim33; Synonyms=Kiaa1113;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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).
RX   PubMed=15256250; DOI=10.1016/j.gene.2004.02.056;
RA   Yan K.P., Dolle P., Mark M., Lerouge T., Wendling O., Chambon P.,
RA   Losson R.;
RT   "Molecular cloning, genomic structure, and expression analysis of the
RT   mouse transcriptional intermediary factor 1 gamma gene.";
RL   Gene 334:3-13(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 55-1142 (ISOFORM BETA).
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 949-1142 (ISOFORM ALPHA).
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   [4]
RP   DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX   PubMed=15314655; DOI=10.1371/journal.pbio.0020237;
RA   Ransom D.G., Bahary N., Niss K., Traver D., Burns C., Trede N.S.,
RA   Paffett-Lugassy N., Saganic W.J., Lim C.A., Hersey C., Zhou Y.,
RA   Barut B.A., Lin S., Kingsley P.D., Palis J., Orkin S.H., Zon L.I.;
RT   "The zebrafish moonshine gene encodes transcriptional intermediary
RT   factor 1 gamma, an essential regulator of hematopoiesis.";
RL   PLoS Biol. 2:1188-1196(2004).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=16751102; DOI=10.1016/j.cell.2006.03.045;
RA   He W., Dorn D.C., Erdjument-Bromage H., Tempst P., Moore M.A.,
RA   Massague J.;
RT   "Hematopoiesis controlled by distinct TIF1gamma and Smad4 branches of
RT   the TGFbeta pathway.";
RL   Cell 125:929-941(2006).
CC   -!- FUNCTION: Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4
CC       ubiquitination, nuclear exclusion and degradation via the
CC       ubiquitin proteasome pathway (By similarity). May act as a
CC       transcriptional repressor (By similarity). Inhibits the
CC       transcriptional response to TGF-beta/BMP signaling cascade (By
CC       similarity). Plays a role in the control of cell proliferation (By
CC       similarity). Its association with SMAD2 and SMAD3 stimulates
CC       erythroid differentiation of hematopoietic stem/progenitor.
CC       Monoubiquitinates SMAD4 and acts as an inhibitor of SMAD4-
CC       dependent TGF-beta/BMP signaling cascade (Monoubiquitination of
CC       SMAD4 hampers its ability to form a stable complex with activated
CC       SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade)
CC       (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Homooligomer and heterooligomer with TRIM24 and TRIM28
CC       family members (By similarity). Interacts with SMAD4 in
CC       unstimulated cells (By similarity). Found in a complex with SMAD2
CC       and SMAD3 upon addition of TGF-beta (By similarity). Interacts
CC       with SMAD2 and SMAD3 (By similarity). Interacts with SMAD4 under
CC       basal and induced conditions and, upon TGF-beta signaling, with
CC       activated SMAD2. Forms a ternary complex with SMAD4 and SMAD2 upon
CC       TGF-beta signaling (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=In discrete nuclear dots
CC       resembling nuclear bodies.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Alpha;
CC         IsoId=Q99PP7-1; Sequence=Displayed;
CC       Name=Beta;
CC         IsoId=Q99PP7-2; Sequence=VSP_012068;
CC   -!- TISSUE SPECIFICITY: Ubiquitous with high level in testis.
CC   -!- DEVELOPMENTAL STAGE: Expressed in round hematopoietic cells in
CC       yolk sac blood islands at 8.5 dpc. Expressed uniformly at 10.5
CC       dpc. Expressed in the brain, spinal cord, neuroepithelium and in
CC       spinal ganglia at 12.5 dpc. Expressed in brain, spinal cord,
CC       developing epithelia of the lung, stomach, intestine, outer region
CC       of the developing kidney, liver, brown fat tissue, skeletal
CC       muscle, developing craniofacial region, thymus, cochlear and
CC       pharyngeal epithelia and olfactory and respiratory epithelia at
CC       16.5 dpc.
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.
CC   -----------------------------------------------------------------------
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DR   EMBL; AY458590; AAS10352.1; -; mRNA.
DR   EMBL; AK129293; BAC98103.1; -; mRNA.
DR   EMBL; AF220138; AAG53511.1; -; mRNA.
DR   IPI; IPI00409904; -.
DR   IPI; IPI00480381; -.
DR   RefSeq; NP_001073299.1; NM_001079830.1.
DR   RefSeq; NP_444400.2; NM_053170.2.
DR   UniGene; Mm.195036; -.
DR   ProteinModelPortal; Q99PP7; -.
DR   SMR; Q99PP7; 139-205, 230-330, 902-1096.
DR   STRING; Q99PP7; -.
DR   PhosphoSite; Q99PP7; -.
DR   PRIDE; Q99PP7; -.
DR   Ensembl; ENSMUST00000029444; ENSMUSP00000029444; ENSMUSG00000033014.
DR   Ensembl; ENSMUST00000106860; ENSMUSP00000102473; ENSMUSG00000033014.
DR   GeneID; 94093; -.
DR   KEGG; mmu:94093; -.
DR   UCSC; uc008qsv.1; mouse.
DR   UCSC; uc008qsw.1; mouse.
DR   CTD; 94093; -.
DR   MGI; MGI:2137357; Trim33.
DR   eggNOG; roNOG05445; -.
DR   GeneTree; ENSGT00530000062982; -.
DR   HOGENOM; HBG446888; -.
DR   HOVERGEN; HBG054599; -.
DR   InParanoid; Q99PP7; -.
DR   OrthoDB; EOG4SN1N0; -.
DR   NextBio; 352085; -.
DR   ArrayExpress; Q99PP7; -.
DR   Bgee; Q99PP7; -.
DR   CleanEx; MM_TRIM33; -.
DR   Genevestigator; Q99PP7; -.
DR   GermOnline; ENSMUSG00000033014; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0070410; F:co-SMAD binding; ISS:BHF-UCL.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070412; F:R-SMAD binding; ISS:BHF-UCL.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
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   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; 2.
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; 2.
DR   SMART; SM00184; RING; 2.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 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   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Bromodomain; Coiled coil;
KW   DNA-binding; Ligase; Metal-binding; Nucleus; Phosphoprotein; Repeat;
KW   Repressor; Transcription; Transcription regulation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1   1142       E3 ubiquitin-protein ligase TRIM33.
FT                                /FTId=PRO_0000056396.
FT   DOMAIN      989   1061       Bromo.
FT   ZN_FING     141    201       RING-type.
FT   ZN_FING     228    275       B box-type 1.
FT   ZN_FING     287    328       B box-type 2.
FT   ZN_FING     902    949       PHD-type.
FT   REGION        1    163       Necessary for E3 ubiquitin-protein ligase
FT                                activity and repression of SMAD4
FT                                signaling and transcriptional repression
FT                                (By similarity).
FT   REGION      315    417       Necessary for oligomerization (By
FT                                similarity).
FT   COILED      315    417       Potential.
FT   COMPBIAS     13     18       Poly-Gly.
FT   COMPBIAS     20    122       Ala-rich.
FT   COMPBIAS    524    636       Gln-rich.
FT   COMPBIAS    708    785       Ser-rich.
FT   MOD_RES     268    268       N6-acetyllysine (By similarity).
FT   MOD_RES     521    521       Phosphothreonine (By similarity).
FT   MOD_RES     778    778       N6-acetyllysine (By similarity).
FT   MOD_RES     784    784       N6-acetyllysine (By similarity).
FT   MOD_RES     877    877       Phosphoserine (By similarity).
FT   MOD_RES     968    968       N6-acetyllysine (By similarity).
FT   MOD_RES    1117   1117       Phosphothreonine (By similarity).
FT   MOD_RES    1120   1120       Phosphoserine (By similarity).
FT   MOD_RES    1134   1134       Phosphoserine (By similarity).
FT   VAR_SEQ    1056   1072       Missing (in isoform Beta).
FT                                /FTId=VSP_012068.
FT   CONFLICT    949    952       IGKP -> HASA (in Ref. 3).
SQ   SEQUENCE   1142 AA;  123843 MW;  D43699AE75F0893F CRC64;
     MAENKGGGEA ESGGGGSGSA PVTAGAAGPT AQEAEPPLAA VLVEEEEEEG GRAGAEGGAA
     GPDDGGVAAA SSSSAPAASV PAASVGSAVP GGAASTPAPA AAPAPAPAPA PAPAPAPAPA
     PAPGSSSGPP LGPPASLLDT CAVCQQSLQS RREAEPKLLP CLHSFCLRCL PEPERQLSVP
     IPGGSNGDVQ QVGVIRCPVC RQECRQIDLV DNYFVKDTSE APSSSDEKSE QVCTSCEDNA
     SAVGFCVECG EWLCKTCIEA HQRVKFTKDH LIRKKEDVSE SVGTSGQRPV FCPVHKQEQL
     KLFCETCDRL TCRDCQLLEH KEHRYQFLEE AFQNQKGAIE NLLAKLLEKK NYVHFAATQV
     QNRIKEVNET NKRVEQEIKV AIFTLINEIN KKGKSLLQQL ENVTKERQMK LLQQQNDITG
     LSRQVKHVMN FTNWAIASGS STALLYSKRL ITFQLRHILK ARCDPVPAAN GAIRFHCDPT
     FWAKNVVNLG NLVIESKPAP GYTPNVVVGQ VPPGTNHISK TPGQINLAQL RLQHMQQQVY
     AQKHQQLQQM RLQQPPAPIP TTTATTQQHP RQAAPQMLQQ QPPRLISVQT MQRGNMNCGA
     FQAHQMRLAQ NAARIPGIPR HSAPQYSMMQ PHLQRQHSNP GHAGPFPVVS AHNPINPTSP
     TTATMANANR GPTSPSVTAI ELIPSVTNPE NLPSLPDIPP IQLEDAGSSS LDNLLSRYIS
     GSHLPPQPTS TMNPSPGPSA LSPGSSGLSN SHTPVRPPST SSTGSRGSCG SSGRTAEKSA
     HSFKSDQVKV KQEPGTEEEI CSFSGAVKQE KTEDGRRSAC MLSSPESSLT PPLSTNLHLE
     SELDTLTGLE NHVKTEPTDI SESCKQSGLS NLVNGKSPIR NLMHRSARIG GDGNSKDDDP
     NEDWCAVCQN GGDLLCCEKC PKVFHLTCHV PTLLSFPSGD WICTFCRDIG KPEVEYDCDN
     MQHSKKGKTA QGLSPVDQRK CERLLLYLYC HELSIEFQEP VPVSIPNYYK IIKKPMDLST
     VKKKLQKKHS QHYQIPDDFV ADVRLIFKNC ERFNEMMKVV QVYADTQEIN LKGDSEVAKA
     GKAVALYFED KLSEIYSDRT FTPLPEFEQD EDDGEVTEDS DEDFIQPRRK RLKSDERPVH
     IK
//
ID   ATP5L_MOUSE             Reviewed;         103 AA.
AC   Q9CPQ8; O70590; Q5M9M8;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=ATP synthase subunit g, mitochondrial;
DE            Short=ATPase subunit g;
GN   Name=Atp5l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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=Mammary gland;
RX   MEDLINE=99290043; PubMed=10361692; DOI=10.1271/bbb.63.767;
RA   Baik M., Jeon D., Kim H.;
RT   "Sequence of a cDNA encoding mouse F1F0-ATP synthase g subunit.";
RL   Biosci. Biotechnol. Biochem. 63:767-768(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Hippocampus, Liver, 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   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   [4]
RP   PROTEIN SEQUENCE OF 12-54, 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-54 AND LYS-66, 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. 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 g subunit family.
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DR   EMBL; Y17223; CAA76699.1; -; mRNA.
DR   EMBL; AK005175; BAB23862.1; -; mRNA.
DR   EMBL; AK005321; BAB23952.1; -; mRNA.
DR   EMBL; AK005380; BAB23987.1; -; mRNA.
DR   EMBL; AK008002; BAB25401.1; -; mRNA.
DR   EMBL; AK008012; BAB25408.1; -; mRNA.
DR   EMBL; AK008030; BAB25420.1; -; mRNA.
DR   EMBL; AK008087; BAB25451.1; -; mRNA.
DR   EMBL; AK008183; BAB25516.1; -; mRNA.
DR   EMBL; AK008251; BAB25558.1; -; mRNA.
DR   EMBL; AK008321; BAB25600.1; -; mRNA.
DR   EMBL; AK009465; BAB26305.1; -; mRNA.
DR   EMBL; AK009468; BAB26308.1; -; mRNA.
DR   EMBL; AK009471; BAB26310.1; -; mRNA.
DR   EMBL; AK009612; BAB26392.1; -; mRNA.
DR   EMBL; AK009806; BAB26514.1; -; mRNA.
DR   EMBL; AK011038; BAB27351.1; -; mRNA.
DR   EMBL; AK011046; BAB27357.1; -; mRNA.
DR   EMBL; AK011099; BAB27396.1; -; mRNA.
DR   EMBL; AK019252; BAB31628.1; -; mRNA.
DR   EMBL; AK019274; BAB31641.1; -; mRNA.
DR   EMBL; AK019320; BAB31664.1; -; mRNA.
DR   EMBL; AK019343; BAB31670.1; -; mRNA.
DR   EMBL; AK019350; BAB31672.1; -; mRNA.
DR   EMBL; AK019355; BAB31676.1; -; mRNA.
DR   EMBL; BC031384; AAH31384.1; -; mRNA.
DR   EMBL; BC086880; AAH86880.1; -; mRNA.
DR   EMBL; BC089555; AAH89555.1; -; mRNA.
DR   EMBL; BC094407; AAH94407.1; -; mRNA.
DR   IPI; IPI00876323; -.
DR   RefSeq; NP_038823.2; NM_013795.5.
DR   RefSeq; XP_001478505.1; XM_001478455.2.
DR   UniGene; Mm.14663; -.
DR   UniGene; Mm.481794; -.
DR   STRING; Q9CPQ8; -.
DR   PhosphoSite; Q9CPQ8; -.
DR   PRIDE; Q9CPQ8; -.
DR   Ensembl; ENSMUST00000043675; ENSMUSP00000047960; ENSMUSG00000038717.
DR   Ensembl; ENSMUST00000114688; ENSMUSP00000110336; ENSMUSG00000038717.
DR   GeneID; 100042348; -.
DR   GeneID; 27425; -.
DR   KEGG; mmu:100042348; -.
DR   KEGG; mmu:27425; -.
DR   UCSC; uc009per.1; mouse.
DR   CTD; 27425; -.
DR   MGI; MGI:1351597; Atp5l.
DR   eggNOG; roNOG16549; -.
DR   HOVERGEN; HBG050614; -.
DR   InParanoid; Q9CPQ8; -.
DR   OrthoDB; EOG4C2HC2; -.
DR   NextBio; 453491; -.
DR   ArrayExpress; Q9CPQ8; -.
DR   Bgee; Q9CPQ8; -.
DR   Genevestigator; Q9CPQ8; -.
DR   GermOnline; ENSMUSG00000038717; 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; IPR016702; ATP-Synthase_su_G_mt_met.
DR   InterPro; IPR006808; ATPase_F0-cplx_gsu_mt.
DR   Pfam; PF04718; ATP-synt_G; 1.
DR   PIRSF; PIRSF017835; ATP-synth_g_mitoch_animal; 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    103       ATP synthase subunit g, mitochondrial.
FT                                /FTId=PRO_0000071692.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      24     24       N6-acetyllysine (By similarity).
FT   MOD_RES      54     54       N6-acetyllysine.
FT   MOD_RES      66     66       N6-acetyllysine.
FT   CONFLICT     56     56       I -> M (in Ref. 1; CAA76699).
SQ   SEQUENCE   103 AA;  11425 MW;  66BB25CECD67AA33 CRC64;
     MAKFIRNFAE KAPSMVAAAV TYSKPRLATF WHYAKVELVP PTPAEIPTAI QSVKKIIQSA
     KTGSFKHLTV KEAVLNGLVA TEVWMWFYIG EIIGKRGIVG YDV
//
ID   DHSB_MOUSE              Reviewed;         282 AA.
AC   Q9CQA3; Q3TF82; Q9DC91;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial;
DE            EC=1.3.5.1;
DE   AltName: Full=Iron-sulfur subunit of complex II;
DE            Short=Ip;
DE   Flags: Precursor;
GN   Name=Sdhb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; 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, Bone marrow, 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].
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 49-92; 118-153; 170-179; 208-232 AND 245-257, AND
RP   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: Iron-sulfur protein (IP) subunit of succinate
CC       dehydrogenase (SDH) that is involved in complex II of the
CC       mitochondrial electron transport chain and is responsible for
CC       transferring electrons from succinate to ubiquinone (coenzyme Q)
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Succinate + ubiquinone = fumarate + ubiquinol.
CC   -!- COFACTOR: Binds 1 2Fe-2S cluster (By similarity).
CC   -!- COFACTOR: Binds 1 3Fe-4S cluster (By similarity).
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster (By similarity).
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       fumarate from succinate (eukaryal route): step 1/1.
CC   -!- SUBUNIT: Component of complex II composed of four subunits: the
CC       flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a
CC       cytochrome b560 composed of SDHC and SDHD (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Matrix side (By similarity).
CC   -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate
CC       reductase iron-sulfur protein family.
CC   -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
CC   -!- SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain.
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DR   EMBL; AK003052; BAB22534.1; -; mRNA.
DR   EMBL; AK003533; BAB22842.1; -; mRNA.
DR   EMBL; AK009660; BAB26422.1; -; mRNA.
DR   EMBL; AK153045; BAE31674.1; -; mRNA.
DR   EMBL; AK169252; BAE41016.1; -; mRNA.
DR   EMBL; BC013509; AAH13509.1; -; mRNA.
DR   EMBL; BC051934; AAH51934.1; -; mRNA.
DR   IPI; IPI00338536; -.
DR   PIR; PT0094; PT0094.
DR   RefSeq; NP_075863.2; NM_023374.3.
DR   UniGene; Mm.246965; -.
DR   ProteinModelPortal; Q9CQA3; -.
DR   SMR; Q9CQA3; 39-277.
DR   STRING; Q9CQA3; -.
DR   REPRODUCTION-2DPAGE; Q9CQA3; -.
DR   PRIDE; Q9CQA3; -.
DR   Ensembl; ENSMUST00000010007; ENSMUSP00000010007; ENSMUSG00000009863.
DR   GeneID; 67680; -.
DR   KEGG; mmu:67680; -.
DR   NMPDR; fig|10090.3.peg.10709; -.
DR   UCSC; uc008vnl.1; mouse.
DR   CTD; 67680; -.
DR   MGI; MGI:1914930; Sdhb.
DR   HOGENOM; HBG616382; -.
DR   HOVERGEN; HBG005483; -.
DR   InParanoid; Q9CQA3; -.
DR   OMA; LIVDMEP; -.
DR   OrthoDB; EOG4T4CW4; -.
DR   PhylomeDB; Q9CQA3; -.
DR   BRENDA; 1.3.5.1; 244.
DR   NextBio; 325239; -.
DR   ArrayExpress; Q9CQA3; -.
DR   Bgee; Q9CQA3; -.
DR   Genevestigator; Q9CQA3; -.
DR   GermOnline; ENSMUSG00000009863; Mus musculus.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II; ISS:UniProtKB.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:EC.
DR   GO; GO:0048039; F:ubiquinone binding; ISS:UniProtKB.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR012675; Beta-grasp_ferredoxin-type.
DR   InterPro; IPR001041; Ferredoxin.
DR   InterPro; IPR012285; Fum_reductase_C.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR004489; Succ_DH/fum_Rdtase_Fe-S.
DR   Gene3D; G3DSA:3.10.20.30; Ferredoxin_fold; 1.
DR   Gene3D; G3DSA:1.10.1060.10; Fum_reductase_C; 1.
DR   SUPFAM; SSF54292; Ferredoxin; 1.
DR   SUPFAM; SSF46548; Helical_ferredxn; 1.
DR   TIGRFAMs; TIGR00384; dhsB; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; 3Fe-4S; 4Fe-4S; Direct protein sequencing; Electron transport;
KW   Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Transit peptide;
KW   Transport; Tricarboxylic acid cycle.
FT   TRANSIT       1     30       Mitochondrion (By similarity).
FT   CHAIN        31    282       Succinate dehydrogenase [ubiquinone]
FT                                iron-sulfur subunit, mitochondrial.
FT                                /FTId=PRO_0000010356.
FT   DOMAIN       42    135       2Fe-2S ferredoxin-type.
FT   DOMAIN      178    208       4Fe-4S ferredoxin-type.
FT   METAL        95     95       Iron-sulfur 1 (2Fe-2S) (By similarity).
FT   METAL       100    100       Iron-sulfur 1 (2Fe-2S) (By similarity).
FT   METAL       103    103       Iron-sulfur 1 (2Fe-2S) (By similarity).
FT   METAL       115    115       Iron-sulfur 1 (2Fe-2S) (By similarity).
FT   METAL       188    188       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       191    191       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       194    194       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       198    198       Iron-sulfur 3 (3Fe-4S) (By similarity).
FT   METAL       245    245       Iron-sulfur 3 (3Fe-4S) (By similarity).
FT   METAL       251    251       Iron-sulfur 3 (3Fe-4S) (By similarity).
FT   METAL       255    255       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   BINDING     203    203       Ubiquinone; shared with DHSD (By
FT                                similarity).
FT   CONFLICT     40     40       R -> K (in Ref. 1; BAB22534).
SQ   SEQUENCE   282 AA;  31814 MW;  A8616A911427AF8E CRC64;
     MAATVGVSLK RGFPAAVLGR VGLQFQACRG AQTAAAAAPR IKKFAIYRWD PDKTGDKPRM
     QTYEVDLNKC GPMVLDALIK IKNEVDSTLT FRRSCREGIC GSCAMNINGG NTLACTRRID
     TDLSKVSKIY PLPHMYVIKD LVPDLSNFYA QYKSIEPYLK KKDESQEGKQ QYLQSIEDRE
     KLDGLYECIL CACCSTSCPS YWWNGDKYLG PAVLMQAYRW MIDSRDDFTE ERLAKLQDPF
     SVYRCHTIMN CTQTCPKGLN PGKAIAEIKK MMATYKEKRA LA
//
ID   PCYOX_MOUSE             Reviewed;         505 AA.
AC   Q9CQF9; Q3UHV6; Q69ZW0; Q8BZX1;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Prenylcysteine oxidase;
DE            EC=1.8.3.5;
DE   Flags: Precursor;
GN   Name=Pcyox1; Synonyms=Kiaa0908;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; 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, Liver, 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   [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 5-505.
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   PROTEIN SEQUENCE OF 145-151; 169-193; 292-298; 328-349 AND 421-430,
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   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196, 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-353, 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: Involved in the degradation of prenylated proteins.
CC       Cleaves the thioether bond of prenyl-L-cysteines, such as
CC       farnesylcysteine and geranylgeranylcysteine (By similarity).
CC   -!- CATALYTIC ACTIVITY: An S-prenyl-L-cysteine + O(2) + H(2)O = a
CC       prenal + L-cysteine + H(2)O(2).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- SUBCELLULAR LOCATION: Lysosome (By similarity).
CC   -!- SIMILARITY: Belongs to the prenylcysteine oxidase family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK004799; BAB23572.1; -; mRNA.
DR   EMBL; AK004840; BAB23607.1; -; mRNA.
DR   EMBL; AK031585; BAC27462.1; -; mRNA.
DR   EMBL; AK033373; BAC28252.1; -; mRNA.
DR   EMBL; AK049412; BAC33741.1; -; mRNA.
DR   EMBL; AK145366; BAE26391.1; -; mRNA.
DR   EMBL; AK147190; BAE27750.1; -; mRNA.
DR   EMBL; AK161616; BAE36494.1; -; mRNA.
DR   EMBL; AK169209; BAE40981.1; -; mRNA.
DR   EMBL; BC028308; AAH28308.1; -; mRNA.
DR   EMBL; AK173058; BAD32336.1; -; mRNA.
DR   IPI; IPI00460063; -.
DR   RefSeq; NP_080099.1; NM_025823.4.
DR   UniGene; Mm.30849; -.
DR   ProteinModelPortal; Q9CQF9; -.
DR   SMR; Q9CQF9; 32-128.
DR   PhosphoSite; Q9CQF9; -.
DR   PRIDE; Q9CQF9; -.
DR   Ensembl; ENSMUST00000032065; ENSMUSP00000032065; ENSMUSG00000029998.
DR   GeneID; 66881; -.
DR   KEGG; mmu:66881; -.
DR   UCSC; uc009cro.1; mouse.
DR   CTD; 66881; -.
DR   MGI; MGI:1914131; Pcyox1.
DR   GeneTree; ENSGT00390000011206; -.
DR   HOGENOM; HBG447064; -.
DR   HOVERGEN; HBG053532; -.
DR   InParanoid; Q9CQF9; -.
DR   OMA; SLRMHMW; -.
DR   OrthoDB; EOG469QTP; -.
DR   PhylomeDB; Q9CQF9; -.
DR   BRENDA; 1.8.3.5; 244.
DR   NextBio; 322917; -.
DR   ArrayExpress; Q9CQF9; -.
DR   Bgee; Q9CQF9; -.
DR   CleanEx; MM_PCYOX1; -.
DR   Genevestigator; Q9CQF9; -.
DR   GermOnline; ENSMUSG00000029998; Mus musculus.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0001735; F:prenylcysteine oxidase activity; IMP:MGI.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0030328; P:prenylcysteine catabolic process; IMP:MGI.
DR   InterPro; IPR010795; Prenylcys_lyase.
DR   InterPro; IPR017046; Prenylcysteine_Oxase.
DR   Pfam; PF07156; Prenylcys_lyase; 1.
DR   PIRSF; PIRSF036292; Prenylcysteine_oxidase; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; FAD; Glycoprotein; Isopeptide bond;
KW   Lysosome; Oxidoreductase; Signal; Ubl conjugation.
FT   SIGNAL        1     28       Potential.
FT   CHAIN        29    505       Prenylcysteine oxidase.
FT                                /FTId=PRO_0000023300.
FT   CARBOHYD    196    196       N-linked (GlcNAc...).
FT   CARBOHYD    323    323       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    353    353       N-linked (GlcNAc...).
FT   CROSSLNK    162    162       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CONFLICT    114    114       S -> T (in Ref. 1; BAC28252).
SQ   SEQUENCE   505 AA;  56495 MW;  9169BC4CC7D97561 CRC64;
     MGRFAAALVG SLFWLGLLLC GLGSLASAEP RAPPNRIAIV GAGIGGTSSA YYLRKKFGKD
     VKIDVFEREE VGGRLATLKV QGHDYEAGGS VIHPLNLHMK RFVKELGLSS VPASGGLVGV
     YNGKSLVFEE SSWFVINVIK LVWRYGFQSL RMHMWVEDLL DKFMRIYRYQ SHDYAFSSVE
     KLMHAIGGDD YVRLLNQTLR ENLKKAGFSE TFLNEMIAPV MKVNYGQSTD INAFVGAVSL
     TAADSNLWAV EGGNKIVCSG LLQASSSNLI SGSVMSIEEK TRTKQTGNPT KMYEVVYKTG
     SETHSDFYDI VLVAAPLNRK MSNITFRNFD PPIEEFNDPY QQLVTTFIKG ELNSTLFSSR
     PKDQFGLSAI LVTDDSDMFI NSLSIVASVR QKEGPPPAVD GMHVWKTFSR DILTKEQISK
     LFLSYDYAVR KPWLSYPHYE PPQKCPSIIL HDRLYYLNGI EFAASCMEMS AIAGYNAALL
     AYHRWNGNED MIDQDDLYER LKTEL
//
ID   ERGI2_MOUSE             Reviewed;         377 AA.
AC   Q9CR89; B2KFC8; Q3UX13; Q9CWM6; Q9CYA2; Q9D4R1; Q9D8Z9;
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=Endoplasmic reticulum-Golgi intermediate compartment protein 2;
GN   Name=Ergic2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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=Egg, Embryo, Lung, Placenta, Stomach, 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 GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting 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/6J, Czech II, and FVB/N; 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).
CC   -!- FUNCTION: Possible role in transport between endoplasmic reticulum
CC       and Golgi (By similarity).
CC   -!- SUBUNIT: May interact with EEF1A1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC       compartment membrane; Multi-pass membrane protein (By similarity).
CC       Golgi apparatus, cis-Golgi network membrane; Multi-pass membrane
CC       protein (By similarity). Endoplasmic reticulum membrane; Multi-
CC       pass membrane protein (By similarity). Cytoplasm (By similarity).
CC       Nucleus (By similarity). Note=Cycles between the endoplasmic
CC       reticulum and the Golgi.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9CR89-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CR89-2; Sequence=VSP_019211, VSP_019212;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the ERGIC family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK004661; BAB23451.1; -; mRNA.
DR   EMBL; AK007498; BAB25070.1; -; mRNA.
DR   EMBL; AK008971; BAB25998.1; -; mRNA.
DR   EMBL; AK009483; BAB26318.1; -; mRNA.
DR   EMBL; AK010529; BAB27008.1; -; mRNA.
DR   EMBL; AK016275; BAB30175.1; -; mRNA.
DR   EMBL; AK017876; BAB30984.1; -; mRNA.
DR   EMBL; AK030045; BAC26758.1; -; mRNA.
DR   EMBL; AK135968; BAE22750.1; -; mRNA.
DR   EMBL; AK167391; BAE39481.1; -; mRNA.
DR   EMBL; CU207318; CAQ51879.1; -; Genomic_DNA.
DR   EMBL; BC006895; AAH06895.1; -; mRNA.
DR   EMBL; BC018188; AAH18188.1; -; mRNA.
DR   EMBL; BC026558; AAH26558.1; -; mRNA.
DR   EMBL; BC064749; AAH64749.1; -; mRNA.
DR   IPI; IPI00133365; -.
DR   IPI; IPI00137635; -.
DR   RefSeq; NP_080444.1; NM_026168.4.
DR   RefSeq; NP_080631.1; NM_026355.3.
DR   UniGene; Mm.59812; -.
DR   ProteinModelPortal; Q9CR89; -.
DR   PhosphoSite; Q9CR89; -.
DR   PRIDE; Q9CR89; -.
DR   Ensembl; ENSMUST00000032446; ENSMUSP00000032446; ENSMUSG00000030304.
DR   Ensembl; ENSMUST00000032447; ENSMUSP00000032447; ENSMUSG00000030304.
DR   GeneID; 67456; -.
DR   KEGG; mmu:67456; -.
DR   UCSC; uc009etd.1; mouse.
DR   UCSC; uc009etg.1; mouse.
DR   CTD; 67456; -.
DR   MGI; MGI:1914706; Ergic2.
DR   eggNOG; roNOG09522; -.
DR   GeneTree; ENSGT00530000063113; -.
DR   HOGENOM; HBG315080; -.
DR   HOVERGEN; HBG054683; -.
DR   InParanoid; Q9CR89; -.
DR   OMA; FITIVPT; -.
DR   PhylomeDB; Q9CR89; -.
DR   NextBio; 324624; -.
DR   ArrayExpress; Q9CR89; -.
DR   Bgee; Q9CR89; -.
DR   CleanEx; MM_ERGIC2; -.
DR   Genevestigator; Q9CR89; -.
DR   GermOnline; ENSMUSG00000030304; Mus musculus.
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: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   GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; ISS:HGNC.
DR   InterPro; IPR012936; DUF1692.
DR   Pfam; PF07970; DUF1692; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Endoplasmic reticulum;
KW   ER-Golgi transport; Golgi apparatus; Membrane; Nucleus; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    377       Endoplasmic reticulum-Golgi intermediate
FT                                compartment protein 2.
FT                                /FTId=PRO_0000239384.
FT   TOPO_DOM      1     33       Cytoplasmic (Potential).
FT   TRANSMEM     34     54       Helical; (Potential).
FT   TOPO_DOM     55    319       Lumenal (Potential).
FT   TRANSMEM    320    340       Helical; (Potential).
FT   TOPO_DOM    341    377       Cytoplasmic (Potential).
FT   VAR_SEQ     276    302       ERIINHAAGSHGVSGIFMKYDLSSLMV -> RSLSKIQWEK
FT                                QKNAVCKVYCVVAMTED (in isoform 2).
FT                                /FTId=VSP_019211.
FT   VAR_SEQ     303    377       Missing (in isoform 2).
FT                                /FTId=VSP_019212.
FT   CONFLICT      3      3       R -> G (in Ref. 3; BAB25070).
FT   CONFLICT    220    220       L -> C (in Ref. 3; BAB30984).
FT   CONFLICT    254    254       V -> M (in Ref. 3; BAB30984).
FT   CONFLICT    277    277       R -> S (in Ref. 3; BAB30984).
FT   CONFLICT    341    341       E -> D (in Ref. 3; BAB27008).
SQ   SEQUENCE   377 AA;  42482 MW;  0FF37E719401C824 CRC64;
     MRRLNRRKTL SLVKELDAFP KVPDSYVETS ASGGTVSLIA FTTMALLTIM EFSVYQDTWM
     KYEYEVDKDF SSKLRINIDI TVAMKCHYVG ADVLDLAETM VASADGLAYE PALFDLSPQQ
     REWQRMLQLI QSRLQEEHSL QDVIFKSAFK SASTALPPRE DDSSLTPDAC RIHGHLYVNK
     VAGNFHITVG KAIPHPRGHA HLAALVNHDS YNFSHRIDHL SFGELVPGII NPLDGTEKIA
     VDHNQMFQYF ITVVPTKLHT YKISADTHQF SVTERERIIN HAAGSHGVSG IFMKYDLSSL
     MVTVTEEHMP FWQFFVRLCG IIGGIFSTTG MLHGIGKFIV EIICCRFRLG SYKPVRSVPF
     ADGHTDNHLP LLENNTH
//
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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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   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   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.
CC   -----------------------------------------------------------------------
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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   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.
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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   YIF1B_MOUSE             Reviewed;         311 AA.
AC   Q9CX30; Q32M25; Q3UXJ5;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Protein YIF1B;
DE   AltName: Full=YIP1-interacting factor homolog B;
GN   Name=Yif1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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 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] (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   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9CX30-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CX30-2; Sequence=VSP_028656;
CC   -!- SIMILARITY: Belongs to the YIF1 family.
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DR   EMBL; AK020444; BAB32103.1; -; mRNA.
DR   EMBL; AK135529; BAE22568.1; -; mRNA.
DR   EMBL; BC109331; AAI09332.1; -; mRNA.
DR   IPI; IPI00317932; -.
DR   IPI; IPI00857684; -.
DR   RefSeq; NP_001103671.1; NM_001110201.1.
DR   RefSeq; NP_084163.2; NM_029887.3.
DR   UniGene; Mm.36699; -.
DR   ProteinModelPortal; Q9CX30; -.
DR   IntAct; Q9CX30; 2.
DR   PhosphoSite; Q9CX30; -.
DR   PRIDE; Q9CX30; -.
DR   Ensembl; ENSMUST00000032809; ENSMUSP00000032809; ENSMUSG00000030588.
DR   GeneID; 77254; -.
DR   KEGG; mmu:77254; -.
DR   NMPDR; fig|10090.3.peg.16080; -.
DR   UCSC; uc009gbi.1; mouse.
DR   CTD; 77254; -.
DR   MGI; MGI:1924504; Yif1b.
DR   eggNOG; roNOG11376; -.
DR   GeneTree; ENSGT00390000009423; -.
DR   HOGENOM; HBG745098; -.
DR   HOVERGEN; HBG053252; -.
DR   InParanoid; Q9CX30; -.
DR   OMA; AAQPVFM; -.
DR   OrthoDB; EOG40S0G5; -.
DR   PhylomeDB; Q9CX30; -.
DR   NextBio; 346649; -.
DR   ArrayExpress; Q9CX30; -.
DR   Bgee; Q9CX30; -.
DR   CleanEx; MM_YIF1B; -.
DR   Genevestigator; Q9CX30; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR005578; Hrf1.
DR   PANTHER; PTHR14083; Hrf1; 1.
DR   Pfam; PF03878; YIF1; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    311       Protein YIF1B.
FT                                /FTId=PRO_0000307259.
FT   TOPO_DOM      1    153       Cytoplasmic (Potential).
FT   TRANSMEM    154    174       Helical; (Potential).
FT   TOPO_DOM    175    189       Extracellular (Potential).
FT   TRANSMEM    190    210       Helical; (Potential).
FT   TOPO_DOM    211    216       Cytoplasmic (Potential).
FT   TRANSMEM    217    237       Helical; (Potential).
FT   TOPO_DOM    238    238       Extracellular (Potential).
FT   TRANSMEM    239    259       Helical; (Potential).
FT   TOPO_DOM    260    289       Cytoplasmic (Potential).
FT   TRANSMEM    290    310       Helical; (Potential).
FT   TOPO_DOM    311    311       Extracellular (Potential).
FT   MOD_RES      64     64       Phosphoserine (By similarity).
FT   VAR_SEQ      16     18       Missing (in isoform 2).
FT                                /FTId=VSP_028656.
FT   CONFLICT    160    160       A -> G (in Ref. 1; BAB32103).
FT   CONFLICT    197    197       E -> K (in Ref. 1; BAB32103).
FT   CONFLICT    277    277       V -> E (in Ref. 1; BAE22568).
SQ   SEQUENCE   311 AA;  33983 MW;  BFC353B2D2C37074 CRC64;
     MHATGLAAPA GTPRLRKWPS KRRVPVSQPG MADPHQFFDD TSSAPSRGYG GQPSPGGLGY
     PPSSSDAAFL AAPMSNMAMV YGSSLAAQGK ELVDKNIDRF IPVSKLKYYF AVDTVYVGKK
     LGLLVFPYLH QDWEVQYQQD TPVAPRFDIN APDLYIPAMA FITYILVAGL ALGTQDRFSP
     DLLGLQASSA LAWLTLEVVA ILLSLYLVTV NTDLTTIDLV AFLGYKYVGM IGGVLTGLLF
     GKIGYYLVLA WCCVSIFVFM IRTLRLKILA QAAAEGVPVR GARNQLRMYL TMAVAAAQPV
     LMYWLTFHLV R
//
ID   Q9CX86_MOUSE            Unreviewed;       305 AA.
AC   Q9CX86;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Hnrnpa0; Synonyms=Hnrpa0, Klhl3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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 (AUG-2000) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK019388; BAB31694.1; -; mRNA.
DR   IPI; IPI00109813; -.
DR   RefSeq; NP_084148.1; NM_029872.1.
DR   UniGene; Mm.148973; -.
DR   HSSP; P09651; 1HA1.
DR   ProteinModelPortal; Q9CX86; -.
DR   SMR; Q9CX86; 2-174.
DR   STRING; Q9CX86; -.
DR   PhosphoSite; Q9CX86; -.
DR   PRIDE; Q9CX86; -.
DR   Ensembl; ENSMUST00000007980; ENSMUSP00000007980; ENSMUSG00000007836.
DR   GeneID; 77134; -.
DR   KEGG; mmu:77134; -.
DR   CTD; 77134; -.
DR   MGI; MGI:1924384; Hnrnpa0.
DR   eggNOG; maNOG10470; -.
DR   GeneTree; ENSGT00560000076532; -.
DR   HOGENOM; HBG756718; -.
DR   HOVERGEN; HBG002295; -.
DR   InParanoid; Q9CX86; -.
DR   OMA; DQLCKLF; -.
DR   OrthoDB; EOG4W6NX4; -.
DR   NextBio; 346544; -.
DR   ArrayExpress; Q9CX86; -.
DR   Bgee; Q9CX86; -.
DR   Genevestigator; Q9CX86; -.
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   305 AA;  30530 MW;  B3F3BB8C5480BB56 CRC64;
     MENSQLCKLF IGGLNVQTSE SGLRGHFEAF GTLTDCVVVV NPQTKRSRCF GFVTYSNVEE
     ADAAMAASPH AVDGNTVELK RAVSREDSAR PGAHAKVKKL FVGGLKGDVA EGDLIEHFSQ
     FGAVEKAEII ADKQSGKKRG FGFVYFQSHD AADKAAVVKF HPIQGHRVEV KKAVPKEDIH
     AGGGGARAAR GGRGGGRGRG GGGGGGGRDQ NGLAKGGGGG GGGYNSYGGY GGYGAYGGGG
     GGGGSYGGSD YGNGFGGFGS YSQHQSSYGP MKSGGGGGGG GSWGGRSNSG PYRGGYGGGY
     GGGSF
//
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   TOM70_MOUSE             Reviewed;         611 AA.
AC   Q9CZW5;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Mitochondrial import receptor subunit TOM70;
DE   AltName: Full=Mitochondrial precursor proteins import receptor;
DE   AltName: Full=Translocase of outer membrane 70 kDa subunit;
GN   Name=Tomm70a; Synonyms=D16Wsu109e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; 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 163-171; 330-357; 451-466 AND 520-527, 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   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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-88 AND SER-94, 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-94, 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-94, 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 that accelerates the import of all
CC       mitochondrial precursor proteins (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 CAPN8.
CC   -!- INTERACTION:
CC       Q8K443:Rgs13; NbExp=2; IntAct=EBI-642469, EBI-645999;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC       membrane protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in the base region of the oxyntic
CC       and pyloric mucosae.
CC   -!- SIMILARITY: Belongs to the Tom70 family.
CC   -!- SIMILARITY: Contains 10 TPR repeats.
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DR   EMBL; AK012084; BAB28018.1; -; mRNA.
DR   IPI; IPI00377728; -.
DR   UniGene; Mm.213292; -.
DR   ProteinModelPortal; Q9CZW5; -.
DR   SMR; Q9CZW5; 4-609.
DR   IntAct; Q9CZW5; 14.
DR   STRING; Q9CZW5; -.
DR   PhosphoSite; Q9CZW5; -.
DR   PRIDE; Q9CZW5; -.
DR   Ensembl; ENSMUST00000023433; ENSMUSP00000023433; ENSMUSG00000022752.
DR   MGI; MGI:106295; Tomm70a.
DR   GeneTree; ENSGT00600000084276; -.
DR   HOVERGEN; HBG062335; -.
DR   InParanoid; Q9CZW5; -.
DR   OrthoDB; EOG4GB75W; -.
DR   PhylomeDB; Q9CZW5; -.
DR   ArrayExpress; Q9CZW5; -.
DR   Bgee; Q9CZW5; -.
DR   Genevestigator; Q9CZW5; -.
DR   GermOnline; ENSMUSG00000022752; 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   GO; GO:0005515; F:protein binding; IPI:IntAct.
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   Acetylation; Direct protein sequencing; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Phosphoprotein; Repeat; TPR repeat;
KW   Transmembrane; Transmembrane helix.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    611       Mitochondrial import receptor subunit
FT                                TOM70.
FT                                /FTId=PRO_0000106337.
FT   TOPO_DOM      2     41       Mitochondrial intermembrane (Potential).
FT   TRANSMEM     42     62       Helical; (Potential).
FT   TOPO_DOM     63    611       Cytoplasmic (Potential).
FT   REPEAT      117    150       TPR 1.
FT   REPEAT      156    189       TPR 2.
FT   REPEAT      297    330       TPR 3.
FT   REPEAT      332    365       TPR 4.
FT   REPEAT      370    403       TPR 5.
FT   REPEAT      404    437       TPR 6.
FT   REPEAT      445    478       TPR 7.
FT   REPEAT      479    512       TPR 8.
FT   REPEAT      514    547       TPR 9.
FT   REPEAT      548    581       TPR 10.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      88     88       Phosphothreonine.
FT   MOD_RES      94     94       Phosphoserine.
FT   MOD_RES     188    188       N6-acetyllysine (By similarity).
FT   MOD_RES     473    473       N6-acetyllysine (By similarity).
SQ   SEQUENCE   611 AA;  67521 MW;  486FB79FC4CE5B4F CRC64;
     MAASKPIEAA MAAAAAPGSG NGVGGGGGTA GPGSGAGTLP RWHVALAIGA PLLLGAGAMY
     LWSRRRRRRE AGGRGDASGL KRNSERKTPE GRASPALGSG HHDGSGDSLE MSSLDSAQAA
     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   VPS28_MOUSE             Reviewed;         221 AA.
AC   Q9D1C8;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Vacuolar protein sorting-associated protein 28 homolog;
DE   AltName: Full=Caspase-activated DNase inhibitor that interacts with ASK1;
DE            Short=CIIA;
DE   AltName: Full=ESCRT-I complex subunit VPS28;
GN   Name=Vps28;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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=22919458; PubMed=14557248; DOI=10.1083/jcb.200303003;
RA   Cho S.-G., Kim J.W., Lee Y.H., Hwang H.S., Kim M.S., Ryoo K.,
RA   Kim M.J., Noh K.T., Kim E.K., Cho J.H., Yoon K.W., Cho E.G.,
RA   Park H.S., Chi S.W., Lee M.J., Kang S.S., Ichijo H., Choi E.J.;
RT   "Identification of a novel antiapoptotic protein that antagonizes ASK1
RT   and CAD activities.";
RL   J. Cell Biol. 163:71-81(2003).
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=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 ESCRT-I complex, a regulator of
CC       vesicular trafficking process (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, VPS37B,
CC       VPS37C, FAM125A and FAM125B. Interacts WITH VPS36; the interaction
CC       mediates the association with the ESCRT-II complex. Interacts with
CC       SNF8 and VPS25. Interacts with CEP55 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane (By similarity). Late endosome
CC       membrane; Peripheral membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the VPS28 family.
CC   -!- SIMILARITY: Contains 1 VPS28 C-terminal domain.
CC   -!- SIMILARITY: Contains 1 VPS28 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; AF373710; AAN71982.1; -; mRNA.
DR   EMBL; AK003699; BAB22945.1; -; mRNA.
DR   EMBL; BC013535; AAH13535.1; -; mRNA.
DR   IPI; IPI00133591; -.
DR   RefSeq; NP_080118.1; NM_025842.3.
DR   UniGene; Mm.30028; -.
DR   ProteinModelPortal; Q9D1C8; -.
DR   SMR; Q9D1C8; 18-120, 123-220.
DR   MINT; MINT-218076; -.
DR   STRING; Q9D1C8; -.
DR   PRIDE; Q9D1C8; -.
DR   Ensembl; ENSMUST00000078803; ENSMUSP00000077856; ENSMUSG00000062381.
DR   GeneID; 66914; -.
DR   KEGG; mmu:66914; -.
DR   UCSC; uc007wlc.1; mouse.
DR   CTD; 66914; -.
DR   MGI; MGI:1914164; Vps28.
DR   GeneTree; ENSGT00390000007486; -.
DR   HOGENOM; HBG559171; -.
DR   HOVERGEN; HBG054248; -.
DR   InParanoid; Q9D1C8; -.
DR   OMA; GNTSKCI; -.
DR   OrthoDB; EOG4TQMB1; -.
DR   PhylomeDB; Q9D1C8; -.
DR   NextBio; 323003; -.
DR   ArrayExpress; Q9D1C8; -.
DR   Bgee; Q9D1C8; -.
DR   CleanEx; MM_VPS28; -.
DR   Genevestigator; Q9D1C8; -.
DR   GermOnline; ENSMUSG00000062381; Mus musculus.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR007143; VPS28.
DR   InterPro; IPR017899; VPS28_C.
DR   InterPro; IPR017898; VPS28_N.
DR   PANTHER; PTHR12937; VPS28; 1.
DR   Pfam; PF03997; VPS28; 1.
DR   PIRSF; PIRSF017535; VPS28; 1.
DR   PROSITE; PS51310; VPS28_C; 1.
DR   PROSITE; PS51313; VPS28_N; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Endosome; Membrane; Protein transport; Transport.
FT   CHAIN         1    221       Vacuolar protein sorting-associated
FT                                protein 28 homolog.
FT                                /FTId=PRO_0000120952.
FT   DOMAIN       13    120       VPS28 N-terminal.
FT   DOMAIN      124    220       VPS28 C-terminal.
SQ   SEQUENCE   221 AA;  25452 MW;  DC144A4A27857245 CRC64;
     MFHGIPATPG VGAPGNKPEL YEEVKLYKNA REREKYDNMA ELFAVVKTMQ ALEKAYIKDC
     VTPNEYTAAC SRLLVQYKAA FRQVQGSEIS SIDEFCRKFR LDCPLAMERI KEDRPITIKD
     DKGNLNRCIA DVVSLFITVM DKLRLEIRAM DEIQPDLREL METMHRMSHL PPDFEGRQTV
     SQWLQTLSGM SASDELDDSQ VRQMLFDLES AYNAFNRFLH A
//
ID   ERP44_MOUSE             Reviewed;         406 AA.
AC   Q9D1Q6; Q3TVI1; Q6A045;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Endoplasmic reticulum resident protein 44;
DE            Short=ER protein 44;
DE            Short=ERp44;
DE   AltName: Full=Thioredoxin domain-containing protein 4;
DE   Flags: Precursor;
GN   Name=Erp44; Synonyms=Kiaa0573, Txndc4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; 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   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   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   INTERACTION WITH ITPR1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   MUTAGENESIS OF CYS-58.
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).
CC   -!- FUNCTION: Mediates thiol-dependent retention in the early
CC       secretory pathway, forming mixed disulfides with substrate
CC       proteins through its conserved CRFS motif. Inhibits the calcium
CC       channel activity of ITPR1. May have a role in the control of
CC       oxidative protein folding in the endoplasmic reticulum. Required
CC       to retain ERO1L and ERO1LB in the endoplasmic reticulum (By
CC       similarity).
CC   -!- SUBUNIT: Forms mixed disulfides with both ERO1L and ERO1LB and
CC       cargo folding intermediates (By similarity). Directly interacts
CC       with ITPR1 in a pH-, redox state- and calcium-dependent manner,
CC       but not with ITPR2 or ITPR3. The strength of this interaction
CC       inversely correlates with calcium concentration.
CC   -!- INTERACTION:
CC       P11881:Itpr1; NbExp=2; IntAct=EBI-541567, EBI-541478;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32251.1; 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; AK003217; BAB22648.1; -; mRNA.
DR   EMBL; AK151497; BAE30449.1; -; mRNA.
DR   EMBL; AK160113; BAE35637.1; -; mRNA.
DR   EMBL; AK172973; BAD32251.1; ALT_INIT; mRNA.
DR   EMBL; BC019558; AAH19558.1; -; mRNA.
DR   IPI; IPI00134058; -.
DR   RefSeq; NP_083848.1; NM_029572.2.
DR   UniGene; Mm.317701; -.
DR   ProteinModelPortal; Q9D1Q6; -.
DR   SMR; Q9D1Q6; 33-401.
DR   IntAct; Q9D1Q6; 6.
DR   MINT; MINT-4138820; -.
DR   STRING; Q9D1Q6; -.
DR   REPRODUCTION-2DPAGE; IPI00134058; -.
DR   REPRODUCTION-2DPAGE; Q9D1Q6; -.
DR   PRIDE; Q9D1Q6; -.
DR   Ensembl; ENSMUST00000030028; ENSMUSP00000030028; ENSMUSG00000028343.
DR   GeneID; 76299; -.
DR   KEGG; mmu:76299; -.
DR   UCSC; uc008suy.1; mouse.
DR   CTD; 76299; -.
DR   MGI; MGI:1923549; Erp44.
DR   eggNOG; roNOG08460; -.
DR   GeneTree; ENSGT00390000015018; -.
DR   HOGENOM; HBG377698; -.
DR   InParanoid; Q9D1Q6; -.
DR   OMA; GSMTNFD; -.
DR   OrthoDB; EOG4Z0B5R; -.
DR   PhylomeDB; Q9D1Q6; -.
DR   NextBio; 344925; -.
DR   ArrayExpress; Q9D1Q6; -.
DR   Bgee; Q9D1Q6; -.
DR   Genevestigator; Q9D1Q6; -.
DR   GermOnline; ENSMUSG00000028343; Mus musculus.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; ISS:UniProtKB.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0009100; P:glycoprotein metabolic process; ISS:UniProtKB.
DR   GO; GO:0006457; P:protein folding; ISS:UniProtKB.
DR   GO; GO:0006986; P:response to unfolded protein; ISS:UniProtKB.
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; 2.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 3.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Disulfide bond; Endoplasmic reticulum; Signal.
FT   SIGNAL        1     29       By similarity.
FT   CHAIN        30    406       Endoplasmic reticulum resident protein
FT                                44.
FT                                /FTId=PRO_0000034181.
FT   DOMAIN       30    138       Thioredoxin.
FT   REGION      236    285       Interaction with ITPR1.
FT   MOTIF       403    406       Prevents secretion from ER (Potential).
FT   DISULFID    189    241       By similarity.
FT   DISULFID    301    318       By similarity.
FT   MUTAGEN      58     58       C->S: No effect on interaction with
FT                                ITPR1.
SQ   SEQUENCE   406 AA;  46853 MW;  F87935A5EB932927 CRC64;
     MNPAVFLSLA DLRCSLLLLV TSIFTPITAE IASLDSENID EILNNADVAL VNFYADWCRF
     SQMLHPIFEE ASDVIKEEYP DKNQVVFARV DCDQHSDIAQ RYRISKYPTL KLFRNGMMMK
     REYRGQRSVK ALADYIRQQK SNPVHEIQSL DEVTNLDRSK RNIIGYFEQK DSENYRVFER
     VASILHDDCA FLSAFGDLSK PERYNGDNVI YKPPGRSAPD MVYLGSMTNF DVTYNWIQDK
     CVPLVREITF ENGEELTEEG LPFLILFHMK DDTESLEIFQ NEVARQLISE KGTINFLHAD
     CDKFRHPLLH IQKTPADCPV IAIDSFRHMY VFGDFKDVLI PGKLKQFVFD LHSGKLHREF
     HHGPDPTDTA PGEQDQDVAS SPPESSFQKL APSEYRYTLL RDRDEL
//
ID   SP2_MOUSE               Reviewed;         612 AA.
AC   Q9D2H6; Q6A0E1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   08-FEB-2011, entry version 76.
DE   RecName: Full=Transcription factor Sp2;
GN   Name=Sp2; Synonyms=Kiaa0048;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; 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).
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   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   -!- FUNCTION: Binds to GC box promoters elements and selectively
CC       activates mRNA synthesis from genes that contain functional
CC       recognition sites (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9D2H6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D2H6-2; Sequence=VSP_022022;
CC   -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein
CC       family.
CC   -!- SIMILARITY: Contains 3 C2H2-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH21759.1; Type=Erroneous initiation;
CC       Sequence=AAH86457.1; Type=Erroneous initiation;
CC       Sequence=BAD32155.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK172877; BAD32155.1; ALT_INIT; Transcribed_RNA.
DR   EMBL; AK019649; BAB31823.1; -; mRNA.
DR   EMBL; BC021759; AAH21759.1; ALT_INIT; mRNA.
DR   EMBL; BC086457; AAH86457.1; ALT_INIT; mRNA.
DR   IPI; IPI00469258; -.
DR   IPI; IPI00816909; -.
DR   RefSeq; NP_001074433.1; NM_001080964.1.
DR   RefSeq; NP_084496.2; NM_030220.3.
DR   UniGene; Mm.155547; -.
DR   HSSP; P08047; 1SP2.
DR   ProteinModelPortal; Q9D2H6; -.
DR   SMR; Q9D2H6; 517-610.
DR   PhosphoSite; Q9D2H6; -.
DR   PRIDE; Q9D2H6; -.
DR   Ensembl; ENSMUST00000107626; ENSMUSP00000103252; ENSMUSG00000018678.
DR   GeneID; 78912; -.
DR   KEGG; mmu:78912; -.
DR   UCSC; uc007ldf.1; mouse.
DR   UCSC; uc007ldg.1; mouse.
DR   CTD; 78912; -.
DR   MGI; MGI:1926162; Sp2.
DR   GeneTree; ENSGT00590000082841; -.
DR   HOVERGEN; HBG008933; -.
DR   InParanoid; Q9D2H6; -.
DR   NextBio; 349734; -.
DR   ArrayExpress; Q9D2H6; -.
DR   Bgee; Q9D2H6; -.
DR   CleanEx; MM_SP2; -.
DR   Genevestigator; Q9D2H6; -.
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; 2.
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   Activator; Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    612       Transcription factor Sp2.
FT                                /FTId=PRO_0000269192.
FT   ZN_FING     524    548       C2H2-type 1.
FT   ZN_FING     554    578       C2H2-type 2.
FT   ZN_FING     584    606       C2H2-type 3.
FT   MOD_RES     191    191       Phosphothreonine (By similarity).
FT   MOD_RES     549    549       Phosphothreonine (By similarity).
FT   VAR_SEQ       1      7       Missing (in isoform 2).
FT                                /FTId=VSP_022022.
FT   CONFLICT      6      6       M -> T (in Ref. 3; AAH86457).
FT   CONFLICT     97     97       Missing (in Ref. 1; BAD32155).
SQ   SEQUENCE   612 AA;  64908 MW;  FF2778DC55B4044F CRC64;
     MSDPQMSMAA TAAVSPSDYL QPAAATTQDS QPSPLALLAA TCSKIGPPAV EAAVTPPAPP
     QPTPRKLVPI KPAPLPLSPC KNSFSILSSK GNILQIQGSQ LSTSYPGGQF VFAIQNPTLI
     NKGSRSNASI QYQVPQIQGN SSQTIQVQPS LTNQIQVIPG TNQAITTPST SGHKPVPIKP
     APVQKSSTTT TPVQSGANVV KLTGGGSNMT LTLPLNNLVN TSDIGGPAQL LTESPPTPLS
     KTNKKARKKS LPVSQPSVAV AEQVETVLIE TTADNIIQAG NNLLIVQSPG GGQPAVVQQV
     QVVPPKAEQQ QVVQIPQQAL RVVQAASATL PTVPQKPSQN FQIQTTEPTP TQVYIRTPSG
     EVQTVLVQDS PPATAATTST VTCNSPALRA PHLSGTSKKH SAAILRKERP LPKIAPAGSI
     ISLNAAQLAA AAQAMQTINI NGVQVQGVPV TITNTGGQQQ LTVQNVSGNN LTISGLSPTQ
     IQLQMEQALA GEAQPGEKRR RMACTCPNCK DGEKRSGEQG KKKHVCHIPD CGKTFRKTSL
     LRAHVRLHTG ERPFVCNWFF CGKRFTRSDE LQRHARTHTG DKRFECAQCQ KRFMRSDHLT
     KHYKTHLGTK GL
//
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   -----------------------------------------------------------------------
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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   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   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   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   CL023_MOUSE             Reviewed;         115 AA.
AC   Q9DAM7;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=UPF0444 transmembrane protein C12orf23 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=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].
RC   STRAIN=C57BL/6J; 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: Belongs to the UPF0444 family.
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DR   EMBL; AK005698; BAB24195.1; -; mRNA.
DR   EMBL; AK142035; BAE24921.1; -; mRNA.
DR   EMBL; BC086492; AAH86492.1; -; mRNA.
DR   IPI; IPI00118827; -.
DR   RefSeq; NP_001013046.1; NM_001013028.2.
DR   UniGene; Mm.335025; -.
DR   PRIDE; Q9DAM7; -.
DR   Ensembl; ENSMUST00000095383; ENSMUSP00000093030; ENSMUSG00000060935.
DR   GeneID; 103266; -.
DR   KEGG; mmu:103266; -.
DR   UCSC; uc007glb.1; mouse.
DR   MGI; MGI:2143652; AI597468.
DR   eggNOG; roNOG16572; -.
DR   GeneTree; ENSGT00390000013899; -.
DR   HOGENOM; HBG445423; -.
DR   HOVERGEN; HBG058969; -.
DR   InParanoid; Q9DAM7; -.
DR   OMA; GIFNVTK; -.
DR   OrthoDB; EOG4D7Z7B; -.
DR   PhylomeDB; Q9DAM7; -.
DR   NextBio; 355870; -.
DR   ArrayExpress; Q9DAM7; -.
DR   Bgee; Q9DAM7; -.
DR   CleanEx; MM_AI597468; -.
DR   Genevestigator; Q9DAM7; -.
DR   GermOnline; ENSMUSG00000060935; 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    115       UPF0444 transmembrane protein C12orf23
FT                                homolog.
FT                                /FTId=PRO_0000263630.
FT   TRANSMEM     39     59       Helical; (Potential).
FT   TRANSMEM     77     97       Helical; (Potential).
SQ   SEQUENCE   115 AA;  11549 MW;  4C3E54AFD5199F59 CRC64;
     MNQADKNQEI PSYLSDEPPE GSMKDHPQQQ PGMLSRVTGG IFSVTKGAVG ATIGGVAWIG
     GKSLEVTKTA VTTVPSMGIG LVKGGVSAVA GGVTAVGSAV VNKVPLSGKK KDKSD
//
ID   PLIN3_MOUSE             Reviewed;         437 AA.
AC   Q9DBG5; Q3TK05; Q8BKV9; Q9CZK1;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Perilipin-3;
DE   AltName: Full=Cargo selection protein TIP47;
DE   AltName: Full=Mannose-6-phosphate receptor-binding protein 1;
GN   Name=Plin3; Synonyms=M6prbp1, Tip47;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; 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 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=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and 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 (2.8 ANGSTROMS) OF 191-437.
RX   PubMed=15242596; DOI=10.1016/j.str.2004.04.021;
RA   Hickenbottom S.J., Kimmel A.R., Londos C., Hurley J.H.;
RT   "Structure of a lipid droplet protein; the PAT family member TIP47.";
RL   Structure 12:1199-1207(2004).
CC   -!- FUNCTION: Required for the transport of mannose 6-phosphate
CC       receptors (MPR) from endosomes to the trans-Golgi network (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with the cytoplasmic domains of both M6PR and
CC       IGF2R. Homooligomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Endosome
CC       membrane; Peripheral membrane protein; Cytoplasmic side (By
CC       similarity). Lipid droplet (By similarity). Note=Membrane
CC       associated on endosomes. Detected in the envelope and the core of
CC       lipid bodies and in lipid sails (By similarity).
CC   -!- SIMILARITY: Belongs to the perilipin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC33798.1; Type=Frameshift; Positions=400;
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DR   EMBL; AK004970; BAB23708.1; -; mRNA.
DR   EMBL; AK012517; BAB28291.1; -; mRNA.
DR   EMBL; AK049537; BAC33798.1; ALT_FRAME; mRNA.
DR   EMBL; AK050140; BAC34089.1; -; mRNA.
DR   EMBL; AK132313; BAE21098.1; -; mRNA.
DR   EMBL; AK167214; BAE39340.1; -; mRNA.
DR   EMBL; BC011116; AAH11116.1; -; mRNA.
DR   IPI; IPI00319270; -.
DR   RefSeq; NP_080112.1; NM_025836.3.
DR   UniGene; Mm.311696; -.
DR   PDB; 1SZI; X-ray; 2.80 A; A=191-437.
DR   PDBsum; 1SZI; -.
DR   ProteinModelPortal; Q9DBG5; -.
DR   SMR; Q9DBG5; 206-431.
DR   IntAct; Q9DBG5; 1.
DR   STRING; Q9DBG5; -.
DR   PhosphoSite; Q9DBG5; -.
DR   REPRODUCTION-2DPAGE; IPI00319270; -.
DR   PRIDE; Q9DBG5; -.
DR   Ensembl; ENSMUST00000019726; ENSMUSP00000019726; ENSMUSG00000024197.
DR   GeneID; 66905; -.
DR   KEGG; mmu:66905; -.
DR   UCSC; uc008dbn.1; mouse.
DR   CTD; 66905; -.
DR   MGI; MGI:1914155; Plin3.
DR   eggNOG; maNOG15210; -.
DR   GeneTree; ENSGT00500000044795; -.
DR   HOGENOM; HBG714626; -.
DR   HOVERGEN; HBG002935; -.
DR   InParanoid; Q9DBG5; -.
DR   OMA; VGQMVLS; -.
DR   OrthoDB; EOG41ZFB4; -.
DR   PhylomeDB; Q9DBG5; -.
DR   NextBio; 322981; -.
DR   ArrayExpress; Q9DBG5; -.
DR   Bgee; Q9DBG5; -.
DR   CleanEx; MM_M6PRBP1; -.
DR   Genevestigator; Q9DBG5; -.
DR   GermOnline; ENSMUSG00000024197; Mus musculus.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005811; C:lipid particle; IEA:UniProtKB-SubCell.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR004279; Perilipin.
DR   PANTHER; PTHR14024; Perilipin; 1.
DR   Pfam; PF03036; Perilipin; 1.
DR   PIRSF; PIRSF036881; PAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Endosome; Lipid droplet;
KW   Membrane; Phosphoprotein; Transport.
FT   CHAIN         1    437       Perilipin-3.
FT                                /FTId=PRO_0000099891.
FT   MOD_RES      65     65       N6-acetyllysine (By similarity).
FT   MOD_RES     130    130       Phosphoserine (By similarity).
FT   MOD_RES     174    174       Phosphothreonine (By similarity).
FT   MOD_RES     179    179       Phosphoserine (By similarity).
FT   MOD_RES     183    183       Phosphoserine (By similarity).
FT   STRAND      207    210
FT   HELIX       212    216
FT   HELIX       227    235
FT   STRAND      239    242
FT   HELIX       243    245
FT   HELIX       248    287
FT   HELIX       324    350
FT   TURN        351    354
FT   HELIX       357    376
FT   HELIX       377    379
FT   HELIX       383    385
FT   HELIX       388    413
FT   STRAND      421    427
SQ   SEQUENCE   437 AA;  47262 MW;  F7CDD3A754A5C04D CRC64;
     MSSNGTDAPA EAQAAMEEPV VQPSVVDRVA GLPLISSTYG MVSAAYTSTK ENYPHVRTVC
     DVAEKGVKTL TTAAVSTAQP ILSKLEPQIA TASEYAHRGL DRLQESLPIL QQPTEKVLAD
     TKELVSSTVS GAQEMVSSSV SSAKETVATR VTGAVDVTLG AVQNSVDKTK SAMTSGVQSV
     MGSRVGQMVI SGVDRVLVKS EAWADNRLPL TEAELALIAT PPEDSDMASL QQQRQEQNYF
     VRLGSLSERL RNHAYEHSLG KLQNARQKAQ ETLQQLTSVL GLMESVKQGV DQRLGEGQEK
     LHQMWLSWNQ KTPQDAEKDP AKPEQVEARA LSMFRDITQQ LQSMCVALGA SIQGLPSHVR
     EQAQQARSQV NDLQATFSGI HSFQDLSAGV LAQTRERIAR AREALDNTVE YVAQNTPAMW
     LVGPFAPGIT EKTPEGK
//
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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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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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   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   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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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   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   -----------------------------------------------------------------------
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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   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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   CRIP2_MOUSE             Reviewed;         208 AA.
AC   Q9DCT8;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Cysteine-rich protein 2;
DE            Short=CRP-2;
DE   AltName: Full=Heart LIM protein;
GN   Name=Crip2; Synonyms=Crp2, Hlp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; 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 DEVELOPMENTAL STAGE.
RC   STRAIN=129/Sv; TISSUE=Heart;
RX   MEDLINE=22126604; PubMed=12128222; DOI=10.1016/S0925-4773(02)00139-9;
RA   Yu T.S., Moctezuma-Anaya M., Kubo A., Keller G., Robertson S.;
RT   "The heart LIM protein gene (Hlp), expressed in the developing and
RT   adult heart, defines a new tissue-specific LIM-only protein family.";
RL   Mech. Dev. 116:187-192(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
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   [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).
RN   [5]
RP   INTERACTION WITH TGFB1I1.
RX   PubMed=15713747; DOI=10.1242/jcs.01683;
RA   Kim-Kaneyama J.-R., Suzuki W., Ichikawa K., Ohki T., Kohno Y.,
RA   Sata M., Nose K., Shibanuma M.;
RT   "Uni-axial stretching regulates intracellular localization of Hic-5
RT   expressed in smooth-muscle cells in vivo.";
RL   J. Cell Sci. 118:937-949(2005).
CC   -!- SUBUNIT: Interacts with TGFB1I1.
CC   -!- DEVELOPMENTAL STAGE: In the embryo, its expression is primarily
CC       restricted to the developing heart. In situ hybridization showed
CC       expression at E7.75 in the paired heart-forming primordia prior to
CC       linear heart-tube formation. At E8.5, strong expression is
CC       detected in the heart, with equal expression in both heart
CC       chambers. Expression is detected in both myocardium and
CC       endocardium, and in vascular endothelium. Later in fetal
CC       development low levels of expression is detected outside the
CC       heart, including dorsal root ganglia and the spinal cord. In the
CC       adult, it is expressed at highest levels in the heart, and at
CC       lower levels in the brain, skeletal muscle and aorta.
CC   -!- SIMILARITY: Contains 2 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; AF469648; AAM89218.1; -; mRNA.
DR   EMBL; AF470625; AAM89219.1; -; Genomic_DNA.
DR   EMBL; AF450245; AAM97586.1; -; Genomic_DNA.
DR   EMBL; AK002484; BAB22136.1; -; mRNA.
DR   EMBL; BC002093; AAH02093.1; -; mRNA.
DR   EMBL; BC002096; AAH02096.1; -; mRNA.
DR   IPI; IPI00121319; -.
DR   RefSeq; NP_077185.1; NM_024223.2.
DR   UniGene; Mm.133825; -.
DR   ProteinModelPortal; Q9DCT8; -.
DR   SMR; Q9DCT8; 1-63, 126-184.
DR   STRING; Q9DCT8; -.
DR   PhosphoSite; Q9DCT8; -.
DR   PRIDE; Q9DCT8; -.
DR   Ensembl; ENSMUST00000084882; ENSMUSP00000081943; ENSMUSG00000006356.
DR   GeneID; 68337; -.
DR   KEGG; mmu:68337; -.
DR   UCSC; uc007pfy.1; mouse.
DR   CTD; 68337; -.
DR   MGI; MGI:1915587; Crip2.
DR   GeneTree; ENSGT00550000074548; -.
DR   HOGENOM; HBG403138; -.
DR   HOVERGEN; HBG051143; -.
DR   InParanoid; Q9DCT8; -.
DR   OMA; FCHKPCY; -.
DR   OrthoDB; EOG4MKNH5; -.
DR   NextBio; 327013; -.
DR   ArrayExpress; Q9DCT8; -.
DR   Bgee; Q9DCT8; -.
DR   CleanEx; MM_CRIP2; -.
DR   Genevestigator; Q9DCT8; -.
DR   GermOnline; ENSMUSG00000006356; Mus musculus.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030097; P:hemopoiesis; IDA:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IDA: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; LIM domain; Metal-binding; Phosphoprotein; Repeat; Zinc.
FT   CHAIN         1    208       Cysteine-rich protein 2.
FT                                /FTId=PRO_0000075711.
FT   DOMAIN        5     57       LIM zinc-binding 1.
FT   DOMAIN      126    178       LIM zinc-binding 2.
FT   COMPBIAS     63     73       Gly-rich.
FT   COMPBIAS    180    194       Gly-rich.
FT   MOD_RES      77     77       Phosphotyrosine (By similarity).
FT   MOD_RES     138    138       N6-acetyllysine (By similarity).
SQ   SEQUENCE   208 AA;  22727 MW;  9A3AEF8A8FBA1D19 CRC64;
     MASKCPKCDK TVYFAEKVSS LGKDWHKFCL KCERCNKTLT PGGHAEHDGK PFCHKPCYAT
     LFGPKGVNIG GAGSYIYEKP QTEAPQVTGP IEVPVVRTEE RKTSGPPKGP SKASSVTTFT
     GEPNMCPRCN KRVYFAEKVT SLGKDWHRPC LRCERCSKTL TPGGHAEHDG QPYCHKPCYG
     ILFGPKGVNT GAVGSYIYDK DPEGTVQP
//
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   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   SORC2_MOUSE             Reviewed;        1159 AA.
AC   Q9EPR5; B2RSI4;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=VPS10 domain-containing receptor SorCS2;
DE   Flags: Precursor;
GN   Name=Sorcs2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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=11165493; DOI=10.1016/S0925-4773(00)00523-2;
RA   Rezgaoui M., Hermey G., Riedel I.B., Hampe W., Schaller H.C.,
RA   Hermans-Borgmeyer I.;
RT   "Identification of SorCS2, a novel member of the VPS10 domain
RT   containing receptor family, prominently expressed in the developing
RT   mouse brain.";
RL   Mech. Dev. 100:335-338(2001).
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   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-830, 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   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Detected in brain, lung, testis and heart.
CC   -!- DEVELOPMENTAL STAGE: Expression is highest in developing brain.
CC       Transiently expressed in all 3 germ layers.
CC   -!- SIMILARITY: Belongs to the SORCS family. SORCS2 subfamily.
CC   -!- SIMILARITY: Contains 6 BNR repeats.
CC   -!- SIMILARITY: Contains 1 PKD domain.
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DR   EMBL; AY004316; AAF88135.1; -; mRNA.
DR   EMBL; BC138875; AAI38876.1; -; mRNA.
DR   IPI; IPI00110262; -.
DR   RefSeq; NP_112151.2; NM_030889.2.
DR   UniGene; Mm.34113; -.
DR   ProteinModelPortal; Q9EPR5; -.
DR   SMR; Q9EPR5; 179-286, 542-603, 764-872.
DR   STRING; Q9EPR5; -.
DR   PRIDE; Q9EPR5; -.
DR   Ensembl; ENSMUST00000037370; ENSMUSP00000041828; ENSMUSG00000029093.
DR   GeneID; 81840; -.
DR   KEGG; mmu:81840; -.
DR   UCSC; uc008xek.1; mouse.
DR   CTD; 81840; -.
DR   MGI; MGI:1932289; Sorcs2.
DR   GeneTree; ENSGT00510000046443; -.
DR   HOVERGEN; HBG059252; -.
DR   InParanoid; Q9EPR5; -.
DR   OrthoDB; EOG4JWVCS; -.
DR   ArrayExpress; Q9EPR5; -.
DR   Bgee; Q9EPR5; -.
DR   Genevestigator; Q9EPR5; -.
DR   GermOnline; ENSMUSG00000029093; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
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; SM00089; PKD; 1.
DR   SMART; SM00602; VPS10; 1.
DR   SUPFAM; SSF49299; PKD; 1.
DR   PROSITE; PS50093; PKD; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     49       Potential.
FT   CHAIN        50   1159       VPS10 domain-containing receptor SorCS2.
FT                                /FTId=PRO_0000033173.
FT   TOPO_DOM     50   1078       Lumenal (Potential).
FT   TRANSMEM   1079   1099       Helical; (Potential).
FT   TOPO_DOM   1100   1159       Cytoplasmic (Potential).
FT   REPEAT      182    193       BNR 1.
FT   REPEAT      232    243       BNR 2.
FT   REPEAT      273    284       BNR 3.
FT   REPEAT      468    479       BNR 4.
FT   REPEAT      545    556       BNR 5.
FT   REPEAT      587    598       BNR 6.
FT   DOMAIN      786    876       PKD.
FT   COMPBIAS    715    720       Poly-Ser.
FT   CARBOHYD    158    158       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    328    328       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    362    362       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    600    600       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    830    830       N-linked (GlcNAc...).
FT   CARBOHYD    891    891       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    902    902       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1159 AA;  128872 MW;  9B9F501F2A525D2A CRC64;
     MAHRGPPSAP KRPGPTAPDR SFQALLPPCW PRSWPLLLLL LVLVAACGAM GRSPQPGRQG
     PGVQITRLLP AGRTESGDRK DPQARESEPS VPGLGPGSAS GPSTDGAPAP GKGRRARAVP
     VAGAASASRA QVSLISTSFV LKGDATHNQA MVHWTGENSS VILILTKYYH ADMGKVLESS
     LWRSSDFGTT YTKLTLQPGV TTVIDNFYIC PANKRKIILV SSSLGDREQS LFLSTDEGAT
     FQKYPVPFLV ETLLFHPKEE DKVLAYTKDS KLYVSSDLGK KWTLLQERVT KDHVFWAVSG
     VDDDPNLVHV EAQDLSGGYR YYTCLIYNCS AQPHIAPFSG PIDRGSLTVQ DEYIFLKATS
     TNRTKYYVSY RRSDFVLMKL PKYALPKDLQ IISTDEQQVF VAVQEWNQVD TYNLYQSDLR
     GVRYSLVLEN VRSSRQAEEN VVIDILEVRG VKGVFLANQK VDGKVTTVIT YNKGRDWDYL
     RPPSTDMNGK PTNCQPPDCY LHLHLRWADN PYVSGTVHTK DTAPGLIMGA GNLGSQLVEY
     KEEMYITSDC GHTWRQVFEE EHHVLYLDHG GVIAAIKDTS IPLKILKFSV DEGHTWSTHN
     FTSTSVFVDG LLSEPGDETL VMTVFGHISF RSDWELVKVD FRPSFPRQCG EDDYSSWDLT
     DLQGDHCIMG QQRSYRKRKS TSWCVKGRSF TSALTSRVCK CRDSDFLCDY GFERSSSSES
     TANKCSANFW FNPLSPPEDC VLGQTYTSSL GYRKVVSNVC EGGVDLQQSP VQLQCPLQAP
     RGLQVSIRGE AVAVRPREDV LFVVRQEQGD VLTTKYQVDL GDGFKAMYVN LTLTGEPIRH
     HYESPGIYRV SVRAENMAGH DEAVLFVQVN SPLQALYLEV VPVIGVNQEV NLTAVLLPLN
     PNLTVFYWWI GHSLQPLLSL DNSVTTKFTD AGDVRVTVQA ACGNSVLQDS RLVRVLDQFQ
     VVPLRFSREL DTFNPNTPEW REDVGLVVTR LLSKETSIPE ELLVTVVKPG LPTIADLYVL
     LPLPRPTRKR SLTSDKRLAA VQQALNSHRI SFILRGGLRI LVELRDTDTG PQRPGGSGGY
     WAVVVLFVIG LFAVGAFILY KFKRKRPGRT VYAQMHNEKE QEMTSPVSHS EDAQSTMQGN
     HSGVVLSINS REMHSYLVG
//
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.
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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   ENPP5_MOUSE             Reviewed;         477 AA.
AC   Q9EQG7; A9C479; Q921P7;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 3.
DT   08-FEB-2011, entry version 68.
DE   RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 5;
DE            Short=E-NPP 5;
DE            Short=NPP-5;
DE            EC=3.1.-.-;
DE   Flags: Precursor;
GN   Name=Enpp5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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=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   [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=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and 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=12927778; DOI=10.1016/S0006-291X(03)01454-2;
RA   Ohe Y., Ohnishi H., Okazawa H., Tomizawa K., Kobayashi H., Okawa K.,
RA   Matozaki T.;
RT   "Characterization of nucleotide pyrophosphatase-5 as an
RT   oligomannosidic glycoprotein in rat brain.";
RL   Biochem. Biophys. Res. Commun. 308:719-725(2003).
CC   -!- FUNCTION: May play a role in neuronal cell communication. Lacks
CC       nucleotide pyrophosphatase and lysopholipase D activity (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted (Potential). Membrane; Single-pass
CC       membrane protein (Potential).
CC   -!- TISSUE SPECIFICITY: Expressed abundantly in the brain and kidney,
CC       and at lower levels in the liver.
CC   -!- PTM: N-glycosylated (By similarity).
CC   -!- SIMILARITY: Belongs to the nucleotide
CC       pyrophosphatase/phosphodiesterase family.
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DR   EMBL; AF233377; AAG49143.1; -; mRNA.
DR   EMBL; CT030230; CAP19172.1; -; Genomic_DNA.
DR   EMBL; BC138977; AAI38978.1; -; mRNA.
DR   EMBL; BC138978; AAI38979.1; -; mRNA.
DR   IPI; IPI00111163; -.
DR   PIR; A59390; A59390.
DR   RefSeq; NP_001162091.1; NM_001168620.1.
DR   RefSeq; NP_114392.1; NM_032003.2.
DR   UniGene; Mm.30145; -.
DR   UniGene; Mm.451536; -.
DR   ProteinModelPortal; Q9EQG7; -.
DR   SMR; Q9EQG7; 27-400.
DR   STRING; Q9EQG7; -.
DR   PRIDE; Q9EQG7; -.
DR   Ensembl; ENSMUST00000024756; ENSMUSP00000024756; ENSMUSG00000023960.
DR   GeneID; 83965; -.
DR   KEGG; mmu:83965; -.
DR   UCSC; uc008cpr.1; mouse.
DR   CTD; 83965; -.
DR   MGI; MGI:1933830; Enpp5.
DR   GeneTree; ENSGT00550000074244; -.
DR   HOVERGEN; HBG051485; -.
DR   InParanoid; Q9EQG7; -.
DR   OMA; YLDKDHY; -.
DR   PhylomeDB; Q9EQG7; -.
DR   BRENDA; 3.6.1.9; 244.
DR   NextBio; 350842; -.
DR   ArrayExpress; Q9EQG7; -.
DR   Bgee; Q9EQG7; -.
DR   Genevestigator; Q9EQG7; -.
DR   GermOnline; ENSMUSG00000023960; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
DR   InterPro; IPR017850; Alkaline_phosphatase_core.
DR   InterPro; IPR002591; Phosphodiest/P_Trfase.
DR   Gene3D; G3DSA:3.40.720.10; Alk_phosphtse; 2.
DR   Pfam; PF01663; Phosphodiest; 1.
DR   SUPFAM; SSF53649; Alkaline_phosphatase_core; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Hydrolase; Membrane; Secreted; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     24       By similarity.
FT   CHAIN        25    477       Ectonucleotide
FT                                pyrophosphatase/phosphodiesterase family
FT                                member 5.
FT                                /FTId=PRO_0000036402.
FT   TRANSMEM    432    452       Helical; (Potential).
FT   ACT_SITE     72     72       By similarity.
FT   CARBOHYD    101    101       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    158    158       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    292    292       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    329    329       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    362    362       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    369    369       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    382    382       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    389    389       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   477 AA;  54387 MW;  98845AF8B725FD61 CRC64;
     MIPEFLLASC TLATLCHSAP FSLQPEEQKV LVVSFDGFRW DYLYKVPTPH FHYIMKNGVH
     VNQVTNVFIT KTYPNHYTLV TGLFAENHGI VANDMFDPIL NKSFSLEHMD IYDSKFWEEA
     TPIWITNQRA GHASGAAMWP GADVKIHDSF PTYYLPYNES VSFEDRVAKI IEWFTAKDPI
     NLGFLYWEEP DDTGHDVGPD SPLMGSVISD VDHKLGYLIK MLKRAKLWNN VNLIVTSDHG
     MTQCSKQRVI ELDRYLDKEH YTLIDHSPVA AILPKEGKFD EVYDALAGAH PNLTVYKKEE
     IPERWHYKHN DRVQPIVAVA DEGWYILQNK SDDFLLGNHG YDNALAEMHP IFLAHGPAFR
     KNFTKEAMNS TDLYSLLCHL LNLTALPHNG SFWNVQDLLS SATPKPIPYT QSTTLLLGSD
     KPGEDEQEES YPYYIGVSLG SIIAMVFFVV LIKHLIRSQV HTLQYRQVEV AQPLLQA
//
ID   RIMS2_MOUSE             Reviewed;        1530 AA.
AC   Q9EQZ7; Q8C433; Q8CCK2;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Regulating synaptic membrane exocytosis protein 2;
DE   AltName: Full=Rab-3-interacting molecule 2;
DE            Short=RIM 2;
DE   AltName: Full=Rab-3-interacting protein 2;
GN   Name=Rims2; Synonyms=Rab3ip2, Rim2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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   INTERACTION WITH RAB3A AND EPAC2.
RC   TISSUE=Insulinoma;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; 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   [3]
RP   GENOMIC ORGANIZATION.
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   [4]
RP   INTERACTION WITH PCLO.
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375 AND SER-409, 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-1039 AND THR-1094, 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: Rab effector involved in exocytosis. May act as scaffold
CC       protein.
CC   -!- SUBUNIT: Binds RAB3A and RAB3B that have been activated by GTP-
CC       binding. Binds RIM binding proteins 1 and 2. Interacts with PPFIA3
CC       and PPFIA4. Interacts via its zinc finger with the first C2 domain
CC       of UNC13A. Forms a complex consisting of UNC13A, RIMS2 and RAB3A
CC       (By similarity). Heterodimer with PCLO. Part of a ternary complex
CC       involving PCLO and EPAC2.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, synaptosome.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=RIM2-alpha;
CC         IsoId=Q9EQZ7-1; Sequence=Displayed;
CC       Name=2; Synonyms=RIM2-gamma;
CC         IsoId=Q9EQZ7-2; Sequence=VSP_008181, VSP_008184;
CC         Note=No experimental confirmation available;
CC       Name=3; Synonyms=RIM2-beta;
CC         IsoId=Q9EQZ7-3; Sequence=VSP_008182, VSP_008183;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Detected in testis, pituitary and an
CC       insulinoma cell line. Detected at low levels in cerebellar cortex.
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.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB021131; BAB18975.1; -; mRNA.
DR   EMBL; AK032619; BAC27953.1; -; mRNA.
DR   EMBL; AK083172; BAC38794.1; -; mRNA.
DR   IPI; IPI00111749; -.
DR   IPI; IPI00228585; -.
DR   IPI; IPI00344273; -.
DR   RefSeq; NP_444501.1; NM_053271.1.
DR   UniGene; Mm.309296; -.
DR   ProteinModelPortal; Q9EQZ7; -.
DR   SMR; Q9EQZ7; 31-198, 650-763, 817-943, 1362-1509.
DR   STRING; Q9EQZ7; -.
DR   PhosphoSite; Q9EQZ7; -.
DR   PRIDE; Q9EQZ7; -.
DR   Ensembl; ENSMUST00000082054; ENSMUSP00000080711; ENSMUSG00000037386.
DR   Ensembl; ENSMUST00000090116; ENSMUSP00000087575; ENSMUSG00000037386.
DR   Ensembl; ENSMUST00000110311; ENSMUSP00000105940; ENSMUSG00000037386.
DR   GeneID; 116838; -.
DR   KEGG; mmu:116838; -.
DR   UCSC; uc007vod.1; mouse.
DR   UCSC; uc007voh.1; mouse.
DR   CTD; 116838; -.
DR   MGI; MGI:2152972; Rims2.
DR   GeneTree; ENSGT00550000074588; -.
DR   HOVERGEN; HBG058147; -.
DR   OrthoDB; EOG42BX7R; -.
DR   PhylomeDB; Q9EQZ7; -.
DR   NextBio; 369190; -.
DR   ArrayExpress; Q9EQZ7; -.
DR   Bgee; Q9EQZ7; -.
DR   CleanEx; MM_RIMS2; -.
DR   Genevestigator; Q9EQZ7; -.
DR   GermOnline; ENSMUSG00000037386; Mus musculus.
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:0017137; F:Rab GTPase binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0017156; P:calcium ion-dependent exocytosis; IDA:MGI.
DR   GO; GO:0019933; P:cAMP-mediated signaling; IDA:MGI.
DR   GO; GO:0030073; P:insulin secretion; IDA:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
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   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; Exocytosis; Metal-binding;
KW   Neurotransmitter transport; Phosphoprotein; Repeat; Synapse;
KW   Synaptosome; Transport; Zinc; Zinc-finger.
FT   CHAIN         1   1530       Regulating synaptic membrane exocytosis
FT                                protein 2.
FT                                /FTId=PRO_0000190202.
FT   DOMAIN       26    194       RabBD.
FT   DOMAIN      677    763       PDZ.
FT   DOMAIN      816    922       C2 1.
FT   DOMAIN     1376   1478       C2 2.
FT   ZN_FING     126    182       FYVE-type.
FT   COMPBIAS   1169   1202       Ser-rich.
FT   MOD_RES     375    375       Phosphoserine.
FT   MOD_RES     409    409       Phosphoserine.
FT   MOD_RES     436    436       Phosphoserine (By similarity).
FT   MOD_RES     438    438       Phosphoserine (By similarity).
FT   MOD_RES    1039   1039       Phosphoserine.
FT   MOD_RES    1094   1094       Phosphothreonine.
FT   MOD_RES    1172   1172       Phosphoserine (By similarity).
FT   MOD_RES    1175   1175       Phosphoserine (By similarity).
FT   MOD_RES    1178   1178       Phosphoserine (By similarity).
FT   MOD_RES    1181   1181       Phosphoserine (By similarity).
FT   MOD_RES    1186   1186       Phosphothreonine (By similarity).
FT   MOD_RES    1187   1187       Phosphoserine (By similarity).
FT   VAR_SEQ       1   1245       Missing (in isoform 2).
FT                                /FTId=VSP_008181.
FT   VAR_SEQ       1    232       Missing (in isoform 3).
FT                                /FTId=VSP_008182.
FT   VAR_SEQ     233    272       PGDLSVPAVEKGRAHGLTRQDTIKNGSGVKHQIASDMPSD
FT                                -> MQFETLRQVCNSVLSHFHGVFSSPPNILQNELFGQTLN
FT                                NA (in isoform 3).
FT                                /FTId=VSP_008183.
FT   VAR_SEQ    1246   1292       NDGSQSDTAVGALGTSGKKRRSSIGAKMVAIVGLSRKSRSA
FT                                SQLSQT -> MGRQGLGGTGAAGRSMQRSQSRSSLSASFEA
FT                                LAGYFPCMNSLEEDEG (in isoform 2).
FT                                /FTId=VSP_008184.
SQ   SEQUENCE   1530 AA;  172863 MW;  58CF11BF7152357D CRC64;
     MSAPLGPRGR PAPTPAASQP PPQPEMPDLS HLTEEERKII LAVMDRQKKE EEKEQSVLKI
     KEEHKAQPTQ WFPFSGITEL VNNVLQPQQK QPNEKEPQTK 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
     DRDRSHPRTG SVQTSPSSTP GTGRRGRQLP QLPPKGTLER SAMDIEERNR QMKLNKYKQV
     AGSDPRLEQD YHSKYRSGWD PHRGADTVST KSSDSDVSDV SAVSRTSSAS RFSSTSYMSV
     QSERPRGNRK ISVFTSKMQN RQMGVSGKNL TKSTSISGDM CSLEKNDGSQ SDTAVGALGT
     SGKKRRSSIG AKMVAIVGLS RKSRSASQLS QTEGGGKKLR STVQRSTETG LAVEMRNWMT
     RQASRESTDG SMNSYSSEGN LIFPGVRLAS DSQFSDFLDG LGPAQLVGRQ TLATPAMGDI
     QVGMMDKKGQ LEVEIIRARG LVVKPGSKTL PAPYVKVYLL DNGVCIAKKK TKVARKTLEP
     LYQQLLSFEE SPQGRVLQII VWGDYGRMDH KSFMGVAQIL LDELELSNMV IGWFKLFPPS
     SLVDPTLAPL TRRASQSSLE SSTGPSYSRS
//
ID   TICN2_MOUSE             Reviewed;         423 AA.
AC   Q9ER58;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-FEB-2011, entry version 85.
DE   RecName: Full=Testican-2;
DE   AltName: Full=SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycan 2;
DE   Flags: Precursor;
GN   Name=Spock2; Synonyms=Ticn2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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   Hartmann U., Paulsson M., Maurer P.;
RT   "Cloning of mouse testican-2.";
RL   Submitted (SEP-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   -!- FUNCTION: May participate in diverse steps of neurogenesis. Binds
CC       calcium (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix (Probable).
CC   -!- TISSUE SPECIFICITY: Brain specific.
CC   -!- PTM: O-glycosylated; contains chondroitin sulfate and heparan
CC       sulfate (By similarity).
CC   -!- SIMILARITY: Contains 1 Kazal-like domain.
CC   -!- SIMILARITY: Contains 1 thyroglobulin type-1 domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ278999; CAC08507.1; -; mRNA.
DR   EMBL; BC057324; AAH57324.1; -; mRNA.
DR   IPI; IPI00111600; -.
DR   RefSeq; NP_443720.1; NM_052994.2.
DR   UniGene; Mm.153429; -.
DR   ProteinModelPortal; Q9ER58; -.
DR   SMR; Q9ER58; 82-377.
DR   STRING; Q9ER58; -.
DR   MEROPS; I31.954; -.
DR   PRIDE; Q9ER58; -.
DR   Ensembl; ENSMUST00000072315; ENSMUSP00000072157; ENSMUSG00000058297.
DR   GeneID; 94214; -.
DR   KEGG; mmu:94214; -.
DR   UCSC; uc007fel.1; mouse.
DR   CTD; 94214; -.
DR   MGI; MGI:1891351; Spock2.
DR   GeneTree; ENSGT00510000046429; -.
DR   HOVERGEN; HBG026595; -.
DR   OMA; ICKPCHM; -.
DR   NextBio; 352179; -.
DR   ArrayExpress; Q9ER58; -.
DR   Bgee; Q9ER58; -.
DR   Genevestigator; Q9ER58; -.
DR   GermOnline; ENSMUSG00000058297; Mus musculus.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0050840; F:extracellular matrix binding; IDA:MGI.
DR   GO; GO:0005539; F:glycosaminoglycan binding; IDA:MGI.
DR   GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR   GO; GO:0019800; P:peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan; IDA:MGI.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR002350; Prot_inh_Kazal.
DR   InterPro; IPR011497; Prot_Inh_Kazal_2.
DR   InterPro; IPR019577; SPARC/Testican_Ca-bd-dom.
DR   InterPro; IPR000716; Thyroglobulin_1.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Gene3D; G3DSA:4.10.800.10; Thyroglobulin_1; 1.
DR   Pfam; PF07648; Kazal_2; 1.
DR   Pfam; PF10591; SPARC_Ca_bdg; 1.
DR   Pfam; PF00086; Thyroglobulin_1; 1.
DR   SMART; SM00280; KAZAL; 1.
DR   SMART; SM00211; TY; 1.
DR   SUPFAM; SSF57610; Thyroglobulin_1; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
DR   PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR   PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Heparan sulfate; Phosphoprotein; Proteoglycan; Secreted; Signal.
FT   SIGNAL        1     22       Potential.
FT   CHAIN        23    423       Testican-2.
FT                                /FTId=PRO_0000026702.
FT   DOMAIN      130    182       Kazal-like.
FT   DOMAIN      309    375       Thyroglobulin type-1.
FT   COMPBIAS    392    415       Glu-rich.
FT   MOD_RES      86     86       Phosphothreonine (By similarity).
FT   CARBOHYD    225    225       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    382    382       O-linked (Xyl...) (glycosaminoglycan)
FT                                (Potential).
FT   CARBOHYD    387    387       O-linked (Xyl...) (glycosaminoglycan)
FT                                (Potential).
FT   DISULFID     90    101       By similarity.
FT   DISULFID     95    111       By similarity.
FT   DISULFID    136    166       By similarity.
FT   DISULFID    139    159       By similarity.
FT   DISULFID    148    180       By similarity.
FT   DISULFID    312    336       By similarity.
FT   DISULFID    347    354       By similarity.
FT   DISULFID    356    375       By similarity.
SQ   SEQUENCE   423 AA;  46863 MW;  20D73E3DB3BC1A15 CRC64;
     MRAPGSGRLA LPLLLLAVVA LAEGDAKGLK EGETPGNFME DEQWLSSISQ YSGKIKHWNR
     FRDEVEDDYI KSWEDNQQGD EALDTTKDPC QKVKCSRHKV CVAQGYQRAM CISRKKLEHR
     IKQPSLKLHG GKDSVCKPCH MAQLASVCGS DGHTYSSVCK LEQQACLSSK QLAVRCEGPC
     PCPTEQSTAS TTDSKSETCT GQDLADLGDR LRDWFQLLRE NSKQNGSANS ATNPAGLDKS
     LGASCKDSIG WMFSKLDTSG DLFLDQTELA AINLDKYEVC IRPFFNSCDT YKDGRVSTAE
     WCFCFWREKP PCLAELERTQ IQEAAKKKPG VFIPSCDEDG YYRKMQCDQS RGDCWCVDQL
     GLELTGTRMH GTPDCDDIVG FSGDFGSGVG WEDEEEKETE EAGEEAEEEE GEAGEADDGG
     YIW
//
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   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   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   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;
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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   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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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   ELF2_MOUSE              Reviewed;         593 AA.
AC   Q9JHC9; Q6NST2; Q8BTX8; Q9JHC7; Q9JHC8; Q9JHD0;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=ETS-related transcription factor Elf-2;
DE   AltName: Full=E74-like factor 2;
DE   AltName: Full=New ETS-related factor;
GN   Name=Elf2; Synonyms=Nerf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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 LMO2.
RC   TISSUE=T-cell;
RX   MEDLINE=97154704; PubMed=9001422; DOI=10.1038/sj.leu.2400516;
RA   Wilkinson D.A., Neale G.A.M., Mao S., Naeve C.W., Goorha R.M.;
RT   "Elf-2, a rhombotin-2 binding ets transcription factor: discovery and
RT   potential role in T cell leukemia.";
RL   Leukemia 11:86-96(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
RA   Wilkinson D.A., Neale G.A.M., Mao S., Fernandes E.R., Davenport J.W.,
RA   Naeve C.W., Goorha R.M.;
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-175 (ISOFORM 1).
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).
CC   -!- FUNCTION: Probably transcriptionally activates the LYN and BLK
CC       promoters and acts synergistically with RUNX1 to transactivate the
CC       BLK promoter (By similarity).
CC   -!- SUBUNIT: Interacts with LIM domains of LMO2. Interacts via its N-
CC       terminal region with RUNX1.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=4;
CC         IsoId=Q9JHC9-1; Sequence=Displayed;
CC       Name=1; Synonyms=elf-2a;
CC         IsoId=Q9JHC9-2; Sequence=VSP_014160;
CC       Name=2; Synonyms=elf-2b;
CC         IsoId=Q9JHC9-3; Sequence=VSP_014159, VSP_014160;
CC       Name=3;
CC         IsoId=Q9JHC9-4; Sequence=VSP_014159;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined. Highest
CC       levels in thymocytes and bone marrow.
CC   -!- SIMILARITY: Belongs to the ETS family.
CC   -!- SIMILARITY: Contains 1 ETS DNA-binding domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF256216; AAF67191.1; -; mRNA.
DR   EMBL; AF256217; AAF67192.1; -; mRNA.
DR   EMBL; AF256218; AAF67193.1; -; mRNA.
DR   EMBL; AF256219; AAF67194.1; -; mRNA.
DR   EMBL; AK088422; BAC40346.1; -; mRNA.
DR   EMBL; BC069901; AAH69901.1; -; mRNA.
DR   IPI; IPI00119253; -.
DR   IPI; IPI00607912; -.
DR   IPI; IPI00607942; -.
DR   IPI; IPI00608103; -.
DR   RefSeq; NP_075991.1; NM_023502.1.
DR   UniGene; Mm.131038; -.
DR   ProteinModelPortal; Q9JHC9; -.
DR   SMR; Q9JHC9; 207-291.
DR   STRING; Q9JHC9; -.
DR   PhosphoSite; Q9JHC9; -.
DR   PRIDE; Q9JHC9; -.
DR   Ensembl; ENSMUST00000091144; ENSMUSP00000088678; ENSMUSG00000037174.
DR   Ensembl; ENSMUST00000108053; ENSMUSP00000103688; ENSMUSG00000037174.
DR   GeneID; 69257; -.
DR   KEGG; mmu:69257; -.
DR   UCSC; uc008pdo.1; mouse.
DR   UCSC; uc008pdp.1; mouse.
DR   UCSC; uc008pdr.1; mouse.
DR   UCSC; uc008pds.1; mouse.
DR   CTD; 69257; -.
DR   MGI; MGI:1916507; Elf2.
DR   GeneTree; ENSGT00600000084143; -.
DR   HOGENOM; HBG714786; -.
DR   HOVERGEN; HBG007183; -.
DR   InParanoid; Q9JHC9; -.
DR   OMA; CNEDLAA; -.
DR   OrthoDB; EOG4HX50W; -.
DR   PhylomeDB; Q9JHC9; -.
DR   NextBio; 328977; -.
DR   ArrayExpress; Q9JHC9; -.
DR   Bgee; Q9JHC9; -.
DR   CleanEx; MM_ELF2; -.
DR   Genevestigator; Q9JHC9; -.
DR   GermOnline; ENSMUSG00000037174; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0016563; F:transcription activator activity; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR   InterPro; IPR000418; Ets.
DR   InterPro; IPR022084; TF_Elf-1_N.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF12310; Elf-1_N; 1.
DR   Pfam; PF00178; Ets; 1.
DR   PRINTS; PR00454; ETSDOMAIN.
DR   SMART; SM00413; ETS; 1.
DR   PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR   PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR   PROSITE; PS50061; ETS_DOMAIN_3; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    593       ETS-related transcription factor Elf-2.
FT                                /FTId=PRO_0000204088.
FT   DNA_BIND    208    290       ETS.
FT   MOD_RES     182    182       Phosphothreonine (By similarity).
FT   MOD_RES     185    185       Phosphoserine (By similarity).
FT   MOD_RES     191    191       Phosphoserine (By similarity).
FT   MOD_RES     363    363       Phosphoserine (By similarity).
FT   MOD_RES     372    372       Phosphoserine (By similarity).
FT   MOD_RES     432    432       Phosphoserine (By similarity).
FT   MOD_RES     523    523       Phosphothreonine (By similarity).
FT   VAR_SEQ       1     79       MASAVVDSGGSALELPSDGGENQEGGDTGPDCPAVIVEPVP
FT                                SARLEQGYAAQVLVYDDETYMMQDVAEEQEVETENSET ->
FT                                MATSLHEGPTNQLDLLIRA (in isoform 2 and
FT                                isoform 3).
FT                                /FTId=VSP_014159.
FT   VAR_SEQ     118    129       Missing (in isoform 1 and isoform 2).
FT                                /FTId=VSP_014160.
FT   CONFLICT    159    159       S -> W (in Ref. 3; BAC40346).
FT   CONFLICT    171    171       M -> K (in Ref. 4; AAH69901).
SQ   SEQUENCE   593 AA;  63203 MW;  A6E67486141AB903 CRC64;
     MASAVVDSGG SALELPSDGG ENQEGGDTGP DCPAVIVEPV PSARLEQGYA AQVLVYDDET
     YMMQDVAEEQ EVETENSETV EASVHSSNAH CTDKTIEAAE ALLHMESPTC LRDSRSPVEV
     FVPPCISTPE FIHAAMRPDV ITETVVEVST EESEPMDASP IPTSPDSHEP MKKKKVGRKP
     KTQQSPVSNG SPELGIKKKA REGKGNTTYL WEFLLDLLQD KNTCPRYIKW TQREKGIFKL
     VDSKAVSKLW GKHKNKPDMN YETMGRALRY YYQRGILAKV EGQRLVYQFK DMPKNIVVID
     DDKSETCPED LAAAADDKSL ERVSLSAESL LKAATAVRGG KNSSPLNCSR AEKGVARVVN
     ITSPTHDGSS RSPTTTAPVS AAAAPRTVRV AMQVPVVMTS LGQKISAVAV QSVNAGTGSP
     LITSTSPASA SSPKVVIQTV PTVMPASTEN GDRITMQPAK IITIPATQLA QCQLQAKSNL
     TGSGSINIVG TPLAVRALTP VSIAHGTPVM RLSVPAQQAS GQTPPRVISA LLKGPEGKSE
     AKKQEHDVKT LQLVEEKGAD GNKTVTHVVV VSAPSAIALP VTMKTEGLVT CEK
//
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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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   TULP4_MOUSE             Reviewed;        1547 AA.
AC   Q9JIL5; B2RQP8; Q8CA75; Q922C2;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Tubby-related protein 4;
DE   AltName: Full=Tubby superfamily protein;
DE   AltName: Full=Tubby-like protein 4;
GN   Name=Tulp4; Synonyms=Tusp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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=Spleen;
RX   MEDLINE=21479402; PubMed=11595174; DOI=10.1016/S0378-1119(01)00582-0;
RA   Li Q.-Z., Wang C.-Y., Shi J.-D., Ruan Q.-G., Eckenrode S.,
RA   Davoodi-Semiromi A., Kukar T., Gu Y., Lian W., Wu D., She J.-X.;
RT   "Molecular cloning and characterization of the mouse and human TUSP
RT   gene, a novel member of the tubby superfamily.";
RL   Gene 273:275-284(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   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 1122-1547.
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: May be a substrate-recognition component of a SCF-like
CC       ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex
CC       which mediates the ubiquitination and subsequent proteasomal
CC       degradation of target proteins (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: The SOCS box domain mediates the interaction with the
CC       Elongin BC complex, an adapter module in different E3 ubiquitin
CC       ligase complexes (By similarity).
CC   -!- SIMILARITY: Belongs to the TUB family.
CC   -!- SIMILARITY: Contains 1 SOCS box domain.
CC   -!- SIMILARITY: Contains 3 WD repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF219945; AAF87974.1; -; mRNA.
DR   EMBL; AK039439; BAC30348.1; -; mRNA.
DR   EMBL; BC008557; AAH08557.1; -; mRNA.
DR   EMBL; BC138024; AAI38025.1; -; mRNA.
DR   EMBL; BC138025; AAI38026.1; -; mRNA.
DR   IPI; IPI00120734; -.
DR   RefSeq; NP_473381.1; NM_054040.3.
DR   UniGene; Mm.28251; -.
DR   UniGene; Mm.449307; -.
DR   ProteinModelPortal; Q9JIL5; -.
DR   SMR; Q9JIL5; 42-218, 1467-1542.
DR   PRIDE; Q9JIL5; -.
DR   Ensembl; ENSMUST00000039655; ENSMUSP00000049248; ENSMUSG00000034377.
DR   GeneID; 68842; -.
DR   KEGG; mmu:68842; -.
DR   UCSC; uc008agh.2; mouse.
DR   CTD; 68842; -.
DR   MGI; MGI:1916092; Tulp4.
DR   GeneTree; ENSGT00600000084110; -.
DR   HOGENOM; HBG444710; -.
DR   HOVERGEN; HBG057880; -.
DR   InParanoid; Q9JIL5; -.
DR   OMA; LANQNVQ; -.
DR   OrthoDB; EOG4C2H8N; -.
DR   PhylomeDB; Q9JIL5; -.
DR   NextBio; 328035; -.
DR   ArrayExpress; Q9JIL5; -.
DR   Bgee; Q9JIL5; -.
DR   CleanEx; MM_TULP4; -.
DR   Genevestigator; Q9JIL5; -.
DR   GermOnline; ENSMUSG00000034377; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR001496; SOCS_C.
DR   InterPro; IPR000007; Tubby_C.
DR   InterPro; IPR008983; Tumour_necrosis_fac-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:3.20.90.10; Tubby_C; 2.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   Pfam; PF07525; SOCS_box; 1.
DR   Pfam; PF01167; Tub; 1.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00969; SOCS_box; 1.
DR   SMART; SM00320; WD40; 2.
DR   SUPFAM; SSF49842; TNF_like; 1.
DR   SUPFAM; SSF54518; Tubby_C; 2.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS50225; SOCS; 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   Cytoplasm; Repeat; Ubl conjugation pathway; WD repeat.
FT   CHAIN         1   1547       Tubby-related protein 4.
FT                                /FTId=PRO_0000186473.
FT   REPEAT       80    119       WD 1.
FT   REPEAT      123    162       WD 2.
FT   REPEAT      165    204       WD 3.
FT   DOMAIN      364    414       SOCS box.
FT   REGION     1436   1547       TUB.
FT   CONFLICT   1420   1420       G -> R (in Ref. 3; BAC30348).
SQ   SEQUENCE   1547 AA;  169638 MW;  8B7CA7A250884423 CRC64;
     MYAAVEHGPV LCSDSNILCL SWKGRVPKSE KEKPVCRRRY YEEGWLATGN GRGVVGVTFT
     SSHCRRDRST PQRINFNLRG HNSEVVLVRW NEPYQKLATC DADGGIFVWI QYEGRWSVEL
     VNDRGAQVSD FTWSHDGTQA LISYRDGFVL VGSVSGQRHW SSEINLESQI TCGIWTPDDQ
     QVLFGTADGQ VIVMDCHGRM LAHVLLHESD GILSMSWNYP IFLVEDSSES DTDSDDYSPP
     QDGPAAYPIP VQNTKPLLTV SFTSGDISLM NNYDDLSPTV IRSGLKEVVA QWCTQGDLLA
     VAGMEQQAQL SELPNGPLLK SAMVKFYNVR GEHIFTLDTL VQRPIISICW GHRDSRLLMA
     SGPALYVVRV EHRVSSLQLL CQQAIASTLR EDKDVNKLTL PPRLCSYLST AFIPTIKPPI
     PDPNNMRDFV SYPSAGNERL HCTMKRTEDD PEVGGPCYTL YLEYLGGLVP ILKGRRISKL
     RPEFVIMDPR TDSKSDEIYG NSLISTVIDS CNCSDSSDIE LSDDWAAKKS PKISRSSKSP
     KLPRISIEAR KSPKLPRAAQ EISRSPRLPM RKPSMGSPSL TRREFPFEDI TQHNYLAQVT
     SNIWGTKFKI VGLAAFLPTN LGAVIYKTSL LHLQPRQMTI YLPEVRKISM DYINLPVFNP
     NVFSEDEDDL PVTGASGVPE NNPPCTVNIP IAPIHSSAQA LSPTQSIGLV QSLLANQNVQ
     LDVLTNQTTA VGSAEHAGDA ATQYPVSSRY SNPGQVIFGG VEMGRIIQNP PQLPLPPPPP
     PPPQAPMQLS AVDHGDRDHE HLQKSAKALR PVPQLAAEGD AVVFSAPQEV QVAKMNPPPP
     YPGTIPAAPT TAAPPPPLPP PQPPVDVCLK KGDFSLYPTA AHYQPPLGYE RITTFDSSGN
     VEEVCRPRTR MLCSQNTYTL PGPGSSATLR LTATEKKVPQ PCTSATLNRL TVPRYSIPTG
     DPPPYPEIAS QLAQGRSAAQ RLDNSLIHAT LRRNNREVAL KMAQLADSSR APLQPLAKPK
     GGAAGAVAQL PARPPPALYT CSQCSGAGPS SQSGAALAHA ISTSPLASQS SYNLLSPPDT
     SRDRTDYVNS AFTEDEALSQ HCQLEKPLRH PPLPEAAVTM KRPPPYQWDP MLGEDVWVPQ
     ERTAQPTVPN PLKLSPLMLG QGQHLDVARV PFVPPKSPSS PTATFPTGYG MGMPYPGSYN
     NPSLPGVQAP CSPKDALSQA QFAQQESAVV LQPAYPPSLS YCTLPPTYPG SSTCSSVQLP
     PIALHPWNSY STCPPMQNTQ GTLPPKPHLV VEKPLVSPPP AELQSHMGTE VMVETADNFQ
     EVLSLTESPV PQRTEKFGKK NRKRLDSRAE EGSVQAITEG KVKKDARTLS DFNSLISSPR
     LGREKKKVKS QKDQLKSKKL NKTNEFQDSS ESEPELFISG DELMNQSQGS KKGWKSKRSL
     RTASELEEFK CRKASEKEDG RLGSQGFVYV MANKQPLWNE ATQVYQLDFG GRVTQESAKN
     FQIELEGRQV MQFGRIDGNA YILDFQYPFS AVQAFAVALA NVTQRLK
//
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;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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.
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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   ADRM1_MOUSE             Reviewed;         407 AA.
AC   Q9JKV1; Q3UKZ8; Q8BPH8; Q922A7;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Proteasomal ubiquitin receptor ADRM1;
DE   AltName: Full=110 kDa cell membrane glycoprotein;
DE            Short=Gp110;
DE   AltName: Full=Adhesion-regulating molecule 1;
DE            Short=ARM-1;
DE   AltName: Full=Rpn13 homolog;
GN   Name=Adrm1; Synonyms=Gp110;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=20374361; PubMed=10919708; DOI=10.1023/A:1006790912877;
RA   Simins A.B., Weighardt H., Weidner K.M., Weidle U.H., Holzmann B.;
RT   "Functional cloning of ARM-1, an adhesion-regulating molecule
RT   upregulated in metastatic tumor cells.";
RL   Clin. Exp. Metastasis 17:641-648(1999).
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting 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; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and 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, AND LACK OF GLYCOSYLATION.
RX   PubMed=15819879; DOI=10.1111/j.1742-4658.2005.04613.x;
RA   Lamerant N., Kieda C.;
RT   "Adhesion properties of adhesion-regulating molecule 1 protein on
RT   endothelial cells.";
RL   FEBS J. 272:1833-1844(2005).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=17139257; DOI=10.1038/sj.emboj.7601450;
RA   Qiu X.-B., Ouyang S.-Y., Li C.-J., Miao S., Wang L., Goldberg A.L.;
RT   "hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the
RT   deubiquitinating enzyme, UCH37.";
RL   EMBO J. 25:5742-5753(2006).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=16815440; DOI=10.1016/j.jmb.2006.06.011;
RA   Joergensen J.P., Lauridsen A.-M., Kristensen P., Dissing K.,
RA   Johnsen A.H., Hendil K.B., Hartmann-Petersen R.;
RT   "Adrm1, a putative cell adhesion regulating protein, is a novel
RT   proteasome-associated factor.";
RL   J. Mol. Biol. 360:1043-1052(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., 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   STRUCTURE BY NMR OF 22-130, X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF
RP   1-150, FUNCTION, PH DOMAIN, AND INTERACTION WITH UBIQUITIN; UCHL5 AND
RP   PSMD1.
RX   PubMed=18497827; DOI=10.1038/nature06924;
RA   Schreiner P., Chen X., Husnjak K., Randles L., Zhang N., Elsasser S.,
RA   Finley D., Dikic I., Walters K.J., Groll M.;
RT   "Ubiquitin docking at the proteasome through a novel pleckstrin-
RT   homology domain interaction.";
RL   Nature 453:548-552(2008).
CC   -!- FUNCTION: Functions as a proteasomal ubiquitin receptor. Recruits
CC       the deubiquitinating enzyme UCHL5 at the 26S proteasome and
CC       promotes its activity.
CC   -!- SUBUNIT: Interacts with PSMD1, ubiquitin and UCHL5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (By similarity).
CC   -!- TISSUE SPECIFICITY: Present in all tissues examined (at protein
CC       level).
CC   -!- DOMAIN: The PH domain mediates interactions with PSMD1 and
CC       ubiquitin. Preferential binding to the proximal subunit of K48-
CC       linked diubiquitin allows UCHL5 access to the distal subunit.
CC   -!- PTM: Not N-glycosylated.
CC   -!- PTM: Not O-glycosylated (Probable).
CC   -!- SIMILARITY: Belongs to the ADRM1 family.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- CAUTION: Although initially described as a cell membrane
CC       glycoprotein, ADRM1 is intracellular and non-glycosylated, and has
CC       probably no direct role in cell adhesion.
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DR   EMBL; AF225959; AAF33401.1; -; mRNA.
DR   EMBL; AK075674; BAC35889.1; -; mRNA.
DR   EMBL; AK145474; BAE26457.1; -; mRNA.
DR   EMBL; AK145792; BAE26653.1; -; mRNA.
DR   EMBL; AK166878; BAE39089.1; -; mRNA.
DR   EMBL; AL663027; CAM16214.1; -; Genomic_DNA.
DR   EMBL; BC008974; AAH08974.1; -; mRNA.
DR   EMBL; BC031517; AAH31517.1; -; mRNA.
DR   IPI; IPI00331155; -.
DR   RefSeq; NP_062796.2; NM_019822.3.
DR   UniGene; Mm.379082; -.
DR   PDB; 2R2Y; X-ray; 1.70 A; A=2-150.
DR   PDB; 2Z59; NMR; -; A=22-130.
DR   PDBsum; 2R2Y; -.
DR   PDBsum; 2Z59; -.
DR   ProteinModelPortal; Q9JKV1; -.
DR   SMR; Q9JKV1; 22-130.
DR   STRING; Q9JKV1; -.
DR   PhosphoSite; Q9JKV1; -.
DR   PRIDE; Q9JKV1; -.
DR   Ensembl; ENSMUST00000061437; ENSMUSP00000050076; ENSMUSG00000039041.
DR   GeneID; 56436; -.
DR   KEGG; mmu:56436; -.
DR   CTD; 56436; -.
DR   MGI; MGI:1929289; Adrm1.
DR   eggNOG; roNOG06499; -.
DR   GeneTree; ENSGT00390000013839; -.
DR   HOGENOM; HBG384303; -.
DR   HOVERGEN; HBG073518; -.
DR   InParanoid; Q9JKV1; -.
DR   OMA; MNVPAGP; -.
DR   OrthoDB; EOG4QZ7MN; -.
DR   NextBio; 312618; -.
DR   Bgee; Q9JKV1; -.
DR   CleanEx; MM_ADRM1; -.
DR   Genevestigator; Q9JKV1; -.
DR   GermOnline; ENSMUSG00000039041; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0060612; P:adipose tissue development; IMP:BHF-UCL.
DR   GO; GO:0042699; P:follicle-stimulating hormone signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0048477; P:oogenesis; IMP:BHF-UCL.
DR   GO; GO:0060399; P:positive regulation of growth hormone receptor signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0033081; P:regulation of T cell differentiation in thymus; IMP:BHF-UCL.
DR   GO; GO:0060009; P:Sertoli cell development; IMP:BHF-UCL.
DR   GO; GO:0007286; P:spermatid development; IMP:BHF-UCL.
DR   GO; GO:0048538; P:thymus development; IMP:BHF-UCL.
DR   InterPro; IPR006773; 26S_Psome_Ubiquitin-recp_Rpn13.
DR   PANTHER; PTHR12225; ARM_1; 1.
DR   Pfam; PF04683; ARM_1; 1.
DR   PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Proteasome; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    407       Proteasomal ubiquitin receptor ADRM1.
FT                                /FTId=PRO_0000020632.
FT   DOMAIN       22    130       PH.
FT   REGION        2    132       Interaction with PSMD1.
FT   REGION      362    407       Interaction with UCHL5 (By similarity).
FT   COMPBIAS    135    202       Gly-rich.
FT   COMPBIAS    193    257       Ser-rich.
FT   COMPBIAS    203    213       Poly-Ser.
FT   MOD_RES       2      2       N-acetylthreonine (By similarity).
FT   MOD_RES      21     21       N6-acetyllysine (By similarity).
FT   MOD_RES     211    211       Phosphoserine (By similarity).
FT   MOD_RES     213    213       Phosphoserine.
FT   MOD_RES     217    217       Phosphothreonine (By similarity).
FT   MOD_RES     220    220       Phosphoserine (By similarity).
FT   MOD_RES     405    405       Phosphoserine (By similarity).
FT   CROSSLNK     34     34       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CONFLICT    109    109       M -> I (in Ref. 2; BAC35889).
FT   CONFLICT    171    171       L -> I (in Ref. 2; BAE26653).
FT   CONFLICT    226    226       R -> S (in Ref. 2; BAC35889).
FT   CONFLICT    359    359       F -> I (in Ref. 1; AAF33401).
FT   STRAND       24     34
FT   STRAND       37     40
FT   STRAND       45     51
FT   STRAND       57     63
FT   TURN         64     66
FT   STRAND       69     74
FT   STRAND       79     84
FT   STRAND       93     98
FT   TURN         99    101
FT   STRAND      104    109
FT   STRAND      111    114
FT   HELIX       117    129
SQ   SEQUENCE   407 AA;  42060 MW;  210AFDF7379C962D CRC64;
     MTTSGALFPS LVPGSRGSST KYLVEFRAGK MSLKGTTVTP DKRKGLVYIQ QTDDSLIHFC
     WKDRTSGTVE DDLIIFPDDC EFKRVPQCPS GRVYVLKFKA GSKRLFFWMQ EPKTDQDEEH
     CRKVNECLNN PPMPGSLGAS GSSGHELSAL GGEGGLQSLL GNMSHSQLMQ LIGPAGLGGL
     GGLGALTGPG LASLLGSSGP PASSSSSSSR SQSAAVTPSS STSSARATPA PSAPAAASAT
     SPSPAPSSGN GTSTAASPTQ PIQLSDLQSI LATMNVPAGP GGSQQVDLAS VLTPEIMAPI
     LANADVQERL LPYLPSGESL PQTADEIQNT LTSPQFQQAL GMFSAALASG QLGPLMCQFG
     LPAEAVEAAN KGDVEAFAKA MQNNAKSDPK EGDTKDKKDE EEDMSLD
//
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   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.
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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   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   SEM7A_MOUSE             Reviewed;         664 AA.
AC   Q9QUR8; O88371;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Semaphorin-7A;
DE   AltName: Full=Semaphorin-K1;
DE            Short=Sema K1;
DE   AltName: Full=Semaphorin-L;
DE            Short=Sema L;
DE   AltName: CD_antigen=CD108;
DE   Flags: Precursor;
GN   Name=Sema7a; Synonyms=Cd108, Semal, Semk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
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=99096477; PubMed=9878861; DOI=10.1016/S0167-4781(98)00245-0;
RA   Sato Y., Takahashi H.;
RT   "Molecular cloning and expression of murine homologue of semaphorin K1
RT   gene.";
RL   Biochim. Biophys. Acta 1443:419-422(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   MEDLINE=98389619; PubMed=9721204; DOI=10.1006/geno.1998.5256;
RA   Lange C., Liehr T., Goen M., Gebhart E., Fleckenstein B., Ensser A.;
RT   "New eukaryotic semaphorins with close homology to semaphorins of DNA
RT   viruses.";
RL   Genomics 51:340-350(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   MEDLINE=20340072; PubMed=10885563;
RX   DOI=10.1034/j.1399-0039.2000.550505.x;
RA   Mine T., Harada K., Matsumoto T., Yamana H., Shirouzu K., Itoh K.,
RA   Yamada A.;
RT   "CDw108 expression during T-cell development.";
RL   Tissue Antigens 55:429-436(2000).
RN   [4]
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   [5]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=12879062; DOI=10.1038/nature01790;
RA   Pasterkamp R.J., Peschon J.J., Spriggs M.K., Kolodkin A.L.;
RT   "Semaphorin 7A promotes axon outgrowth through integrins and MAPKs.";
RL   Nature 424:398-405(2003).
RN   [6]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=16713976; DOI=10.1016/j.immuni.2006.03.013;
RA   Czopik A.K., Bynoe M.S., Palm N., Raine C.S., Medzhitov R.;
RT   "Semaphorin 7A is a negative regulator of T cell responses.";
RL   Immunity 24:591-600(2006).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH
RP   ITGA1 AND ITGB1, AND TISSUE SPECIFICITY.
RX   PubMed=17377534; DOI=10.1038/nature05652;
RA   Suzuki K., Okuno T., Yamamoto M., Pasterkamp R.J., Takegahara N.,
RA   Takamatsu H., Kitao T., Takagi J., Rennert P.D., Kolodkin A.L.,
RA   Kumanogoh A., Kikutani H.;
RT   "Semaphorin 7A initiates T-cell-mediated inflammatory responses
RT   through alpha1beta1 integrin.";
RL   Nature 446:680-684(2007).
CC   -!- FUNCTION: Plays an important role in integrin-mediated signaling
CC       and functions both in regulating cell migration and immune
CC       responses. Promotes formation of focal adhesion complexes,
CC       activation of the protein kinase PTK2/FAK1 and subsequent
CC       phosphorylation of MAPK1 and MAPK3. Promotes production of
CC       proinflammatory cytokines by monocytes and macrophages. Plays an
CC       important role in modulating inflammation and T cell-mediated
CC       immune responses. Promotes axon growth in the embryonic olfactory
CC       bulb. Promotes attachment, spreading and dendrite outgrowth in
CC       melanocytes.
CC   -!- SUBUNIT: Interacts with PLXNC1 (By similarity). Interacts with
CC       ITGA1 and ITGB1.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor;
CC       Extracellular side.
CC   -!- TISSUE SPECIFICITY: Highly expressed in activated T cells (at
CC       protein level). Highest expression in brain. Lower in heart,
CC       thymus, spleen, testis and ovary. The expression increases in late
CC       embryonic and postnatal stages. Detected in T cells.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice display normal
CC       levels of lymphocytes in spleen, and normal activation of T cells
CC       by antigenic stimuli. In contrast, production of proinflammatory
CC       cytokines by macrophages is much reduced. The effect on contact
CC       hypersensitivity and experimental autoimmune encephalomyelitis is
CC       controversial. Reduced size of the lateral olfactory tract.
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   -!- CAUTION: The exact role in regulating T cell function is under
CC       debate. According to (PubMed:16713976), SEMA7A-deficient mice are
CC       highly susceptible to contact hypersensitivity and experimental
CC       autoimmune encephalomyelitis. According to (PubMed:17377534) mice
CC       do not develop contact hypersensitivity, and are highly resistant
CC       to experimental autoimmune encephalomyelitis.
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DR   EMBL; AB017532; BAA75665.1; -; mRNA.
DR   EMBL; AF030699; AAC34262.1; -; mRNA.
DR   EMBL; AF176670; AAD53118.1; -; mRNA.
DR   EMBL; BC057875; AAH57875.1; -; mRNA.
DR   IPI; IPI00315280; -.
DR   RefSeq; NP_035482.1; NM_011352.2.
DR   UniGene; Mm.335187; -.
DR   ProteinModelPortal; Q9QUR8; -.
DR   SMR; Q9QUR8; 46-631.
DR   STRING; Q9QUR8; -.
DR   PRIDE; Q9QUR8; -.
DR   Ensembl; ENSMUST00000043059; ENSMUSP00000042211; ENSMUSG00000038264.
DR   GeneID; 20361; -.
DR   KEGG; mmu:20361; -.
DR   UCSC; uc009pvy.1; mouse.
DR   CTD; 20361; -.
DR   MGI; MGI:1306826; Sema7a.
DR   eggNOG; maNOG12005; -.
DR   GeneTree; ENSGT00390000013125; -.
DR   HOGENOM; HBG127219; -.
DR   HOVERGEN; HBG079171; -.
DR   InParanoid; Q9QUR8; -.
DR   OMA; CILFIEN; -.
DR   OrthoDB; EOG4N30ND; -.
DR   NextBio; 298249; -.
DR   ArrayExpress; Q9QUR8; -.
DR   Bgee; Q9QUR8; -.
DR   Genevestigator; Q9QUR8; -.
DR   GermOnline; ENSMUSG00000038264; Mus musculus.
DR   GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
DR   GO; GO:0004872; F:receptor activity; IEA:InterPro.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB.
DR   GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR   GO; GO:0060907; P:positive regulation of macrophage cytokine production; IDA:UniProtKB.
DR   GO; GO:0050727; P:regulation of inflammatory response; IDA:UniProtKB.
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   Cell membrane; Developmental protein; Differentiation; Disulfide bond;
KW   Glycoprotein; GPI-anchor; Immunoglobulin domain;
KW   Inflammatory response; Lipoprotein; Membrane; Neurogenesis; Signal.
FT   SIGNAL        1     44       Potential.
FT   CHAIN        45    646       Semaphorin-7A.
FT                                /FTId=PRO_0000032349.
FT   PROPEP      647    664       Removed in mature form (Potential).
FT                                /FTId=PRO_0000032350.
FT   DOMAIN       53    488       Sema.
FT   DOMAIN      542    627       Ig-like C2-type.
FT   REGION      265    267       Interaction with integrins (By
FT                                similarity).
FT   MOTIF       265    267       Cell attachment site (Potential).
FT   LIPID       646    646       GPI-anchor amidated alanine (Potential).
FT   CARBOHYD    102    102       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    154    154       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    256    256       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    328    328       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    600    600       N-linked (GlcNAc...) (Potential).
FT   DISULFID    117    123       By similarity.
FT   DISULFID    140    149       By similarity.
FT   DISULFID    264    364       By similarity.
FT   DISULFID    289    333       By similarity.
FT   DISULFID    491    509       By similarity.
FT   DISULFID    498    539       By similarity.
FT   DISULFID    501    516       By similarity.
FT   DISULFID    564    611       By similarity.
FT   DISULFID    585    594       By similarity.
FT   CONFLICT    357    357       P -> S (in Ref. 2; AAC34262).
SQ   SEQUENCE   664 AA;  74994 MW;  1804A31C3C55B715 CRC64;
     MTPPPPGRAA PSAPRARVLS LPARFGLPLR LRLLLVFWVA AASAQGHSRS GPRISAVWKG
     QDHVDFSQPE PHTVLFHEPG SFSVWVGGRG KVYHFNFPEG KNASVRTVNI GSTKGSCQDK
     QDCGNYITLL ERRGNGLLVC GTNARKPSCW NLVNDSVVMS LGEMKGYAPF SPDENSLVLF
     EGDEVYSTIR KQEYNGKIPR FRRIRGESEL YTSDTVMQNP QFIKATIVHQ DQAYDDKIYY
     FFREDNPDKN PEAPLNVSRV AQLCRGDQGG ESSLSVSKWN TFLKAMLVCS DAATNRNFNR
     LQDVFLLPDP SGQWRDTRVY GVFSNPWNYS AVCVYSLGDI DRVFRTSSLK GYHMGLPNPR
     PGMCLPKKQP IPTETFQVAD SHPEVAQRVE PMGPLKTPLF HSKYHYQKVV VHRMQASNGE
     TFHVLYLTTD RGTIHKVVES GDQDHSFVFN IMEIQPFHRA AAIQAISLDA DRRKLYVTSQ
     WEVSQVPLDM CEVYSGGCHG CLMSRDPYCG WDQDRCVSIY SSQRSVLQSI NPAEPHRECP
     NPKPDEAPLQ KVSLARNSRY YLTCPMESRH ATYLWRHEEN VEQSCEPGHQ SPSCILFIEN
     LTARQYGHYR CEAQEGSYLR EAQHWELLPE DRALAEQLMG HARALAASFW LGVLPTLILG
     LLVH
//
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;
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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   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.
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; 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   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.
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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   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   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.
CC   -----------------------------------------------------------------------
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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   SPY2_MOUSE              Reviewed;         315 AA.
AC   Q9QXV8; Q9WUQ9;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Protein sprouty homolog 2;
DE            Short=Spry-2;
GN   Name=Spry2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster;
RX   MEDLINE=99175483; PubMed=10074434; DOI=10.1016/S0960-9822(99)80094-3;
RA   Tefft J.D., Lee M., Smith S., Leinwand M., Zhao J., Bringas P. Jr.,
RA   Crowe D.L., Warburton D.;
RT   "Conserved function of mSpry-2, a murine homolog of Drosophila
RT   sprouty, which negatively modulates respiratory organogenesis.";
RL   Curr. Biol. 9:219-222(1999).
CC   -!- FUNCTION: May function as an antagonist of fibroblast growth
CC       factor (FGF) pathways and may negatively modulate respiratory
CC       organogenesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection,
CC       ruffle membrane. Note=Associated with microtubules in unstimulated
CC       cells but is translocated to the membrane ruffles in cells
CC       stimulated ith EGF (epidermal growth factor).
CC   -!- TISSUE SPECIFICITY: In adult, highly expressed in brain, lung,
CC       heart and at lower levels in skeletal muscle and kidney. In
CC       embryo, highly expressed in lung epithelial cells, primarily in
CC       the distal airways.
CC   -!- DEVELOPMENTAL STAGE: At E8.5 expressed in the primitive streak,
CC       rostral forebrain, cells lateral to the posterior hindbrain,
CC       anterior hindbrain and developing midbrain. At E9.5 continues to
CC       be expressed in the rostral forebrain and primitive streak, and is
CC       also detected in the branchial arches and the forelimb bud. At
CC       E10.5 expressed in the somites, frontonasal processes, tailbud,
CC       and hindlimb bud.
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF176905; AAD56006.1; -; mRNA.
DR   EMBL; AF153084; AAD34167.1; -; mRNA.
DR   IPI; IPI00135613; -.
DR   RefSeq; NP_036027.1; NM_011897.3.
DR   UniGene; Mm.479257; -.
DR   UniGene; Mm.481243; -.
DR   UniGene; Mm.89982; -.
DR   ProteinModelPortal; Q9QXV8; -.
DR   IntAct; Q9QXV8; 1.
DR   STRING; Q9QXV8; -.
DR   PhosphoSite; Q9QXV8; -.
DR   PRIDE; Q9QXV8; -.
DR   Ensembl; ENSMUST00000022709; ENSMUSP00000022709; ENSMUSG00000022114.
DR   GeneID; 24064; -.
DR   KEGG; mmu:24064; -.
DR   UCSC; uc007uxy.1; mouse.
DR   CTD; 24064; -.
DR   MGI; MGI:1345138; Spry2.
DR   eggNOG; roNOG10965; -.
DR   GeneTree; ENSGT00390000003535; -.
DR   HOGENOM; HBG444143; -.
DR   HOVERGEN; HBG003544; -.
DR   InParanoid; Q9QXV8; -.
DR   OMA; SAQHKHE; -.
DR   OrthoDB; EOG43TZW1; -.
DR   PhylomeDB; Q9QXV8; -.
DR   NextBio; 304033; -.
DR   ArrayExpress; Q9QXV8; -.
DR   Bgee; Q9QXV8; -.
DR   CleanEx; MM_SPRY2; -.
DR   Genevestigator; Q9QXV8; -.
DR   GermOnline; ENSMUSG00000022114; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0048754; P:branching morphogenesis of a tube; IMP:MGI.
DR   GO; GO:0045165; P:cell fate commitment; IGI:MGI.
DR   GO; GO:0042472; P:inner ear morphogenesis; IGI:MGI.
DR   GO; GO:0060437; P:lung growth; IDA:MGI.
DR   GO; GO:0060425; P:lung morphogenesis; IDA:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IDA:MGI.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:MGI.
DR   GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IDA:MGI.
DR   GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:MGI.
DR   GO; GO:0051387; P:negative regulation of nerve growth factor receptor signaling pathway; IDA:MGI.
DR   GO; GO:0034261; P:negative regulation of Ras GTPase activity; IDA:MGI.
DR   GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IDA:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR   InterPro; IPR007875; Sprouty.
DR   Pfam; PF05210; Sprouty; 1.
DR   PROSITE; PS51227; SPR; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW   Developmental protein; Membrane; Microtubule; Phosphoprotein.
FT   CHAIN         1    315       Protein sprouty homolog 2.
FT                                /FTId=PRO_0000076902.
FT   DOMAIN      177    291       SPR.
FT   COMPBIAS    124    130       Poly-Ser.
FT   COMPBIAS    178    301       Cys-rich.
FT   MOD_RES     140    140       Phosphoserine (By similarity).
FT   CONFLICT    163    163       V -> I (in Ref. 2; AAD34167).
SQ   SEQUENCE   315 AA;  34623 MW;  81514698EAD809A7 CRC64;
     MEARAQSGNG SQPLLQTAHD SGRQRGEPDP RDALTQQVHV LSLDQIRAIR NTNEYTEGPT
     VVPRPGLKPA PRPSTQHKHE RLHGLPEHRQ PPRLQPSQVH SSRAPLSRSI STVSSGSRSS
     TRTSTSSSSS EQRLLGPSFS HGPAAADGII RVQPKSELKP GDVKPLSKDD LGLHAYRCED
     CGKCKCKECT YPRPLPSDWI CDKQCLCSAQ NVIDYGTCVC CVKGLFYHCS NDDEDNCADN
     PCSCSQSHCC TRWSAMGVMS LFLPCLWCYL PAKGCLKLCQ GCYDRVNRPG CRCKNSNTVC
     CKVPTVPPRN FEKPT
//
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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   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).
CC   -----------------------------------------------------------------------
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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   DNJB1_MOUSE             Reviewed;         340 AA.
AC   Q9QYJ3;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=DnaJ homolog subfamily B member 1;
DE   AltName: Full=Heat shock 40 kDa protein 1;
DE            Short=HSP40;
DE            Short=Heat shock protein 40;
GN   Name=Dnajb1; Synonyms=Hsp40, Hspf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; 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=Liver, and Testis;
RX   MEDLINE=20541279; PubMed=11092732;
RA   Hata M., Ohtsuka K.;
RT   "Cloning and expression of murine Hsp40 gene: differences in
RT   initiation sites between heat-induced and constitutive transcripts.";
RL   DNA Seq. 11:213-223(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).
CC   -!- FUNCTION: Interacts with HSP70 and can stimulate its ATPase
CC       activity. Stimulates the association between HSC70 and HIP (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with DNAJC3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Nucleus, nucleolus (By similarity). Note=Translocates
CC       rapidly from the cytoplasm to the nucleus, and especially to the
CC       nucleoli, upon heat shock (By similarity).
CC   -!- INDUCTION: By heat shock (By similarity).
CC   -!- SIMILARITY: Contains 1 J domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AB028272; BAA88083.1; -; mRNA.
DR   EMBL; AB028273; BAA95672.1; -; Genomic_DNA.
DR   EMBL; BC012962; AAH12962.1; -; mRNA.
DR   IPI; IPI00136253; -.
DR   RefSeq; NP_061278.1; NM_018808.2.
DR   UniGene; Mm.282092; -.
DR   ProteinModelPortal; Q9QYJ3; -.
DR   SMR; Q9QYJ3; 1-74, 118-335.
DR   STRING; Q9QYJ3; -.
DR   PhosphoSite; Q9QYJ3; -.
DR   PRIDE; Q9QYJ3; -.
DR   Ensembl; ENSMUST00000005620; ENSMUSP00000005620; ENSMUSG00000005483.
DR   GeneID; 81489; -.
DR   KEGG; mmu:81489; -.
DR   UCSC; uc009mkp.1; mouse.
DR   CTD; 81489; -.
DR   MGI; MGI:1931874; Dnajb1.
DR   GeneTree; ENSGT00600000084029; -.
DR   HOGENOM; HBG635315; -.
DR   HOVERGEN; HBG066727; -.
DR   InParanoid; Q9QYJ3; -.
DR   OMA; GGFTNMN; -.
DR   OrthoDB; EOG4PVP00; -.
DR   PhylomeDB; Q9QYJ3; -.
DR   NextBio; 350390; -.
DR   ArrayExpress; Q9QYJ3; -.
DR   Bgee; Q9QYJ3; -.
DR   CleanEx; MM_DNAJB1; -.
DR   Genevestigator; Q9QYJ3; -.
DR   GermOnline; ENSMUSG00000005483; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0051085; P:chaperone mediated protein folding requiring cofactor; IGI:MGI.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Acetylation; Chaperone; Cytoplasm; Nucleus; Stress response.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    340       DnaJ homolog subfamily B member 1.
FT                                /FTId=PRO_0000071017.
FT   DOMAIN        2     70       J.
FT   MOD_RES      44     44       N6-acetyllysine (By similarity).
SQ   SEQUENCE   340 AA;  38167 MW;  F775BFBA4A5D324E CRC64;
     MGKDYYQTLG LARGASDDEI KRAYRRQALR YHPDKNKEPG AEEKFKEIAE AYDVLSDPRK
     REIFDRYGEE GLKGGSPSGG SSGGANGTSF SYTFHGDPHA MFAEFFGGRN PFDTFFGQRN
     GEEGMDIDDT FSSFPMGMGG FTNMNFGRSR PSQEPTRKKQ DPPVTHDLRV SLEEIYSGCT
     KKMKISHKRL NPDGKSIRNE DKILTIEVKR GWKEGTKITF PKEGDQTSNN IPADIVFVLK
     DKPHNIFKRD GSDVIYPARI SLREALCGCT VNVPTLDGRT IPVVFKDVIR PGMRRKVPGE
     GLPLPKTPEK RGDLVIEFEV IFPERIPVSS RTILEQVLPI
//
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   FBX6_MOUSE              Reviewed;         295 AA.
AC   Q9QZN4; A2A7H0; A2A7H2; B2KFL0; B2KFL2; Q3TML5; Q3UCB0;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=F-box only protein 6;
DE   AltName: Full=F-box only protein 6b;
DE   AltName: Full=F-box protein that recognizes sugar chains 2;
DE   AltName: Full=F-box/G-domain protein 2;
GN   Name=Fbxo6; Synonyms=Fbs2, Fbxo6b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, 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/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting 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 (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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   FUNCTION, IDENTIFICATION IN A SCF PROTEIN LIGASE COMPLEX,
RP   SUGAR-BINDING, AND TISSUE SPECIFICITY.
RX   PubMed=12939278; DOI=10.1074/jbc.M304157200;
RA   Yoshida Y., Tokunaga F., Chiba T., Iwai K., Tanaka K., Tai T.;
RT   "Fbs2 is a new member of the E3 ubiquitin ligase family that
RT   recognizes sugar chains.";
RL   J. Biol. Chem. 278:43877-43884(2003).
RN   [7]
RP   FUNCTION, SUGAR-BINDING, AND INTERACTION WITH VCP.
RX   PubMed=15723043; DOI=10.1038/sj.embor.7400351;
RA   Yoshida Y., Adachi E., Fukiya K., Iwai K., Tanaka K.;
RT   "Glycoprotein-specific ubiquitin ligases recognize N-glycans in
RT   unfolded substrates.";
RL   EMBO Rep. 6:239-244(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., 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   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 some SCF (SKP1-CUL1-
CC       F-box protein)-type E3 ubiquitin ligase complexes. Involved in DNA
CC       damage response by specifically recognizing activated CHK1
CC       (phosphorylated on 'Ser-345'), promoting its ubiquitination and
CC       degradation. Ubiquitination of CHK1 is required to insure that
CC       activated CHK1 does not accumulate as cells progress through S
CC       phase, or when replication forks encounter transient impediments
CC       during normal DNA replication (By similarity). Involved in
CC       endoplasmic reticulum-associated degradation pathway (ERAD) for
CC       misfolded lumenal proteins by recognizing and binding sugar chains
CC       on unfolded glycoproteins that are retrotranlocated into the
CC       cytosol and promoting their ubiquitination and subsequent
CC       degradation. Able to recognize and bind denatured glycoproteins,
CC       which are modified with not only high-mannose but also complex-
CC       type oligosaccharides. Also recognizes sulfated glycans.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with CHK1 and CUL1 (By similarity). Part of a
CC       SCF (SKP1-cullin-F-box) protein ligase complex. Interacts with
CC       VCP.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Present in liver and kidney (at protein
CC       level). Widely expressed.
CC   -!- DEVELOPMENTAL STAGE: Weakly expressed in embryos.
CC   -!- SIMILARITY: Contains 1 F-box domain.
CC   -!- SIMILARITY: Contains 1 FBA (F-box associated) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM14908.1; Type=Erroneous gene model prediction;
CC       Sequence=CAQ51914.1; Type=Erroneous gene model prediction;
CC       Sequence=CAQ52206.1; Type=Erroneous gene model prediction;
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DR   EMBL; AF176526; AAF09135.1; -; mRNA.
DR   EMBL; AK002840; BAB22397.1; -; mRNA.
DR   EMBL; AK150612; BAE29703.1; -; mRNA.
DR   EMBL; AK152888; BAE31571.1; -; mRNA.
DR   EMBL; AK165867; BAE38426.1; -; mRNA.
DR   EMBL; AK170743; BAE41996.1; -; mRNA.
DR   EMBL; AK171483; BAE42484.1; -; mRNA.
DR   EMBL; AL606929; CAM14906.1; -; Genomic_DNA.
DR   EMBL; AL606929; CAM14908.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CU207376; CAQ51912.1; -; Genomic_DNA.
DR   EMBL; CU207417; CAQ51912.1; JOINED; Genomic_DNA.
DR   EMBL; CU207376; CAQ51914.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CU207417; CAQ51914.1; JOINED; Genomic_DNA.
DR   EMBL; CU207417; CAQ52204.1; -; Genomic_DNA.
DR   EMBL; CU207376; CAQ52204.1; JOINED; Genomic_DNA.
DR   EMBL; CU207417; CAQ52206.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CU207376; CAQ52206.1; JOINED; Genomic_DNA.
DR   EMBL; CH466594; EDL14804.1; -; Genomic_DNA.
DR   EMBL; CH466594; EDL14805.1; -; Genomic_DNA.
DR   EMBL; CH466594; EDL14807.1; -; Genomic_DNA.
DR   EMBL; BC017512; AAH17512.1; -; mRNA.
DR   IPI; IPI00137697; -.
DR   RefSeq; NP_001157176.1; NM_001163704.1.
DR   RefSeq; NP_001157177.1; NM_001163705.1.
DR   RefSeq; NP_001157178.1; NM_001163706.1.
DR   RefSeq; NP_001157179.1; NM_001163707.1.
DR   RefSeq; NP_056612.1; NM_015797.4.
DR   UniGene; Mm.27445; -.
DR   ProteinModelPortal; Q9QZN4; -.
DR   SMR; Q9QZN4; 2-250.
DR   STRING; Q9QZN4; -.
DR   PRIDE; Q9QZN4; -.
DR   Ensembl; ENSMUST00000030858; ENSMUSP00000030858; ENSMUSG00000055401.
DR   Ensembl; ENSMUST00000056965; ENSMUSP00000062348; ENSMUSG00000055401.
DR   Ensembl; ENSMUST00000105706; ENSMUSP00000101331; ENSMUSG00000055401.
DR   GeneID; 50762; -.
DR   KEGG; mmu:50762; -.
DR   UCSC; uc008vud.1; mouse.
DR   CTD; 50762; -.
DR   MGI; MGI:1354743; Fbxo6.
DR   GeneTree; ENSGT00390000003865; -.
DR   HOGENOM; HBG716440; -.
DR   HOVERGEN; HBG003593; -.
DR   InParanoid; Q9QZN4; -.
DR   OMA; WRDLIDV; -.
DR   OrthoDB; EOG4VX267; -.
DR   PhylomeDB; Q9QZN4; -.
DR   NextBio; 307659; -.
DR   ArrayExpress; Q9QZN4; -.
DR   Bgee; Q9QZN4; -.
DR   CleanEx; MM_FBXO6; -.
DR   Genevestigator; Q9QZN4; -.
DR   GermOnline; ENSMUSG00000055401; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR   GO; GO:0030246; F:carbohydrate binding; IDA:MGI.
DR   GO; GO:0001948; F:glycoprotein binding; IDA:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:MGI.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0030433; P:ER-associated protein catabolic process; IMP:UniProtKB.
DR   GO; GO:0006516; P:glycoprotein catabolic process; IDA:MGI.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Cytoplasm; DNA damage; DNA repair; Phosphoprotein;
KW   Ubl conjugation pathway; Unfolded protein response.
FT   CHAIN         1    295       F-box only protein 6.
FT                                /FTId=PRO_0000119883.
FT   DOMAIN        1     48       F-box.
FT   DOMAIN       69    250       FBA.
FT   MOD_RES     276    276       Phosphoserine.
FT   CONFLICT     77     77       R -> K (in Ref. 3; CAQ52204/CAQ52206/
FT                                CAQ51912/CAQ51914 and 4; EDL14807/
FT                                EDL14805/EDL14804).
FT   CONFLICT    252    252       T -> A (in Ref. 2; BAE29703).
SQ   SEQUENCE   295 AA;  34493 MW;  D515D3C25CC73B22 CRC64;
     MVHINELPEN ILLELFIHIP APQLLRNCRL VCRLWRDLID VVSLWKRKSL REGFFTKDRC
     EPVEDWKVFY ILCSLQRNLL RNPCAEENLS SWRIDSNGGD RWKVETLPGS CGTSFPDNKV
     KKYFVTSFEM CLKSQMVDLK AEGYCEELMD TFRPDIVVKD WVAPRADCGC TYQLRVQLAS
     ADYIVLASFE PPPVTFQQWN DAKWQEISHT FSDYPPGVRH ILFQHGGQDT QFWKGWYGPR
     VTNSSIIISH RTAKNPPPAR TLPEETVVIG RRRRASDSNT HEGFFWQGLW QRLRR
//
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   PLOD3_MOUSE             Reviewed;         741 AA.
AC   Q9R0E1; Q542E0; Q9CYY9;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3;
DE            EC=1.14.11.4;
DE   AltName: Full=Lysyl hydroxylase 3;
DE            Short=LH3;
DE   Flags: Precursor;
GN   Name=Plod3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=99357020; PubMed=10429951; DOI=10.1016/S0945-053X(99)00016-5;
RA   Ruotsalainen H., Sipila L., Kerkela E., Pospiech H., Myllylae R.;
RT   "Characterization of cDNAs for mouse lysyl hydroxylase 1, 2 and 3,
RT   their phylogenetic analysis and tissue-specific expression in the
RT   mouse.";
RL   Matrix Biol. 18:325-329(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   MEDLINE=21233587; PubMed=11334715; DOI=10.1016/S0945-053X(01)00130-5;
RA   Ruotsalainen H., Vanhatupa S., Tampio M., Sipila L., Valtavaara M.,
RA   Myllylae R.;
RT   "Complete genomic structure of mouse lysyl hydroxylase 2 and lysyl
RT   hydroxylase 3/collagen glucosyltransferase.";
RL   Matrix Biol. 20:137-146(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, 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   [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   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-66, 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: Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences
CC       in collagens. These hydroxylysines serve as sites of attachment
CC       for carbohydrate units and are essential for the stability of the
CC       intermolecular collagen cross-links.
CC   -!- CATALYTIC ACTIVITY: L-lysine-[procollagen] + 2-oxoglutarate + O(2)
CC       = (2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO(2).
CC   -!- COFACTOR: Iron.
CC   -!- COFACTOR: Ascorbate.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane;
CC       Peripheral membrane protein; Lumenal side.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the heart, lung, liver and
CC       testis.
CC   -!- SIMILARITY: Contains 1 Fe2OG dioxygenase 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; AF046783; AAD54618.1; -; mRNA.
DR   EMBL; AY014830; AAK00576.1; -; Genomic_DNA.
DR   EMBL; AK013195; BAB28704.1; -; mRNA.
DR   EMBL; AK033360; BAC28246.1; -; mRNA.
DR   EMBL; AK088948; BAC40669.1; -; mRNA.
DR   EMBL; BC043047; AAH43047.1; -; mRNA.
DR   EMBL; BC054734; AAH54734.1; -; mRNA.
DR   IPI; IPI00127406; -.
DR   RefSeq; NP_036092.1; NM_011962.3.
DR   UniGene; Mm.251003; -.
DR   ProteinModelPortal; Q9R0E1; -.
DR   STRING; Q9R0E1; -.
DR   PRIDE; Q9R0E1; -.
DR   Ensembl; ENSMUST00000004968; ENSMUSP00000004968; ENSMUSG00000004846.
DR   GeneID; 26433; -.
DR   KEGG; mmu:26433; -.
DR   UCSC; uc009abj.1; mouse.
DR   CTD; 26433; -.
DR   MGI; MGI:1347008; Plod3.
DR   eggNOG; roNOG07750; -.
DR   GeneTree; ENSGT00550000074427; -.
DR   HOGENOM; HBG380935; -.
DR   HOVERGEN; HBG053618; -.
DR   InParanoid; Q9R0E1; -.
DR   OMA; EPHIADS; -.
DR   OrthoDB; EOG4K0QMV; -.
DR   BRENDA; 1.14.11.4; 244.
DR   BRENDA; 2.4.1.66; 244.
DR   NextBio; 304493; -.
DR   ArrayExpress; Q9R0E1; -.
DR   Bgee; Q9R0E1; -.
DR   Genevestigator; Q9R0E1; -.
DR   GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
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:0033823; F:procollagen glucosyltransferase activity; IDA:MGI.
DR   GO; GO:0008475; F:procollagen-lysine 5-dioxygenase activity; IDA:MGI.
DR   GO; GO:0070831; P:basement membrane assembly; IMP:MGI.
DR   GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR   GO; GO:0001886; P:endothelial cell morphogenesis; IMP:MGI.
DR   GO; GO:0048730; P:epidermis morphogenesis; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0060425; P:lung morphogenesis; IMP:MGI.
DR   GO; GO:0021915; P:neural tube development; IMP:MGI.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   GO; GO:0042311; P:vasodilation; IMP:MGI.
DR   InterPro; IPR005123; Oxoglutarate/Fe-dep_oxygenase.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR001006; Procol_lys_dOase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
DR   PROSITE; PS01325; LYS_HYDROXYLASE; 1.
PE   1: Evidence at protein level;
KW   Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron; Membrane;
KW   Metal-binding; Oxidoreductase; Signal; Vitamin C.
FT   SIGNAL        1     27       Potential.
FT   CHAIN        28    741       Procollagen-lysine,2-oxoglutarate 5-
FT                                dioxygenase 3.
FT                                /FTId=PRO_0000024687.
FT   DOMAIN      650    741       Fe2OG dioxygenase.
FT   ACT_SITE    732    732       Potential.
FT   METAL       670    670       Iron (By similarity).
FT   METAL       672    672       Iron (By similarity).
FT   METAL       722    722       Iron (By similarity).
FT   CARBOHYD     66     66       N-linked (GlcNAc...).
FT   CARBOHYD    286    286       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    551    551       N-linked (GlcNAc...) (Potential).
FT   CONFLICT      8      8       P -> H (in Ref. 3; BAB28704).
SQ   SEQUENCE   741 AA;  84922 MW;  D1B79B386339D9F4 CRC64;
     MAAAGPEPRL LLLLLLLLPP LPPVTSASDR PRGANAVNPD KLLVITVATA ETEGYRRFLQ
     SAEFFNYTVR TLGLGQEWRG GDVARTVGGG QKVRWLKKEM EKYADQKDMI IMFVDSYDVI
     LASSPTELLK KFVQSGSHLL FSAESFCWPE WGLAEQYPEV GMGKRFLNSG GFIGFAPTIH
     QIVRQWNYKD DDDDQLFYTQ LYLDPGLREK LKLSLDHKSR IFQNLNGALD EVILKFDQNR
     VRIRNVAYDT LPVVVHGNGP TKLQLNYLGN YVPNGWTPQG GCGFCNQTLR TLPGGQPPPR
     VLLAVFVEQP TPFLPRFLQR LLLLDYPPDR ISLFLHNSEV YHEPHIADAW PQLQDHFSAV
     KLVGPEEALS AGEARDMAMD SCRQNPECEF YFSLDADAVL TNPETLRVLI EQNRKVIAPM
     LSRHGKLWSN FWGALSPNEY YARSEDYVEL VQRKRVGVWN VPYISQAYVI RGETLRTELP
     QKEVFSSSDT DPDMAFCKSV RDKGIFLHLS NQHEFGRLLA TSRYDTDHLH PDLWQIFDNP
     VDWREQYIHE NYSRALDGEG LVEQPCPDVY WFPLLTEQMC DELVEEMEHY GQWSGGRHED
     SRLAGGYENV PTVDIHMKQV GYEDQWLQLL RTYVGPMTEY LFPGYHTKTR AVMNFVVRYR
     PDEQPSLRPH HDSSTFTLNV ALNHKGVDYE GGGCRFLRYD CRISSPRKGW ALLHPGRLTH
     YHEGLPTTRG TRYIMVSFVD P
//
ID   PLOD1_MOUSE             Reviewed;         728 AA.
AC   Q9R0E2;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1;
DE            EC=1.14.11.4;
DE   AltName: Full=Lysyl hydroxylase 1;
DE            Short=LH1;
DE   Flags: Precursor;
GN   Name=Plod1; Synonyms=Plod;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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=99357020; PubMed=10429951; DOI=10.1016/S0945-053X(99)00016-5;
RA   Ruotsalainen H., Sipila L., Kerkela E., Pospiech H., Myllylae R.;
RT   "Characterization of cDNAs for mouse lysyl hydroxylase 1, 2 and 3,
RT   their phylogenetic analysis and tissue-specific expression in the
RT   mouse.";
RL   Matrix Biol. 18:325-329(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).
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-198, 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: Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences
CC       in collagens. These hydroxylysines serve as sites of attachment
CC       for carbohydrate units and are essential for the stability of the
CC       intermolecular collagen cross-links.
CC   -!- CATALYTIC ACTIVITY: L-lysine-[procollagen] + 2-oxoglutarate + O(2)
CC       = (2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO(2).
CC   -!- COFACTOR: Iron (By similarity).
CC   -!- COFACTOR: Ascorbate (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane;
CC       Peripheral membrane protein; Lumenal side.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the liver, heart, lung,
CC       skeletal muscle and kidney.
CC   -!- SIMILARITY: Contains 1 Fe2OG dioxygenase 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; AF046782; AAD54617.1; -; mRNA.
DR   EMBL; BC006599; AAH06599.1; -; mRNA.
DR   IPI; IPI00127407; -.
DR   RefSeq; NP_035252.1; NM_011122.3.
DR   UniGene; Mm.37371; -.
DR   ProteinModelPortal; Q9R0E2; -.
DR   SMR; Q9R0E2; 552-726.
DR   STRING; Q9R0E2; -.
DR   PRIDE; Q9R0E2; -.
DR   Ensembl; ENSMUST00000019199; ENSMUSP00000019199; ENSMUSG00000019055.
DR   GeneID; 18822; -.
DR   KEGG; mmu:18822; -.
DR   UCSC; uc008vtk.1; mouse.
DR   CTD; 18822; -.
DR   MGI; MGI:99907; Plod1.
DR   GeneTree; ENSGT00550000074427; -.
DR   HOGENOM; HBG380935; -.
DR   HOVERGEN; HBG053618; -.
DR   InParanoid; Q9R0E2; -.
DR   OMA; KFEMGHV; -.
DR   OrthoDB; EOG4K0QMV; -.
DR   BRENDA; 1.14.11.4; 244.
DR   NextBio; 295184; -.
DR   ArrayExpress; Q9R0E2; -.
DR   Bgee; Q9R0E2; -.
DR   Genevestigator; Q9R0E2; -.
DR   GermOnline; ENSMUSG00000019055; Mus musculus.
DR   GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
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:0008475; F:procollagen-lysine 5-dioxygenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR005123; Oxoglutarate/Fe-dep_oxygenase.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR001006; Procol_lys_dOase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
DR   PROSITE; PS01325; LYS_HYDROXYLASE; 1.
PE   1: Evidence at protein level;
KW   Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron; Membrane;
KW   Metal-binding; Oxidoreductase; Signal; Vitamin C.
FT   SIGNAL        1     18       By similarity.
FT   CHAIN        19    728       Procollagen-lysine,2-oxoglutarate 5-
FT                                dioxygenase 1.
FT                                /FTId=PRO_0000024679.
FT   DOMAIN      637    728       Fe2OG dioxygenase.
FT   ACT_SITE    719    719       Potential.
FT   METAL       657    657       Iron (By similarity).
FT   METAL       659    659       Iron (By similarity).
FT   METAL       709    709       Iron (By similarity).
FT   CARBOHYD    198    198       N-linked (GlcNAc...).
FT   CARBOHYD    539    539       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    687    687       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   728 AA;  83595 MW;  339C2D71976ED985 CRC64;
     MRSLLLLAPL AWLLLVQAKD DAKLEDNLLV LTVATKETEG FRRFKRSAQF FNYKIQSLGL
     GEDWSVDGGP AAAGGGQKVR LLKKALEKHA DKEDLVILFV DSYDVVFASG PRELLKKFQQ
     AKSQVVFSAE EHIYPDRRLE AKYPTVPDGK RFLGSGGFIG YAPSLSKLVA EWEGQDSDSD
     QLFYTKIFLN PEKREQINIS LDHRCRIFQN LDGALDEVVL KFEMGHVRAR NLAYDTLPVV
     VHGNGPTKLQ LNYLGNYIPR FWTFETGCTV CDEGLRSLKG IGDEALPTVL VGVFIEQPTP
     FLSLFFLRLL RLRYPQKQMR LFIHNQERHH KLQVEQFLAE HGSEYQSVKL VGPEVRMANA
     DARNMGADLC RQDQTCTYYF SVDADVALTE PNSLRLLIEQ NKNVIAPLMT RHGRLWSNFW
     GGLSADGYYA RSEDYVDIVQ GRRVGVWNVP YISNIYLIKG SALRAELQNV DLFHYSKLDS
     DMSFCANVRQ QEVFMFLTNR HTFGHLLSLD NYQTTHLHND LWEVFSNPED WKEKYIHENY
     TKALAGKLVE TPCPDVYWFP IFTEAACDEL VEEMEHYGQW SLGDNKDNRI QGGYENVPTI
     DIHMNQITFE REWHKFLVEY IAPMTEKLYP GYYTRAQFDL AFVVRYKPDE QPSLMPHHDA
     STFTVNIALN RVGEDYEGGG CRFLRYNCSV RAPRKGWALL HPGRLTHYHE GLPTTKGTRY
     IAVSFVDP
//
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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   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;
CC   -----------------------------------------------------------------------
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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   FOXO1_MOUSE             Reviewed;         652 AA.
AC   Q9R1E0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Forkhead box protein O1;
DE   AltName: Full=Forkhead box protein O1A;
DE   AltName: Full=Forkhead in rhabdomyosarcoma;
GN   Name=Foxo1; Synonyms=Fkhr, Foxo1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; 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 AT THR-24; SER-253 AND
RP   SER-316, AND MUTAGENESIS OF THR-24; SER-253 AND SER-316.
RC   TISSUE=Liver;
RX   MEDLINE=99278356; PubMed=10347145; DOI=10.1074/jbc.274.23.15982;
RA   Nakae J., Park B.C., Accili D.;
RT   "Insulin stimulates phosphorylation of the forkhead transcription
RT   factor FKHR on serine 253 through a Wortmannin-sensitive pathway.";
RL   J. Biol. Chem. 274:15982-15985(1999).
RN   [2]
RP   INTERACTION WITH LRPPRC.
RX   PubMed=17050673; DOI=10.1101/gad.1483906;
RA   Cooper M.P., Qu L., Rohas L.M., Lin J., Yang W., Erdjument-Bromage H.,
RA   Tempst P., Spiegelman B.M.;
RT   "Defects in energy homeostasis in Leigh syndrome French Canadian
RT   variant through PGC-1alpha/LRP130 complex.";
RL   Genes Dev. 20:2996-3009(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-464 AND SER-465, 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: Transcription factor (By similarity).
CC   -!- SUBUNIT: Interacts with LRPPRC.
CC   -!- INTERACTION:
CC       P10275:AR (xeno); NbExp=1; IntAct=EBI-1371343, EBI-608057;
CC       Q6PB66:Lrpprc; NbExp=2; IntAct=EBI-1371343, EBI-1371262;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between
CC       cytoplasm and nucleus.
CC   -!- PTM: IGF1 rapidly induces phosphorylation of Thr-24, Ser-253 and
CC       Ser-319. Phosphorylation of Ser-253 decreases DNA-binding activity
CC       and promotes the phosphorylation of Thr-24, and Ser-319, which
CC       leads to nuclear exclusion and loss of function. Phosphorylation
CC       of Ser-326 is independent of IGF1 and leads to reduced function.
CC       Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity). Phosphorylated by AKT; insulin-induced.
CC   -!- SIMILARITY: Contains 1 fork-head DNA-binding domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF126056; AAD40636.1; -; mRNA.
DR   IPI; IPI00314283; -.
DR   UniGene; Mm.29891; -.
DR   ProteinModelPortal; Q9R1E0; -.
DR   SMR; Q9R1E0; 151-241.
DR   IntAct; Q9R1E0; 8.
DR   MINT; MINT-5112421; -.
DR   STRING; Q9R1E0; -.
DR   PhosphoSite; Q9R1E0; -.
DR   PRIDE; Q9R1E0; -.
DR   Ensembl; ENSMUST00000053764; ENSMUSP00000055308; ENSMUSG00000044167.
DR   MGI; MGI:1890077; Foxo1.
DR   HOGENOM; HBG714085; -.
DR   HOVERGEN; HBG057789; -.
DR   InParanoid; Q9R1E0; -.
DR   OrthoDB; EOG49S66C; -.
DR   Reactome; REACT_13641; Regulation of Beta-Cell Development.
DR   ArrayExpress; Q9R1E0; -.
DR   Bgee; Q9R1E0; -.
DR   CleanEx; MM_FOXO1; -.
DR   Genevestigator; Q9R1E0; -.
DR   GermOnline; ENSMUSG00000044167; Mus musculus.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
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:0006916; P:anti-apoptosis; ISS:UniProtKB.
DR   GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR   GO; GO:0031018; P:endocrine pancreas development; TAS:Reactome.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IMP:MGI.
DR   GO; GO:0045722; P:positive regulation of gluconeogenesis; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR   GO; GO:0042127; P:regulation of cell proliferation; 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; PS00657; FORK_HEAD_1; FALSE_NEG.
DR   PROSITE; PS00658; FORK_HEAD_2; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; DNA-binding; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    652       Forkhead box protein O1.
FT                                /FTId=PRO_0000091873.
FT   DNA_BIND    156    232       Fork-head.
FT   COMPBIAS     89     96       Poly-Ala.
FT   COMPBIAS    135    139       Poly-Ala.
FT   MOD_RES      24     24       Phosphothreonine (Probable).
FT   MOD_RES     253    253       Phosphoserine; by PKB/AKT1.
FT   MOD_RES     284    284       Phosphoserine (By similarity).
FT   MOD_RES     316    316       Phosphoserine (Probable).
FT   MOD_RES     326    326       Phosphoserine; by DYRK1A (By similarity).
FT   MOD_RES     464    464       Phosphothreonine.
FT   MOD_RES     465    465       Phosphoserine.
FT   MOD_RES     506    506       Phosphoserine (By similarity).
FT   MUTAGEN      24     24       T->A: Decreases insulin-induced
FT                                phosphorylation by approximately 30%.
FT   MUTAGEN     253    253       S->A: Abolishes insulin-induced
FT                                phosphorylation.
FT   MUTAGEN     316    316       S->A: Decreases insulin-induced
FT                                phosphorylation by approximately 30%.
SQ   SEQUENCE   652 AA;  69502 MW;  3FE4C322AA85205F CRC64;
     MAEAPQVVET DPDFEPLPRQ RSCTWPLPRP EFNQSNSTTS SPAPSGGAAA NPDAAASLAS
     ASAVSTDFMS NLSLLEESED FARAPGCVAV AAAAAASRGL CGDFQGPEAG CVHPAPPQPP
     PTGPLSQPPP VPPSAAAAAG PLAGQPRKTS SSRRNAWGNL SYADLITKAI ESSAEKRLTL
     SQIYEWMVKS VPYFKDKGDS NSSAGWKNSI RHNLSLHSKF IRVQNEGTGK SSWWMLNPEG
     GKSGKSPRRR AASMDNNSKF AKSRGRAAKK KASLQSGQEG PGDSPGSQFS KWPASPGSHS
     NDDFDNWSTF RPRTSSNAST ISGRLSPIMT EQDDLGDGDV HSLVYPPSAA KMASTLPSLS
     EISNPENMEN LLDNLNLLSS PTSLTVSTQS SPGSMMQQTP CYSFAPPNTS LNSPSPNYSK
     YTYGQSSMSP LPQMPMQTLQ DSKSSYGGLN QYNCAPGLLK ELLTSDSPPH NDIMSPVDPG
     VAQPNSRVLG QNVMMGPNSV MPAYGSQASH NKMMNPSSHT HPGHAQQTAS VNGRTLPHVV
     NTMPHTSAMN RLTPVKTPLQ VPLSHPMQMS ALGSYSSVSS CNGYGRMGVL HQEKLPSDLD
     GMFIERLDCD MESIIRNDPM DGDTLDFNFD NVLPNQSFPH SVKTTTHSWV SG
//
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.
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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   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   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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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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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   WNT8B_MOUSE             Reviewed;         350 AA.
AC   Q9WUD6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Protein Wnt-8b;
DE   Flags: Precursor;
GN   Name=Wnt8b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   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=99373258; PubMed=10441746; DOI=10.1007/s003359901115;
RA   Richardson M., Redmond D., Watson C.J., Mason J.O.;
RT   "Mouse Wnt8B is expressed in the developing forebrain and maps to
RT   chromosome 19.";
RL   Mamm. Genome 10:923-925(1999).
CC   -!- FUNCTION: Ligand for members of the frizzled family of seven
CC       transmembrane receptors. May play an important role in the
CC       development and differentiation of certain forebrain structures,
CC       notably the hippocampus.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- SIMILARITY: Belongs to the Wnt family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF130349; AAD31816.1; -; mRNA.
DR   IPI; IPI00124527; -.
DR   UniGene; Mm.88365; -.
DR   STRING; Q9WUD6; -.
DR   Ensembl; ENSMUST00000041163; ENSMUSP00000042867; ENSMUSG00000036961.
DR   UCSC; uc008hpt.1; mouse.
DR   MGI; MGI:109485; Wnt8b.
DR   GeneTree; ENSGT00600000084119; -.
DR   HOVERGEN; HBG001595; -.
DR   InParanoid; Q9WUD6; -.
DR   OrthoDB; EOG4CNQRC; -.
DR   NextBio; 302861; -.
DR   ArrayExpress; Q9WUD6; -.
DR   Bgee; Q9WUD6; -.
DR   CleanEx; MM_WNT8B; -.
DR   Genevestigator; Q9WUD6; -.
DR   GermOnline; ENSMUSG00000036961; Mus musculus.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005102; F:receptor binding; TAS:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0007267; P:cell-cell signaling; TAS:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR   GO; GO:0009887; P:organ morphogenesis; TAS:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR   GO; GO:0007223; P:Wnt receptor signaling pathway, calcium modulating pathway; IEA:InterPro.
DR   InterPro; IPR013301; Wnt8.
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; PR01892; WNT8PROTEIN.
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; Glycoprotein; Secreted;
KW   Signal; Wnt signaling pathway.
FT   SIGNAL        1     21       Potential.
FT   CHAIN        22    350       Protein Wnt-8b.
FT                                /FTId=PRO_0000041451.
FT   CARBOHYD    102    102       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    258    258       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   350 AA;  38576 MW;  69CEE7790461597A CRC64;
     MFLMKPVCVL LVTCVLHRSH AWSVNNFLMT GPKAYLVYSS SVAAGAQSGI EECKYQFAWD
     RWNCPERALQ LSSHGGLRSA NRETAFVHAI SSAGVMYTLT RNCSLGDFDN CGCDDSRNGQ
     LGGQGWLWGG CSDNVGFGEA ISKQFVDALE TGQDARAAMN LHNNEAGRKA VKGTMKRTCK
     CHGVSGSCTT QTCWLQLPEF REVGAHLKEK YHAALKVDLL QGAGNSAAGR GAIADTFRSI
     STRELVHLED SPDYCLENKT LGLLGTEGRE CLRRGRALGR WERRSCRRLC GDCGLAVEER
     RAETVSSCNC KFHWCCAVRC EQCRRRVTKY FCSRAERPPR GAAHKPGKNS
//
ID   IF4H_MOUSE              Reviewed;         248 AA.
AC   Q9WUK2; Q9WUK3;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Eukaryotic translation initiation factor 4H;
DE            Short=eIF-4H;
DE   AltName: Full=Williams-Beuren syndrome chromosomal region 1 protein homolog;
GN   Name=Eif4h; Synonyms=Wbscr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; 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], ALTERNATIVE SPLICING, AND TISSUE
RP   SPECIFICITY.
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   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG).
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 SHORT).
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 97-109, 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   STRUCTURE BY NMR OF 32-125.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of RNA binding domain in eukaryotic translation
RT   initiation factor 4H.";
RL   Submitted (OCT-2006) to the PDB data bank.
CC   -!- FUNCTION: Stimulates the RNA helicase activity of EIF4A in the
CC       translation initiation complex. Binds weakly mRNA (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=Q9WUK2-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=Q9WUK2-2; Sequence=VSP_005800;
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in heart, liver and
CC       testis and at lower levels in brain, spleen, lung, skeletal
CC       muscle, kidney and embryonic tissues. Both isoforms are expressed
CC       at similar levels.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR   EMBL; AF139987; AAD34859.1; -; Genomic_DNA.
DR   EMBL; AF139987; AAD34860.1; -; Genomic_DNA.
DR   EMBL; AF289664; AAF99330.1; -; Genomic_DNA.
DR   EMBL; BC014796; AAH14796.1; -; mRNA.
DR   IPI; IPI00124742; -.
DR   IPI; IPI00222560; -.
DR   RefSeq; NP_291039.1; NM_033561.1.
DR   UniGene; Mm.27955; -.
DR   PDB; 2DNG; NMR; -; A=34-123.
DR   PDBsum; 2DNG; -.
DR   ProteinModelPortal; Q9WUK2; -.
DR   SMR; Q9WUK2; 27-125.
DR   STRING; Q9WUK2; -.
DR   PhosphoSite; Q9WUK2; -.
DR   PRIDE; Q9WUK2; -.
DR   Ensembl; ENSMUST00000036125; ENSMUSP00000048833; ENSMUSG00000040731.
DR   Ensembl; ENSMUST00000078220; ENSMUSP00000077347; ENSMUSG00000040731.
DR   GeneID; 22384; -.
DR   KEGG; mmu:22384; -.
DR   NMPDR; fig|10090.3.peg.4177; -.
DR   UCSC; uc008zwp.1; mouse.
DR   UCSC; uc008zwq.1; mouse.
DR   CTD; 22384; -.
DR   MGI; MGI:1341822; Eif4h.
DR   GeneTree; ENSGT00530000063406; -.
DR   HOGENOM; HBG717808; -.
DR   HOVERGEN; HBG018193; -.
DR   InParanoid; Q9WUK2; -.
DR   OMA; DRERTHY; -.
DR   OrthoDB; EOG46DM3S; -.
DR   PhylomeDB; Q9WUK2; -.
DR   NextBio; 302749; -.
DR   PMAP-CutDB; Q9WUK2; -.
DR   ArrayExpress; Q9WUK2; -.
DR   Bgee; Q9WUK2; -.
DR   CleanEx; MM_EIF4H; -.
DR   Genevestigator; Q9WUK2; -.
DR   GermOnline; ENSMUSG00000040731; Mus musculus.
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   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   3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW   Direct protein sequencing; Initiation factor; Phosphoprotein;
KW   Protein biosynthesis; RNA-binding.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    248       Eukaryotic translation initiation factor
FT                                4H.
FT                                /FTId=PRO_0000081620.
FT   DOMAIN       42    118       RRM.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      12     12       Phosphotyrosine (By similarity).
FT   MOD_RES      32     32       Phosphoserine (By similarity).
FT   MOD_RES      45     45       Phosphotyrosine (By similarity).
FT   MOD_RES     101    101       Phosphotyrosine (By similarity).
FT   MOD_RES     193    193       Phosphoserine (By similarity).
FT   MOD_RES     245    245       N6-acetyllysine (By similarity).
FT   VAR_SEQ     137    156       Missing (in isoform Short).
FT                                /FTId=VSP_005800.
FT   STRAND       38     40
FT   STRAND       42     48
FT   HELIX        55     61
FT   TURN         62     64
FT   STRAND       67     74
FT   STRAND       76     78
FT   STRAND       80     91
FT   HELIX        92     98
FT   HELIX        99    101
FT   STRAND      112    115
SQ   SEQUENCE   248 AA;  27341 MW;  23E5393BAF183477 CRC64;
     MADFDTYDDR AYSSFGGGRG SRGSAGGHGS RSQKELPTEP PYTAYVGNLP FNTVQGDIDA
     IFKDLSIRSV RLVRDKDTDK FKGFCYVEFD EVDSLKEALT YDGALLGDRS LRVDIAEGRK
     QDKGGFGFRK GGPDDRGMGG SRESRGGWDS RDDFNSGYRD DFLGGRGGSR PGDRRAGPPM
     GSRFRDGPPL RGSNMDFREP TEEERAQRPR LQLKPRTVAT PLNQVANPNS AIFGGARPRE
     EVVQKEQE
//
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.
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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   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   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   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   Distributed under the Creative Commons Attribution-NoDerivs License
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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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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   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.
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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   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.
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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   DYR1B_MOUSE             Reviewed;         629 AA.
AC   Q9Z188; Q3UFR5; Q70UR5; Q9EPM2;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 3.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=Dual specificity tyrosine-phosphorylation-regulated kinase 1B;
DE            EC=2.7.12.1;
GN   Name=Dyrk1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; 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/SvJ, and NMRI; TISSUE=Liver, and Testis;
RX   MEDLINE=99119336; PubMed=9918863; DOI=10.1006/bbrc.1998.9967;
RA   Leder S., Weber Y., Altafaj X., Estivill X., Joost H.-G., Becker W.;
RT   "Cloning and characterization of DYRK1B, a novel member of the DYRK
RT   family of protein kinases.";
RL   Biochem. Biophys. Res. Commun. 254:474-479(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, CATALYTIC ACTIVITY, AND FUNCTION.
RC   STRAIN=NMRI;
RX   PubMed=12633499; DOI=10.1042/BJ20030182;
RA   Leder S., Czajkowska H., Maenz B., De Graaf K., Barthel A.,
RA   Joost H.-G., Becker W.;
RT   "Alternative splicing variants of dual specificity tyrosine
RT   phosphorylated and regulated kinase 1B exhibit distinct patterns of
RT   expression and functional properties.";
RL   Biochem. J. 372:881-888(2003).
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 1-533 (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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-273, 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 TYR-273, 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-273, 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 TYR-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).
CC   -!- FUNCTION: Dual-specificity kinase which possesses both serine/
CC       threonine and tyrosine kinase activity. Enhances the
CC       transcriptional activity of TCF1/HNF1A and FOXO1. Inhibits
CC       epithelial cell migration. Mediates colon carcinoma cell survival
CC       in mitogen-poor environments.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Inhibited by RANBP9 (By similarity).
CC   -!- SUBUNIT: Dimer. Interacts with DCOHM, MAP2K3/MKK3 and TCF1/HNF1A.
CC       Part of a complex consisting of RANBP9, RAN, DYRK1B and COPS5 (By
CC       similarity). Interatcs with DCAF7 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=p69;
CC         IsoId=Q9Z188-1; Sequence=Displayed;
CC       Name=2; Synonyms=p65;
CC         IsoId=Q9Z188-2; Sequence=VSP_022955;
CC         Note=Inactive;
CC       Name=3; Synonyms=p75;
CC         IsoId=Q9Z188-3; Sequence=VSP_022954;
CC   -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are broadly expressed.
CC       Isoform 3 seems specific for skeletal muscle (at protein level).
CC   -!- DEVELOPMENTAL STAGE: Isoform 1 is present from 14 dpc. Isoform 3
CC       is present from 18 dpc (at protein level).
CC   -!- PTM: Phosphorylated by MAP kinase. Tyrosine phosphorylation may be
CC       required for dimerization (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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Y18280; CAA77101.2; -; mRNA.
DR   EMBL; AJ252172; CAC20675.1; -; Genomic_DNA.
DR   EMBL; AJ537610; CAD61290.1; -; mRNA.
DR   EMBL; BC019545; AAH19545.1; -; mRNA.
DR   EMBL; AK148342; BAE28495.1; -; mRNA.
DR   IPI; IPI00323385; -.
DR   IPI; IPI00460677; -.
DR   IPI; IPI00761738; -.
DR   PIR; JG0196; JG0196.
DR   RefSeq; NP_001033046.1; NM_001037957.2.
DR   RefSeq; NP_034222.1; NM_010092.1.
DR   UniGene; Mm.57249; -.
DR   ProteinModelPortal; Q9Z188; -.
DR   SMR; Q9Z188; 100-433.
DR   STRING; Q9Z188; -.
DR   PhosphoSite; Q9Z188; -.
DR   PRIDE; Q9Z188; -.
DR   Ensembl; ENSMUST00000002483; ENSMUSP00000002483; ENSMUSG00000002409.
DR   Ensembl; ENSMUST00000085901; ENSMUSP00000083064; ENSMUSG00000002409.
DR   GeneID; 13549; -.
DR   KEGG; mmu:13549; -.
DR   UCSC; uc009fxz.1; mouse.
DR   CTD; 13549; -.
DR   MGI; MGI:1330302; Dyrk1b.
DR   eggNOG; roNOG10471; -.
DR   GeneTree; ENSGT00550000074148; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG051425; -.
DR   InParanoid; Q9Z188; -.
DR   OMA; LVGGPPD; -.
DR   OrthoDB; EOG42NJ05; -.
DR   NextBio; 284162; -.
DR   ArrayExpress; Q9Z188; -.
DR   Bgee; Q9Z188; -.
DR   Genevestigator; Q9Z188; -.
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:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007520; P:myoblast fusion; 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; Alternative splicing; ATP-binding; Kinase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT   CHAIN         1    629       Dual specificity tyrosine-
FT                                phosphorylation-regulated kinase 1B.
FT                                /FTId=PRO_0000085935.
FT   DOMAIN      111    431       Protein kinase.
FT   NP_BIND     117    125       ATP (By similarity).
FT   REGION      480    520       Interaction with RANBP9 (By similarity).
FT   MOTIF        69     86       Bipartite nuclear localization signal
FT                                (Potential).
FT   COMPBIAS    558    561       Poly-Pro.
FT   COMPBIAS    577    584       Poly-Pro.
FT   ACT_SITE    239    239       Proton acceptor (By similarity).
FT   BINDING     140    140       ATP (By similarity).
FT   MOD_RES      57     57       N6-acetyllysine (By similarity).
FT   MOD_RES     271    271       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     273    273       Phosphotyrosine.
FT   VAR_SEQ       1      1       M -> MLAARPPHWGPHRAPAPRGPSAIPDPGLSGGGSRGA
FT                                GCEKAPPGRAPAPGLTPLRPSEPTM (in isoform 3).
FT                                /FTId=VSP_022954.
FT   VAR_SEQ     366    405       Missing (in isoform 2).
FT                                /FTId=VSP_022955.
FT   CONFLICT    459    459       P -> H (in Ref. 4; BAE28495).
FT   CONFLICT    531    531       S -> P (in Ref. 4; BAE28495).
SQ   SEQUENCE   629 AA;  69178 MW;  54FCE6DBD3918D1C CRC64;
     MAVPPGHGPF SGFPGPQEHT QVLPDVRLLP RRLPLAFRDA ASAPLRKLSV DLIKTYKHIN
     EVYYAKKKRR AQQAPPQDSS TKKEKKVLNH GYDDDNHDYI VRSGERWLER YEIDSLIGKG
     SFGQVVKAYD HQTQELVAIK IIKNKKAFLN QAQIELRLLE LMNQHDTEMK YYIVHLKRHF
     MFRNHLCLVF ELLSYNLYDL LRNTHFRGVS LNLTRKLAQQ LCTALLFLAT PELSIIHCDL
     KPENILLCNP KRSAIKIVDF GSSCQLGQRI YQYIQSRFYR SPEVLLGTPY DLAIDMWSLG
     CILVEMHTGE PLFSGSNEVD QMSRIVEVLG IPPAPMLEQA PKARKYFERL PGGGWTLRRT
     KELRKDYQGP GTRRLQEVLG VQTGGPGGRR AGEPGHSPAD YLRFQDLVLR MLEYEPAARI
     SPLGALQHGF FRRTADEATN TGPAGSSAST SPAPLDTCPS SSTASSISSS GGSSGSSNDN
     RAYRYSNRYC GGPGPPITDC EMNSPQVLPS QPLRPWAGGD VPHKTHQAPI SASTLPGTGA
     QLPPLPRCLG RPPSPTSPPP PELMDVSLVG SPPDCSPPPP APAPQHPAAS ALRTRMTGGR
     PPLPPPDDPA TLGPRLGLHG VPQSTAASS
//
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   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   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   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   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.
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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
//
