ID ABR_HUMAN STANDARD; PRT; 859 AA. AC Q12979; Q13693; Q13694; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 30-MAY-2006, entry version 45. DE Active breakpoint cluster region-related protein. GN Name=ABR; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Hippocampus; RX MEDLINE=94086546; PubMed=8262969; RA Tan E.-C., Leung T., Manser E., Lim L.; RT "The human active breakpoint cluster region-related gene encodes a RT brain protein with homology to guanine nucleotide exchange proteins RT and GTPase-activating proteins."; RL J. Biol. Chem. 268:27291-27298(1993). RN [2] RP NUCLEOTIDE SEQUENCE OF 39-859 (ISOFORMS LONG AND SHORT). RC TISSUE=Fibroblast; RX MEDLINE=93352461; PubMed=8349582; RA Heisterkamp N., Kaartinen V., van Soest S., Bokoch G.M., Groffen J.; RT "Human ABR encodes a protein with GAPrac activity and homology to the RT DBL nucleotide exchange factor domain."; RL J. Biol. Chem. 268:16903-16906(1993). RN [3] RP NUCLEOTIDE SEQUENCE OF 436-597. RX MEDLINE=90067847; PubMed=2587217; RA Heisterkamp N., Morris C., Groffen J.; RT "ABR, an active BCR-related gene."; RL Nucleic Acids Res. 17:8821-8831(1989). CC -!- FUNCTION: GTPase-activating protein for RAC and CDC42. Promotes CC the exchange of RAC or CDC42-bound GDP by GTP, thereby activating CC them. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q12979-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q12979-2; Sequence=VSP_001815; CC -!- TISSUE SPECIFICITY: Highly enriched in the brain. Much weaker CC expression in heart, lung and muscle. CC -!- SIMILARITY: Contains 1 C2 domain. CC -!- SIMILARITY: Contains 1 DH (DBL-homology) domain. CC -!- SIMILARITY: Contains 1 PH domain. CC -!- SIMILARITY: Contains 1 Rho-GAP domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U01147; AAC50063.1; -; mRNA. DR EMBL; L19704; AAC37519.1; -; Unassigned_DNA. DR EMBL; L19705; AAC37518.1; ALT_INIT; Unassigned_DNA. DR PIR; A49307; A49307. DR UniGene; Hs.159306; -. DR HSSP; Q98935; 1F7C. DR Ensembl; ENSG00000159842; Homo sapiens. DR HGNC; HGNC:81; ABR. DR MIM; 600365; gene. DR GO; GO:0005096; F:GTPase activator activity; TAS. DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR001331; GDS_CDC24. DR InterPro; IPR001849; PH. DR InterPro; IPR011993; PH_type. DR InterPro; IPR008936; Rho_GAP. DR InterPro; IPR000198; RhoGAP. DR InterPro; IPR000219; RhoGEF. DR Pfam; PF00168; C2; 1. DR Pfam; PF00169; PH; 1. DR Pfam; PF00620; RhoGAP; 1. DR Pfam; PF00621; RhoGEF; 1. DR SMART; SM00239; C2; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00324; RhoGAP; 1. DR SMART; SM00325; RhoGEF; 1. DR PROSITE; PS50004; C2_DOMAIN; 1. DR PROSITE; PS00741; DH_1; 1. DR PROSITE; PS50010; DH_2; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS50238; RHOGAP; 1. KW Alternative splicing; Guanine-nucleotide releasing factor. FT CHAIN 1 859 Active breakpoint cluster region-related FT protein. FT /FTId=PRO_0000080902. FT DOMAIN 91 284 DH. FT DOMAIN 301 459 PH. FT DOMAIN 463 595 C2. FT DOMAIN 647 845 Rho-GAP. FT COMPBIAS 417 420 Poly-Leu. FT VAR_SEQ 1 82 MEPLSHRGLPRLSWIDTLYSNFSYGTDEYDGEGNEEQKGPP FT EGSETMPYIDESPTMSPQLSARSQGRGDGVSPTPPEGLAPG FT -> MEEEEEAIGLLDKVLEDEDVFLLEECELGTPTSPGSGS FT PFLVAVK (in isoform Short). FT /FTId=VSP_001815. FT CONFLICT 67 67 R -> G (in Ref. 2). FT CONFLICT 657 660 RSKV -> VQGA (in Ref. 2). FT CONFLICT 761 761 L -> V (in Ref. 2). SQ SEQUENCE 859 AA; 97697 MW; 9FD50CD54FA99483 CRC64; MEPLSHRGLP RLSWIDTLYS NFSYGTDEYD GEGNEEQKGP PEGSETMPYI DESPTMSPQL SARSQGRGDG VSPTPPEGLA PGVEAGKGLE MRKLVLSGFL ASEEIYINQL EALLLPMKPL KATATTSQPV LTIQQIETIF YKIQDIYEIH KEFYDNLCPK VQQWDSQVTM GHLFQKLASQ LGVYKAFVDN YKVALETAEK CSQSNNQFQK ISEELKVKGP KDSKDSHTSV TMEALLYKPI DRVTRSTLVL HDLLKHTPVD HPDYPLLQDA LRISQNFLSS INEDIDPRRT AVTTPKGETR QLVKDGFLVE VSESSRKLRH VFLFTDVLLC AKLKKTSAGK HQQYDCKWYI PLADLVFPSP EESEASPQVH PFPDHELEDM KMKISALKSE IQKEKANKGQ SRAIERLKKK MFENEFLLLL NSPTIPFRIH NRNGKSYLFL LSSDYERSEW REAIQKLQKK DLQAFVLSSV ELQVLTGSCF KLRTVHNIPV TSNKDDDESP GLYGFLHVIV HSAKGFKQSA NLYCTLEVDS FGYFVSKAKT RVFRDTAEPK WDEEFEIELE GSQSLRILCY EKCYDKTKVN KDNNEIVDKI MGKGQIQLDP QTVETKNWHT DVIEMNGIKV EFSMKFTSRD MSLKRTPSKK QTGVFGVKIS VVTKRERSKV PYIVRQCVEE VEKRGIEEVG IYRISGVATD IQALKAVFDA NNKDILLMLS DMDINAIAGT LKLYFRELPE PLLTDRLYPA FMEGIALSDP AAKENCMMHL LRSLPDPNLI TFLFLLEHLK RVAEKEPINK MSLHNLATVF GPTLLRPSEV ESKAHLTSAA DIWSHDVMAQ VQVLLYYLQH PPISFAELKR NTLYFSTDV // ID BAIP3_HUMAN STANDARD; PRT; 1187 AA. AC O94812; O94839; Q76N05; Q96RZ3; Q9UJK1; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 31-AUG-2004, sequence version 2. DT 30-MAY-2006, entry version 34. DE BAI1-associated protein 3 (BAP3). GN Name=BAIAP3; Synonyms=KIAA0734; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE, INTERACTION WITH BAI1, AND TISSUE SPECIFICITY. RX MEDLINE=99009239; PubMed=9790924; DOI=10.1006/bbrc.1998.9408; RA Shiratsuchi T., Oda K., Nishimori H., Suzuki M., Takahashi E., RA Tokino T., Nakamura Y.; RT "Cloning and characterization of BAP3 (BAI-associated protein 3), a C2 RT domain-containing protein that interacts with BAI1."; RL Biochem. Biophys. Res. Commun. 251:158-165(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX MEDLINE=99087487; PubMed=9872452; DOI=10.1093/dnares/5.5.277; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XI. RT The complete sequences of 100 new cDNA clones from brain which code RT for large proteins in vitro."; RL DNA Res. 5:277-286(1998). RN [3] RP SEQUENCE REVISION. RX MEDLINE=22158633; PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21096910; PubMed=11157797; DOI=10.1093/hmg/10.4.339; RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., RA Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., RA Higgs D.R.; RT "Sequence, structure and pathology of the fully annotated terminal 2 RT Mb of the short arm of human chromosome 16."; RL Hum. Mol. Genet. 10:339-352(2001). RN [5] RP NUCLEOTIDE SEQUENCE OF 32-1187. RA Frankland J.; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. CC -!- SUBUNIT: Interacts with BAI1. CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain. CC -!- SIMILARITY: Contains 2 C2 domains. CC -!- SIMILARITY: Contains 1 MH (MUNC13 homology) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB017111; BAA34710.1; -; Genomic_DNA. DR EMBL; AB018277; BAA34454.2; ALT_INIT; mRNA. DR EMBL; AE006467; AAK61275.1; -; Genomic_DNA. DR EMBL; AL031709; CAB56182.1; ALT_INIT; Genomic_DNA. DR PIR; JE0347; JE0347. DR UniGene; Hs.458427; -. DR HSSP; P04410; 1A25. DR Ensembl; ENSG00000007516; Homo sapiens. DR HGNC; HGNC:948; BAIAP3. DR MIM; 604009; gene. DR GO; GO:0008022; F:protein C-terminus binding; TAS. DR GO; GO:0007269; P:neurotransmitter secretion; TAS. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR010439; DUF1041. DR Pfam; PF00168; C2; 2. DR Pfam; PF06292; DUF1041; 1. DR PRINTS; PR00360; C2DOMAIN. DR SMART; SM00239; C2; 2. DR PROSITE; PS50004; C2_DOMAIN; 2. KW Repeat. FT CHAIN 1 1187 BAI1-associated protein 3. FT /FTId=PRO_0000064819. FT DOMAIN 182 317 C2 1. FT DOMAIN 561 642 MH. FT DOMAIN 1012 1119 C2 2. FT CONFLICT 582 582 D -> A (in Ref. 1). SQ SEQUENCE 1187 AA; 131901 MW; E38EF36E91BE7DEB CRC64; MRPRGAAFAA GPPGDLHLGT AIGFAGAIWR SRSPAMSTLL DIKSSVLRQV QVCPSFRRRT EQDPGSASAD PQEPATGAWK PGDGVEFFAH MRLMLKKGEG RQGLPCLEVP LRSGSPAPPE PVDPSLGLRA LAPEEVEMLY EEALYTVLYR AGTMGPDQVD DEEALLSYLQ QVFGTSLEEH TEAIERVRKA KAPTYALKVS VMRAKNLLAK DPNGFSDPYC MLGILPASDA TREPRAQKEQ RFGFRKGSKR GGPLPAKCIQ VTEVKSSTLN PVWKEHFLFE IEDVSTDQLH LDIWDHDDDV SLVEACRKLN EVIGLKGMGR YFKQIVKSAR ANGTAGPTED HTDDFLGCLN IPVREVPVAG VDRWFKLEPR SSASRVQGHC HLVLKLITTQ RDTAMSQRGR SGFLSHLLLL SHLLRLEHSA EEPNSSSWRG ELSTPAATIL CLHGAQSNLS PLQLAVLHWQ VSSRHHQTCT LDYSYLLGLL EDMQAHWEEA PSLPQEQEES LADSLSAFSE FGLQLLRQLR DYFPATNSTA VHRLELLLKC LGKLQLFQPS FEICPFESEL NMDIAAALKR GNREWYDRIL NDKSPREQPG PQRLPGLVVL ADAVYDDLQF CYSVYASLFH SILNVDVFTL TFRQLERLVA EEAWVLTEEL SPKMTLEVAS GLFELYLTLA DLQRFWDSIP GRDSRSLALA GIHAPFLPAV KLWFQVLRDQ AKWRLQGAVD MDTLEPVDAS SRHSSSAATA GLCLSHIQEL WVRLAWPDPA QAQGLGTQLG QDVCEATLFY TELLRKKVDT QPGAAGEAVS EALCVVLNNV ELVRKAAGQA LKGLAWPEGA TGPEGVLPRP LLSCTQALDD DLQREAHTVT AHLTSKMVGD IRKYVQHISL SPDSIQNDEA VAPLMKYLDE KLALLNASLV KGNLSRVLEA LWELLLQAIL QALGANRDVS ADFYSRFHFT LEALVSFFHA EGQGLPLESL RDGSYKRLKE ELRLHKCSTR ECIEQFYLDK LKQRTLEQNR FGRLSVRCHY EAAEQRLAVE VLHAADLLPL DANGLSDPFV IVELGPPHLF PLVRSQRTQV KTRTLHPVYD ELFYFSVPAE ACRRRAACVL FTVMDHDWLS TNDFAGEAAL GLGGVTGVAR PQVGGGARAG QPVTLHLCRP RAQVRSALRR LEGRTSKEAQ EFVKKLKELE KCMEADP // ID BAIP3_MOUSE STANDARD; PRT; 1134 AA. AC Q80TT2; Q6RUT4; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 31-AUG-2004, sequence version 2. DT 30-MAY-2006, entry version 22. DE BAI1-associated protein 3 (BAP3). GN Name=Baiap3; Synonyms=Gm937, Kiaa0734; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. 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 [GENOMIC DNA]. 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. CC -!- SUBUNIT: Interacts with BAI1 (By similarity). CC -!- SIMILARITY: Contains 2 C2 domains. CC -!- SIMILARITY: Contains 1 MH (MUNC13 homology) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK122358; BAC65640.1; ALT_INIT; Other_RNA. DR EMBL; AY491413; AAS21653.1; -; Genomic_DNA. DR UniGene; Mm.328859; -. DR Ensembl; ENSMUSG00000047507; Mus musculus. DR MGI; MGI:2685783; Baiap3. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR010439; DUF1041. DR Pfam; PF00168; C2; 2. DR Pfam; PF06292; DUF1041; 1. DR PRINTS; PR00360; C2DOMAIN. DR SMART; SM00239; C2; 2. DR PROSITE; PS50004; C2_DOMAIN; 2. KW Repeat. FT CHAIN 1 1134 BAI1-associated protein 3. FT /FTId=PRO_0000064820. FT DOMAIN 145 280 C2 1. FT DOMAIN 524 606 MH. FT DOMAIN 959 1066 C2 2. FT CONFLICT 178 179 Missing (in Ref. 2). FT CONFLICT 182 182 Y -> D (in Ref. 2). FT CONFLICT 200 200 Q -> R (in Ref. 2). FT CONFLICT 584 584 R -> G (in Ref. 2). SQ SEQUENCE 1134 AA; 127191 MW; 62EC9A52BF441EC9 CRC64; MSTLLDIKSS VLRQVQVCPS FRRKTEQEPE VTNSQEPPTG AWKPGDGVEF FAHMRLILKK GDGRQGLPCP EVLLRSGSPA PAEPVDPNRG LRTLTQEEVE MLYEEALYTV LHRAGTMGPD QVDDEEVLLS YLQQVFGTSS EEHMEAIMRV KKAKAPTYAL KVSVMRAKNL LAKDPNGFSD PYCMLGILPA SSAPQESSGQ KEQRFGFRKG SKRSSPLPAK CIQVTEVKNS TLNPVWKEHF LFEIDDVNTD QLHLDIWDHD DDVSLAEACR KLNEVIGLKG MTRYFKQIVK SARANGTAGP TEDHTDDFLG CLNIPIREVP VAGADRWFKL EPRSSASRVQ GDCHLVLKLI TTQRDTVMNQ RGRSGFLSYL LLLSRVLRFE HRVEEPNSSS WRGELSGPGT TVLCLHGAQS NLSPLQLAVL HWQVSSRHHQ TRTLDYGYLL GLLEDVQAHW EEAASLPQEQ EESLADSFSA FSEFGLRLLR QLRDYFPATN STAVYRLELL LKCLEKLQLF QPAFEICPFE TELSMDIAAA LKRGNREWYD QLLNTKSPRE QPGPQRLAGL VELADIIYED LQLCYGVYAS LFHRQVAEEA WVLTEELSPK MNLEVASGLF ELYLTLADTQ RFWSCIPGRE SRSLALAGIH TPFLPAVKLW LQVLRDQAKW RLQGAVDVDT LEPVDAASKH SSSAATASLC LSHIQELWVR LAWPDPSQAQ GLGTQLSQDM CEASLFYTEL LRKKVDTQPG AAGEAVSEQL CVVLNNVELV RRASGQALRG LAWSEGASGL EGVLPRPLLS CIQALDEDLH REAHTVTAHL TSKMVADIRK YIQHISLSPD SIQNDEAVAP LLKYLDEKLA LLNDALVKEN LNRVLEALWE LLLQAILQAL SANRDVSADF YGRFHFTLEA LVSFFHAEGQ GLPLENLRDG SYKRLQEELR LHKCSTRECI EQFYLDKLKQ RSLEQNRFGR LTVRCHYEAA EQRLAVEVLH AADLLPLDAN GLSDPFVIVE LGPPHLFPLV RSQRTQVKAR TLHPVYDELF HFSVPAEACR RRGACVLFTV MDHDWLSTND FAGEAALGLG GISGIARPHV GGGMRPGQPI TLHLRRPRAQ VRSALRMLEG RTSREAQEFV KKLKELEKCM EADL // ID BCR_HUMAN STANDARD; PRT; 1271 AA. AC P11274; P78501; Q12842; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 30-MAY-2006, entry version 76. DE Breakpoint cluster region protein (EC 2.7.11.1) (NY-REN-26 antigen). GN Name=BCR; Synonyms=BCR1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=88217290; PubMed=3285291; RA Lifshitz B., Fainstein E., Marcelle C., Shtivelman E., Amson R., RA Gale R.P., Canaani E.; RT "bcr genes and transcripts."; RL Oncogene 2:113-117(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=95394474; PubMed=7665185; RA Chissoe S.L., Bodenteich A., Wang Y.-F., Wang Y.-P., Burian D., RA Clifton S.W., Crabtree J., Freeman A., Iyer K., Jian L., Ma Y., RA McLaury H.-J., Pan H.-Q., Sarhan O.H., Toth S., Wang Z., Zhang G., RA Heisterkamp N., Groffen J., Roe B.A.; RT "Sequence and analysis of the human ABL gene, the BCR gene, and RT regions involved in the Philadelphia chromosomal translocation."; RL Genomics 27:67-82(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-872. RX MEDLINE=87218455; PubMed=3107980; RA Hariharan I.K., Adams J.M.; RT "cDNA sequence for human bcr, the gene that translocates to the abl RT oncogene in chronic myeloid leukaemia."; RL EMBO J. 6:115-119(1987). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-693. RX MEDLINE=87092329; PubMed=3540951; RA Mes-Masson A.M., McLaughlin J., Daley G.Q., Paskind M., Witte O.N.; RT "Overlapping cDNA clones define the complete coding region for the RT P210c-abl gene product associated with chronic myelogenous leukemia RT cells containing the Philadelphia chromosome."; RL Proc. Natl. Acad. Sci. U.S.A. 83:9768-9772(1986). RN [5] RP ERRATUM, AND SEQUENCE REVISION. RA Mes-Masson A.M., McLaughlin J., Daley G.Q., Paskind M., Witte O.N.; RL Proc. Natl. Acad. Sci. U.S.A. 84:2507-2507(1987). RN [6] RP NUCLEOTIDE SEQUENCE OF 683-1271. RX MEDLINE=85240564; PubMed=2989703; DOI=10.1038/315758a0; RA Heisterkamp N., Stam K., Groffen J., de Klein A., Grosveld G.; RT "Structural organization of the bcr gene and its role in the Ph' RT translocation."; RL Nature 315:758-761(1985). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46 AND 275-426. RX MEDLINE=91088292; PubMed=2263470; RA Zhu Q.S., Heisterkamp N., Groffen J.; RT "Unique organization of the human BCR gene promoter."; RL Nucleic Acids Res. 18:7119-7125(1990). RN [8] RP NUCLEOTIDE SEQUENCE OF 56-426. RX MEDLINE=88065859; PubMed=2825022; DOI=10.1038/330386a0; RA Fainstein E., Marcelle C., Rosner A., Canaani E., Gale R.P., RA Dreazen O., Smith S.D., Croce C.M.; RT "A new fused transcript in Philadelphia chromosome positive acute RT lymphocytic leukaemia."; RL Nature 330:386-388(1987). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 362-438, AND ALTERNATIVE SPLICING. RX PubMed=2915904; RA Romero P., Beran M., Shtalrid M., Andersson B., Talpaz M., Blick M.; RT "Alternative 5' end of the bcr-abl transcript in chronic myelogenous RT leukemia."; RL Oncogene 4:93-98(1989). RN [10] RP NUCLEOTIDE SEQUENCE OF 670-842. RX MEDLINE=90167280; PubMed=2407300; RA Selleri L., von Lindern M., Hermans A., Meijer D., Torelli G., RA Grosveld G.; RT "Chronic myeloid leukemia may be associated with several bcr-abl RT transcripts including the acute lymphoid leukemia-type 7 kb RT transcript."; RL Blood 75:1146-1153(1990). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-4. RX MEDLINE=91172169; PubMed=1900918; RA Shah N.P., Witte O.N., Denny C.T.; RT "Characterization of the BCR promoter in Philadelphia chromosome- RT positive and -negative cell lines."; RL Mol. Cell. Biol. 11:1854-1860(1991). RN [12] RP FUNCTION. RX MEDLINE=91238969; PubMed=1903516; DOI=10.1038/351400a0; RA Diekmann D., Brill S., Garrett M.D., Totty N., Hsuan J., Monfries C., RA Hall C., Lim L., Hall A.; RT "Bcr encodes a GTPase-activating protein for p21rac."; RL Nature 351:400-402(1991). RN [13] RP INTERACTION WITH ABL1 SH2-DOMAIN. RX MEDLINE=91300547; PubMed=1712671; DOI=10.1016/0092-8674(91)90148-R; RA Pendergast A.M., Muller A.J., Havlik M.H., Maru Y., Witte O.N.; RT "BCR sequences essential for transformation by the BCR-ABL oncogene RT bind to the ABL SH2 regulatory domain in a non-phosphotyrosine- RT dependent manner."; RL Cell 66:161-171(1991). RN [14] RP KINASE ACTIVITY. RX MEDLINE=92034969; PubMed=1657398; RA Maru Y., Witte O.N.; RT "The BCR gene encodes a novel serine/threonine kinase activity within RT a single exon."; RL Cell 67:459-468(1991). RN [15] RP IDENTIFICATION AS A RENAL CANCER ANTIGEN. RC TISSUE=Renal cell carcinoma; RX MEDLINE=99438124; PubMed=10508479; RX DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5; RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., RA Old L.J.; RT "Antigens recognized by autologous antibody in patients with renal- RT cell carcinoma."; RL Int. J. Cancer 83:456-464(1999). RN [16] RP PHOSPHORYLATION AT TYR-177; THR-310; SER-459; SER-463; TYR-591 AND RP TYR-644. 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 [17] RP PHOSPHORYLATION AT SER-1264, AND MASS SPECTROMETRY. RX PubMed=15144186; DOI=10.1021/ac035352d; RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., RA Peters E.C.; RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites RT from human T cells using immobilized metal affinity chromatography and RT tandem mass spectrometry."; RL Anal. Chem. 76:2763-2772(2004). RN [18] RP INTERACTION WITH PDZK1, AND MUTAGENESIS OF 1269-THR--GLU-1271 AND RP VAL-1271. RX PubMed=15494376; DOI=10.1242/jcs.01472; RA Malmberg E.K., Andersson C.X., Gentzsch M., Chen J.H., Mengos A., RA Cui L., Hansson G.C., Riordan J.R.; RT "Bcr (breakpoint cluster region) protein binds to PDZ-domains of RT scaffold protein PDZK1 and vesicle coat protein Mint3."; RL J. Cell Sci. 117:5535-5541(2004). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 3-72, AND RP HOMOTETRAMERIZATION. RX MEDLINE=21671741; PubMed=11780146; DOI=10.1038/nsb747; RA Zhao X., Ghaffari S., Lodish H., Malashkevich V.N., Kim P.S.; RT "Structure of the Bcr-Abl oncoprotein oligomerization domain."; RL Nat. Struct. Biol. 9:117-120(2002). CC -!- FUNCTION: GTPase-activating protein for RAC1 and CDC42. Promotes CC the exchange of RAC or CDC42-bound GDP by GTP, thereby activating CC them. Displays serine/threonine kinase activity. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBUNIT: Homotetramer. Interacts with PDZK1. CC -!- DOMAIN: The region involved in binding to ABL1 SH2-domain is rich CC in serine residues and needs to be Ser/Thr phosphorylated prior to CC SH2 binding. This region is essential for the activation of the CC ABL1 tyrosine kinase and transforming potential of the chimeric CC BCR-ABL oncogene. CC -!- PTM: Autophosphorylated. CC -!- DISEASE: A chromosomal aberration involving BCR is a cause of CC chronic myeloid leukemia (CML) [MIM:608232]. Translocation CC t(9;22)(q34;q11) with ABL1. The translocation produces a BCR-ABL CC found also in acute myeloid leukemia (AML) and acute lymphoblastic CC leukemia (ALL). CC -!- SIMILARITY: Contains 1 C2 domain. CC -!- SIMILARITY: Contains 1 DH (DBL-homology) domain. CC -!- SIMILARITY: Contains 1 PH domain. CC -!- SIMILARITY: Contains 1 Rho-GAP domain. CC -!- WEB RESOURCE: NAME=Atlas Genet. Cytogenet. Oncol. Haematol.; CC URL="http://www.infobiogen.fr/services/chromcancer/Genes/BCR.html". CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y00661; CAA68676.1; -; mRNA. DR EMBL; U07000; AAB60388.1; -; Genomic_DNA. DR EMBL; X02596; CAA26441.1; -; mRNA. DR EMBL; M15025; AAA35594.1; -; Genomic_DNA. DR EMBL; X52828; CAA37010.1; -; Genomic_DNA. DR EMBL; X52829; CAA37011.1; -; Genomic_DNA. DR EMBL; X14676; CAA32806.1; -; mRNA. DR EMBL; M64437; -; NOT_ANNOTATED_CDS; mRNA. DR PIR; A91064; TVHUBR. DR UniGene; Hs.517461; -. DR UniGene; Hs.616387; -. DR PDB; 1K1F; X-ray; A/B/C/D/E/F/G/H=1-72. DR Ensembl; ENSG00000186716; Homo sapiens. DR HGNC; HGNC:1014; BCR. DR MIM; 151410; gene. DR MIM; 608232; phenotype. DR LinkHub; P11274; -. DR GO; GO:0005096; F:GTPase activator activity; TAS. DR GO; GO:0004674; F:protein serine/threonine kinase activity; TAS. DR GO; GO:0006468; P:protein amino acid phosphorylation; TAS. DR GO; GO:0007165; P:signal transduction; TAS. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR001331; GDS_CDC24. DR InterPro; IPR001849; PH. DR InterPro; IPR008936; Rho_GAP. DR InterPro; IPR000198; RhoGAP. DR InterPro; IPR000219; RhoGEF. DR Pfam; PF00168; C2; 1. DR Pfam; PF00620; RhoGAP; 1. DR Pfam; PF00621; RhoGEF; 1. DR SMART; SM00239; C2; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00324; RhoGAP; 1. DR SMART; SM00325; RhoGEF; 1. DR PROSITE; PS50004; C2_DOMAIN; 1. DR PROSITE; PS00741; DH_1; 1. DR PROSITE; PS50010; DH_2; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS50238; RHOGAP; 1. KW 3D-structure; Chromosomal translocation; KW Guanine-nucleotide releasing factor; Kinase; Phosphorylation; KW Proto-oncogene; Serine/threonine-protein kinase; Transferase. FT CHAIN 1 1271 Breakpoint cluster region protein. FT /FTId=PRO_0000080933. FT DOMAIN 498 691 DH. FT DOMAIN 708 866 PH. FT DOMAIN 870 1002 C2. FT DOMAIN 1054 1248 Rho-GAP. FT REGION 1 426 Kinase. FT REGION 197 385 Binding to ABL SH2-domain. FT COMPBIAS 824 827 Poly-Leu. FT SITE 426 427 Breakpoint for translocation to form BCR- FT ABL oncogene. FT MOD_RES 177 177 Phosphotyrosine. FT MOD_RES 310 310 Phosphothreonine. FT MOD_RES 459 459 Phosphoserine. FT MOD_RES 463 463 Phosphoserine. FT MOD_RES 591 591 Phosphotyrosine. FT MOD_RES 644 644 Phosphotyrosine. FT MOD_RES 1264 1264 Phosphoserine. FT MUTAGEN 1269 1271 Missing: Abolishes interaction with FT PDZK1. FT MUTAGEN 1271 1271 V->A: Reduces interaction with PDZK1. FT CONFLICT 287 287 M -> I (in Ref. 1). FT CONFLICT 418 418 G -> D (in Ref. 1). FT CONFLICT 483 483 E -> K (in Ref. 1). FT CONFLICT 560 560 F -> S (in Ref. 1). FT CONFLICT 690 690 E -> D (in Ref. 10). FT CONFLICT 733 733 E -> D (in Ref. 1, 2 and 10). FT CONFLICT 796 796 S -> N (in Ref. 2). FT CONFLICT 961 1004 Missing (in Ref. 1). FT HELIX 4 14 FT TURN 16 17 FT STRAND 18 18 FT STRAND 26 27 FT HELIX 28 64 FT TURN 65 66 SQ SEQUENCE 1271 AA; 142806 MW; A59F76B6F1AF3236 CRC64; MVDPVGFAEA WKAQFPDSEP PRMELRSVGD IEQELERCKA SIRRLEQEVN QERFRMIYLQ TLLAKEKKSY DRQRWGFRRA AQAPDGASEP RASASRPQPA PADGADPPPA EEPEARPDGE GSPGKARPGT ARRPGAAASG ERDDRGPPAS VAALRSNFER IRKGHGQPGA DAEKPFYVNV EFHHERGLVK VNDKEVSDRI SSLGSQAMQM ERKKSQHGAG SSVGDASRPP YRGRSSESSC GVDGDYEDAE LNPRFLKDNL IDANGGSRPP WPPLEYQPYQ SIYVGGMMEG EGKGPLLRSQ STSEQEKRLT WPRRSYSPRS FEDCGGGYTP DCSSNENLTS SEEDFSSGQS SRVSPSPTTY RMFRDKSRSP SQNSQQSFDS SSPPTPQCHK RHRHCPVVVS EATIVGVRKT GQIWPNDGEG AFHGDADGSF GTPPGYGCAA DRAEEQRRHQ DGLPYIDDSP SSSPHLSSKG RGSRDALVSG ALESTKASEL DLEKGLEMRK WVLSGILASE ETYLSHLEAL LLPMKPLKAA ATTSQPVLTS QQIETIFFKV PELYEIHKEF YDGLFPRVQQ WSHQQRVGDL FQKLASQLGV YRAFVDNYGV AMEMAEKCCQ ANAQFAEISE NLRARSNKDA KDPTTKNSLE TLLYKPVDRV TRSTLVLHDL LKHTPASHPD HPLLQDALRI SQNFLSSINE EITPRRQSMT VKKGEHRQLL KDSFMVELVE GARKLRHVFL FTELLLCTKL KKQSGGKTQQ YDCKWYIPLT DLSFQMVDEL EAVPNIPLVP DEELDALKIK ISQIKSDIQR EKRANKGSKA TERLKKKLSE QESLLLLMSP SMAFRVHSRN GKSYTFLISS DYERAEWREN IREQQKKCFR SFSLTSVELQ MLTNSCVKLQ TVHSIPLTIN KEDDESPGLY GFLNVIVHSA TGFKQSSNLY CTLEVDSFGY FVNKAKTRVY RDTAEPNWNE EFEIELEGSQ TLRILCYEKC YNKTKIPKED GESTDRLMGK GQVQLDPQAL QDRDWQRTVI AMNGIEVKLS VKFNSREFSL KRMPSRKQTG VFGVKIAVVT KRERSKVPYI VRQCVEEIER RGMEEVGIYR VSGVATDIQA LKAAFDVNNK DVSVMMSEMD VNAIAGTLKL YFRELPEPLF TDEFYPNFAE GIALSDPVAK ESCMLNLLLS LPEANLLTFL FLLDHLKRVA EKEAVNKMSL HNLATVFGPT LLRPSEKESK LPANPSQPIT MTDSWSLEVM SQVQVLLYFL QLEAIPAPDS KRQSILFSTE V // ID BUD2_YEAST STANDARD; PRT; 1104 AA. AC P33314; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 2. DT 30-MAY-2006, entry version 49. DE Inhibitory regulator protein BUD2/CLA2. GN Name=BUD2; Synonyms=CLA2, ERC25; OrderedLocusNames=YKL092C; GN ORFNames=YKL424; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=94085403; PubMed=8262070; RA Cvrckova F., Nasmyth K.; RT "Yeast G1 cyclins CLN1 and CLN2 and a GAP-like protein have a role in RT bud formation."; RL EMBO J. 12:5277-5286(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=93382538; PubMed=8371782; DOI=10.1038/365269a0; RA Park H.-O., Chant J., Herskowitz I.; RT "BUD2 encodes a GTPase-activating protein for Bud1/Rsr1 necessary for RT proper bud-site selection in yeast."; RL Nature 365:269-274(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S288c / FY1679; RX MEDLINE=94255012; PubMed=8196765; DOI=10.1038/369371a0; RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., RA Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A., RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., RA Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., RA Zimmermann J., Haasemann M., Becker I., Mewes H.-W.; RT "Complete DNA sequence of yeast chromosome XI."; RL Nature 369:371-378(1994). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 237-1104. RX MEDLINE=94262329; PubMed=8203166; RA James C.M., Gent M.E., Oliver S.G.; RT "Sequence analysis of a 3.5 Kb EcoRI fragment from the left arm of RT Saccharomyces cerevisiae chromosome XI reveals the location of the RT MBR1 gene and a sequence related to a GTPase-activating protein."; RL Yeast 10:257-264(1994). RN [5] RP LEVEL OF PROTEIN EXPRESSION. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). CC -!- FUNCTION: Stimulates the GTPase activity of BUD1/RSR1. CC Participates in the regulation of bud-site selection. CC -!- MISCELLANEOUS: Present with 1230 molecules/cell. CC -!- SIMILARITY: Contains 1 C2 domain. CC -!- SIMILARITY: Contains 1 Ras-GAP domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X74130; CAA52228.1; -; Genomic_DNA. DR EMBL; L19162; AAA34461.1; -; Genomic_DNA. DR EMBL; X75561; CAA53241.1; -; Genomic_DNA. DR EMBL; Z28092; CAA81930.1; -; Genomic_DNA. DR PIR; S36773; S36773. DR IntAct; P33314; -. DR GermOnline; 139848; -. DR Ensembl; YKL092C; Saccharomyces cerevisiae. DR GenomeReviews; Y13137_GR; YKL092C. DR SGD; S000001575; BUD2. DR BioCyc; SCER-S28-01:SCER-S28-01-003569-MONOMER; -. DR LinkHub; P33314; -. DR GO; GO:0005622; C:intracellular; TAS. DR GO; GO:0042802; F:identical protein binding; IPI. DR GO; GO:0005099; F:Ras GTPase activator activity; TAS. DR GO; GO:0004871; F:signal transducer activity; TAS. DR GO; GO:0007120; P:axial bud site selection; TAS. DR GO; GO:0007121; P:bipolar bud site selection; TAS. DR GO; GO:0030447; P:filamentous growth; IMP. DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS. DR InterPro; IPR008999; Actin_crosslink. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR001936; RasGAP. DR InterPro; IPR008936; Rho_GAP. DR Pfam; PF00168; C2; 1. DR Pfam; PF00616; RasGAP; 1. DR SMART; SM00239; C2; 1. DR SMART; SM00323; RasGAP; 1. DR PROSITE; PS50004; C2_DOMAIN; 1. DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1. DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1. KW Complete proteome; GTPase activation. FT CHAIN 1 1104 Inhibitory regulator protein BUD2/CLA2. FT /FTId=PRO_0000056656. FT DOMAIN 322 425 C2. FT DOMAIN 505 721 Ras-GAP. FT COMPBIAS 496 499 Poly-Ser. FT COMPBIAS 1096 1099 Poly-Lys. FT CONFLICT 437 437 N -> Y (in Ref. 1). SQ SEQUENCE 1104 AA; 126663 MW; 451AFC3A78384760 CRC64; MSSNNEPAQS RTSYFKLNEF LSNVKHYKNT FKGEIQWCNN LSLNDWKTHY LQITSTGALT HSIDELTADS TNIQPIIKHL QQCRIEIIKD KHSSFKDINA NCNFIIQVNT SGKDNKVYLR VKSWSDFKKL LTCLIWWSSM KTNGIFNKFQ VSRPLEFKSK KMAKPESLLV YKLNVFGPIV KNIVLPPATN ILESPDIINN DDNSVGWFSA MGVLKSNGML DLLLQSDGSL IYSLNISQLL RSEIRILDSS VLQSENSLFL GELPLLRSQL GLEKFRIENI ASAATNSSDI SQEIIVEFPL RIDLEDCFIA LQSFARSEYL SITGSDKSND MKISNSFKIS ILEANFQSIN LNDKNNTPWS IFTDITAWGH TWARTSMVSN SSNPFWREEF QFNELLRLTN SYLEIKQLFH DLNNKKRLRL IGKIKITQEI INDTRYNKET RLPIMDVDNK NFQIGTICIK ISSNLNFILP STNFVKLEKL LMNANLSMVS NLIYKSSSSM ENDNKLTQTS IIFLDIFQSL SRIEEWFHVL IDKELAKIDG TVSRINQKNL DSKHVFNSLF RGNSILTKSI EQYFFRVGNE YLSKALSAIL KEIIESNKSC ELDPARVKEK DEVKKRKIIA DNYKRLYSWV TKIWKRLYAT SNDLPIEIRN VLKIFRQKLE IICIDDTLQI ILNGISGLLF LRFFCPVILN PKLFKYVSQN LNETARRNLT LISKVLLNLS TLTQFANKEP WLMKMNNFID KRHNDLLDYI DKMTQKKLDF NSKILNLSST ISRPKLAIEQ TMLDDLPQIP YLLDKNLRET EFVNLIVNFS QEDMTKMEKY NHMDNGGKGE LIEEEGLLSG SSLNLSVDKK DLDSPIEVKP EIGELEFEKI TENNTEIFGD DLMNLLKSDD VGSRSRDLDN GANSGIKFNS IIPKAEEEKH AMKELEQESC LLYNRINHIR KRLSGYECAS STLFEDKKYS ISLSHKIFYE EIKEGKEIVL KLLNKPTNEN SSARLQKFFT KGVSSKSNNT VGDSYCKFLT IDVSDENPKS SNKTSVHGTS SENGAKDDYL TLPNSQGKGN LGNRFSPTKL SRIMRKPPNA DVPKEQNSRK LTRWFKKKKE TGGS // ID CPNE1_HUMAN STANDARD; PRT; 537 AA. AC Q99829; Q6IBL3; Q9H243; Q9NTZ7; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 30-MAY-2006, entry version 53. DE Copine-1 (Copine I). GN Name=CPNE1; Synonyms=CPN1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=98104118; PubMed=9430674; DOI=10.1074/jbc.273.3.1393; RA Creutz C.E., Tomsig J.L., Snyder S.L., Gautier M.C., Skouri F., RA Beisson J., Cohen J.; RT "The copines, a novel class of C2 domain-containing, calcium- RT dependent, phospholipid-binding proteins conserved from Paramecium to RT humans."; RL J. Biol. Chem. 273:1393-1402(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21638749; PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 332-537. RA Jeon J., Sohn U.; RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: May function in membrane trafficking. Exhibits calcium- CC dependent phospholipid binding properties. CC -!- SIMILARITY: Belongs to the copine family. CC -!- SIMILARITY: Contains 2 C2 domains. CC -!- SIMILARITY: Contains 1 VWFA domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U83246; AAC15920.1; -; mRNA. DR EMBL; CR456790; CAG33071.1; -; mRNA. DR EMBL; AL109827; CAB87610.2; -; Genomic_DNA. DR EMBL; BC001142; AAH01142.1; -; mRNA. DR EMBL; AF314092; AAG49297.1; -; mRNA. DR UniGene; Hs.246413; -. DR Ensembl; ENSG00000125976; Homo sapiens. DR H-InvDB; HIX0019365; -. DR HGNC; HGNC:2314; CPNE1. DR MIM; 604205; gene. DR GO; GO:0005544; F:calcium-dependent phospholipid binding; TAS. DR GO; GO:0001786; F:phosphatidylserine binding; IDA. DR GO; GO:0005215; F:transporter activity; TAS. DR GO; GO:0006629; P:lipid metabolism; TAS. DR GO; GO:0016192; P:vesicle-mediated transport; TAS. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR010734; Copine. DR InterPro; IPR002035; VWF_A. DR Pfam; PF00168; C2; 2. DR Pfam; PF07002; Copine; 1. DR SMART; SM00239; C2; 2. DR SMART; SM00327; VWA; 1. DR PROSITE; PS50004; C2_DOMAIN; 1. DR PROSITE; PS50234; VWFA; FALSE_NEG. KW Polymorphism; Repeat. FT CHAIN 1 537 Copine-1. FT /FTId=PRO_0000144834. FT DOMAIN 1 98 C2 1. FT DOMAIN 144 228 C2 2. FT DOMAIN 285 505 VWFA. FT VARIANT 211 211 Q -> R (in dbSNP:6579255). FT /FTId=VAR_024423. FT CONFLICT 332 339 SDKLFPAF -> NSARAARV (in Ref. 5). FT CONFLICT 367 367 A -> V (in Ref. 2). SQ SEQUENCE 537 AA; 59059 MW; F078D9046C2AAB06 CRC64; MAHCVTLVQL SISCDHLIDK DIGSKSDPLC VLLQDVGGGS WAELGRTERV RNCSSPEFSK TLQLEYRFET VQKLRFGIYD IDNKTPELRD DDFLGGAECS LGQIVSSQVL TLPLMLKPGK PAGRGTITVS AQELKDNRVV TMEVEARNLD KKDFLGKSDP FLEFFRQGDG KWHLVYRSEV IKNNLNPTWK RFSVPVQHFC GGNPSTPIQV QCSDYDSDGS HDLIGTFHTS LAQLQAVPAE FECIHPEKQQ KKKSYKNSGT IRVKICRVET EYSFLDYVMG GCQINFTVGV DFTGSNGDPS SPDSLHYLSP TGVNEYLMAL WSVGSVVQDY DSDKLFPAFG FGAQVPPDWQ VSHEFALNFN PSNPYCAGIQ GIVDAYRQAL PQVRLYGPTN FAPIINHVAR FAAQAAHQGT ASQYFMLLLL TDGAVTDVEA TREAVVRASN LPMSVIIVGV GGADFEAMEQ LDADGGPLHT RSGQAAARDI VQFVPYRRFQ NAPREALAQT VLAEVPTQLV SYFRAQGWAP LKPLPPSAKD PAQAPQA // ID CPNE1_MOUSE STANDARD; PRT; 536 AA. AC Q8C166; Q925K4; Q925K5; DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 30-MAY-2006, entry version 28. DE Copine-1 (Copine I). GN Name=Cpne1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Skin; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-454. RC STRAIN=ILS, and ISS; RX MEDLINE=21363810; PubMed=11471062; DOI=10.1007/s00335-001-1001-x; RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.; RT "High-throughput sequence identification of gene coding variants RT within alcohol-related QTLs."; RL Mamm. Genome 12:657-663(2001). CC -!- FUNCTION: May function in membrane trafficking. Exhibits calcium- CC dependent phospholipid binding properties. CC -!- SIMILARITY: Belongs to the copine family. CC -!- SIMILARITY: Contains 2 C2 domains. CC -!- SIMILARITY: Contains 1 VWFA domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK028882; BAC26170.1; -; mRNA. DR EMBL; BC057554; AAH57554.1; -; mRNA. DR EMBL; AF332057; AAK56086.1; -; mRNA. DR EMBL; AF332058; AAK56087.1; -; mRNA. DR UniGene; Mm.27660; -. DR Ensembl; ENSMUSG00000038171; Mus musculus. DR MGI; MGI:2386621; Cpne1. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR010734; Copine. DR InterPro; IPR002035; VWF_A. DR Pfam; PF00168; C2; 2. DR Pfam; PF07002; Copine; 1. DR SMART; SM00239; C2; 2. DR SMART; SM00327; VWA; 1. DR PROSITE; PS50004; C2_DOMAIN; 1. DR PROSITE; PS50234; VWFA; FALSE_NEG. KW Repeat. FT CHAIN 1 536 Copine-1. FT /FTId=PRO_0000144835. FT DOMAIN 1 97 C2 1. FT DOMAIN 143 227 C2 2. FT DOMAIN 284 504 VWFA. FT CONFLICT 43 43 L -> P (in Ref. 2). FT CONFLICT 452 454 ADF -> GHS (in Ref. 3). SQ SEQUENCE 536 AA; 58887 MW; DF603A71A1A74F7B CRC64; MAHCVTLVQL SVSCEHLIDK DIGSKSDPLC VLLQDVGGAW AELCRTERVR NCSSPEFSKT LQIEYHFETV QKLRFGIYDI DNKTPELGDD DFLGGAECSL GQIVSSQTLT LPLMLKPGKP AGRGTITVSA QELKDSRVVT MEVEARNLDK KDFLGKSDPF LEFFRQGDGK WQLAYRTEVV KNNLNPTWKR FSVSLQHFCG GDLSTPIQVR CSDYDSDGSH DLIGTFHTTL AQLQAVPAEF ECVHPEKQQR KKNYRNSGTV RVKTCRVETE YSFLDYVMGG CQINFTVGVD FTGSNGDPSS PDSLHYLSPT GVNEYLTALW SVGSVVQDYD SDKLFPAFGF GAQVPPDWQV SHEFALNFNP SNPYCAGIQG IVDAYRQALP QVRLYGPTNF APIINHVARF AAQAAQQRSA SQYFVLLLLT DGAVTDVEAT CKAVVDASKL PMSVIIVGVG GADFEVMEQL DADGGPLRTR SGEAAARDIV QFVPYRRFQN APRETLAQTV LAEVPTQMVS YFRAQGWAPL KAPPTPGKGP AQAPQA // ID CPNE2_HUMAN STANDARD; PRT; 548 AA. AC Q96FN4; Q68D19; Q86XP9; DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 15-AUG-2003, sequence version 3. DT 30-MAY-2006, entry version 34. DE Copine-2 (Copine II). GN Name=CPNE2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Placenta; RA Ding P., Han W., Shi S., Rui M., Wang Y., Song Q., Ma D.; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pancreas; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-548. RC TISSUE=Fetal brain; RG The German cDNA consortium; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the copine family. CC -!- SIMILARITY: Contains 2 C2 domains. CC -!- SIMILARITY: Contains 1 VWFA domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF492484; AAO85483.1; -; mRNA. DR EMBL; BC053658; AAH53658.1; -; mRNA. DR EMBL; CR749617; CAH18411.1; -; mRNA. DR UniGene; Hs.339809; -. DR Ensembl; ENSG00000140848; Homo sapiens. DR HGNC; HGNC:2315; CPNE2. DR MIM; 604206; gene. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR010734; Copine. DR InterPro; IPR002035; VWF_A. DR Pfam; PF00168; C2; 2. DR Pfam; PF07002; Copine; 1. DR PRINTS; PR00360; C2DOMAIN. DR SMART; SM00239; C2; 2. DR SMART; SM00327; VWA; 1. DR PROSITE; PS50004; C2_DOMAIN; 2. DR PROSITE; PS50234; VWFA; FALSE_NEG. KW Repeat. FT CHAIN 1 548 Copine-2. FT /FTId=PRO_0000144836. FT DOMAIN 10 115 C2 1. FT DOMAIN 141 246 C2 2. FT DOMAIN 305 507 VWFA. FT CONFLICT 100 100 K -> E (in Ref. 3). SQ SEQUENCE 548 AA; 61190 MW; 39B962C82C591DA0 CRC64; MAHIPSGGAP AAGAAPMGPQ YCVCKVELSV SGQNLLDRDV TSKSDPFCVL FTENNGRWIE YDRTETAINN LNPAFSKKFV LDYHFEEVQK LKFALFDQDK SSMRLDEHDF LGQFSCSLGT IVSSKKITRP LLLLNDKPAG KGLITIAAQE LSDNRVITLS LAGRRLDKKD LFGKSDPFLE FYKPGDDGKW MLVHRTEVIK YTLDPVWKPF TVPLVSLCDG DMEKPIQVMC YDYDNDGGHD FIGEFQTSVS QMCEARDSVP LEFECINPKK QRKKKNYKNS GIIILRSCKI NRDYSFLDYI LGGCQLMFTV GIDFTASNGN PLDPSSLHYI NPMGTNEYLS AIWAVGQIIQ DYDSDKMFPA LGFGAQLPPD WKVSHEFAIN FNPTNPFCSG VDGIAQAYSA CLPHIRFYGP TNFSPIVNHV ARFAAQATQQ RTATQYFILL IITDGVISDM EETRHAVVQA SKLPMSIIIV GVGNADFAAM EFLDGDSRML RSHTGEEAAR DIVQFVPFRE FRNAAKETLA KAVLAELPQQ VVQYFKHKNL PPTNSEPA // ID CPNE2_MOUSE STANDARD; PRT; 548 AA. AC P59108; Q8K1D7; DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2002, sequence version 1. DT 30-MAY-2006, entry version 32. DE Copine-2 (Copine II). GN Name=Cpne2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Liver, and Mammary tumor; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- SIMILARITY: Belongs to the copine family. CC -!- SIMILARITY: Contains 2 C2 domains. CC -!- SIMILARITY: Contains 1 VWFA domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC022128; AAH22128.2; -; mRNA. DR EMBL; BC031801; AAH31801.1; -; mRNA. DR UniGene; Mm.291815; -. DR HSSP; P21707; 1RSY. DR Ensembl; ENSMUSG00000034361; Mus musculus. DR MGI; MGI:2387578; Cpne2. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR010734; Copine. DR InterPro; IPR002035; VWF_A. DR Pfam; PF00168; C2; 2. DR Pfam; PF07002; Copine; 1. DR PRINTS; PR00360; C2DOMAIN. DR SMART; SM00239; C2; 2. DR SMART; SM00327; VWA; 1. DR PROSITE; PS50004; C2_DOMAIN; 2. DR PROSITE; PS50234; VWFA; FALSE_NEG. KW Repeat. FT CHAIN 1 548 Copine-2. FT /FTId=PRO_0000144837. FT DOMAIN 10 115 C2 1. FT DOMAIN 141 246 C2 2. FT DOMAIN 305 507 VWFA. FT CONFLICT 435 435 Missing (in Ref. 1; AAH22128). SQ SEQUENCE 548 AA; 61036 MW; 796F26124D2A0E13 CRC64; MAYIPDGGAP TAGAIPLGSQ CCVCKVELSV SGQNLLDRDV TSKSDPFCVL FIEDNGRWME FDRTETAVNN LNPAFSKKFV LDYHFEEVQK LKFALFDQDK SSAQLDEHDF LGQFSCSLGT IVSSKKITRP LLLMNDKPAG KGVITIAAQE LSDNRVITLS LAGRKLDKKD LFGKSDPFLE FYKPGDDGKW MLVHRTEVIK YTLDPVWKPF TVPLVSLCDG DLEKPIQVMC YDYDSNGGHD FIGEFQTSVL QMSEARDGVP LEIECINPKK QRKKKSYKNS GIIILRSCKI HRNYSFLDYI LGGCQLMFTV GIDFTASNGN PLDPSSLHYI NPMGTNEYLS AIWAVGQIIQ DYDSDKMFPA LGFGAQLPPD WKVSHEFAIN FNPTNPFCSG VDGIAQAYSA CLPHIRFYGP TNFSPIVNHV ARFAAQATQQ QTATQYFILL IITDGVISDM EETRHAVVQA SKLPMSIIIV GVGNADFAAM EFLDGDNRRL RSHTGEEAAR DIVQFVPFRE FRNAAKETLA KAVLAELPQQ VVQYFKHKNL PPTNSEPA // ID CPNE3_HUMAN STANDARD; PRT; 537 AA. AC O75131; Q8IYA1; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 30-MAY-2006, entry version 51. DE Copine-3 (Copine III). GN Name=CPNE3; Synonyms=CPN3, KIAA0636; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND RP PHOSPHORYLATION. RX MEDLINE=20496783; PubMed=11041869; DOI=10.1021/bi001250v; RA Caudell E.G., Caudell J.J., Tang C.-H., Yu T.-K., Frederick M.J., RA Grimm E.A.; RT "Characterization of human copine III as a phosphoprotein with RT associated kinase activity."; RL Biochemistry 39:13034-13043(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX MEDLINE=98403880; PubMed=9734811; DOI=10.1093/dnares/5.3.169; RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., RA Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. X. RT The complete sequences of 100 new cDNA clones from brain which can RT code for large proteins in vitro."; RL DNA Res. 5:169-176(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Skin; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: May function in membrane trafficking. Exhibits calcium- CC dependent phospholipid binding properties (By similarity). Seems CC to have a protein kinase activity. CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- PTM: Phosphorylated on serine and threonine residues. CC -!- SIMILARITY: Belongs to the copine family. CC -!- SIMILARITY: Contains 2 C2 domains. CC -!- SIMILARITY: Contains 1 VWFA domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF077226; AAD46074.2; -; mRNA. DR EMBL; AB014536; BAA31611.2; ALT_INIT; mRNA. DR EMBL; BC036242; AAH36242.1; -; mRNA. DR EMBL; BC066597; AAH66597.1; -; mRNA. DR UniGene; Hs.191219; -. DR HSSP; P21707; 1BYN. DR Ensembl; ENSG00000085719; Homo sapiens. DR H-InvDB; HIX0007631; -. DR HGNC; HGNC:2316; CPNE3. DR MIM; 604207; gene. DR GO; GO:0005829; C:cytosol; IDA. DR GO; GO:0005544; F:calcium-dependent phospholipid binding; TAS. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA. DR GO; GO:0005215; F:transporter activity; TAS. DR GO; GO:0006629; P:lipid metabolism; TAS. DR GO; GO:0016192; P:vesicle-mediated transport; TAS. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR010734; Copine. DR InterPro; IPR002035; VWF_A. DR Pfam; PF00168; C2; 2. DR Pfam; PF07002; Copine; 1. DR PRINTS; PR00360; C2DOMAIN. DR SMART; SM00239; C2; 2. DR SMART; SM00327; VWA; 1. DR PROSITE; PS50004; C2_DOMAIN; 2. DR PROSITE; PS50234; VWFA; FALSE_NEG. KW Direct protein sequencing; Kinase; Phosphorylation; Polymorphism; KW Repeat; Serine/threonine-protein kinase; Transferase. FT CHAIN 1 537 Copine-3. FT /FTId=PRO_0000144838. FT DOMAIN 1 99 C2 1. FT DOMAIN 125 230 C2 2. FT DOMAIN 291 513 VWFA. FT VARIANT 412 412 T -> M (in dbSNP:2304789). FT /FTId=VAR_024424. FT CONFLICT 394 394 P -> Q (in Ref. 3). FT CONFLICT 419 419 Q -> R (in Ref. 3). FT CONFLICT 475 475 R -> H (in Ref. 3). SQ SEQUENCE 537 AA; 60131 MW; 91F2C5EAD611B842 CRC64; MAAQCVTKVA LNVSCANLLD KDIGSKSDPL CVLFLNTSGQ QWYEVERTER IKNCLNPQFS KTFIIDYYFE VVQKLKFGVY DIDNKTIELS DDDFLGECEC TLGQIVSSKK LTRPLVMKTG RPAGKGSITI SAEEIKDNRV VLFEMEARKL DNKDLFGKSD PYLEFHKQTS DGNWLMVHRT EVVKNNLNPV WRPFKISLNS LCYGDMDKTI KVECYDYDND GSHDLIGTFQ TTMTKLKEAS RSSPVEFECI NEKKRQKKKS YKNSGVISVK QCEITVECTF LDYIMGGCQL NFTVGVDFTG SNGDPRSPDS LHYISPNGVN EYLTALWSVG LVIQDYDADK MFPAFGFGAQ IPPQWQVSHE FPMNFNPSNP YCNGIQGIVE AYRSCLPQIK LYGPTNFSPI INHVARFAAA ATQQQTASQY FVLLIITDGV ITDLDETRQA IVNASRLPMS IIIVGVGGAD FSAMEFLDGD GGSLRSPLGE VAIRDIVQFV PFRQFQNAPK EALAQCVLAE IPQQVVGYFN TYKLLPPKNP ATKQQKQ // ID CPNE3_MOUSE STANDARD; PRT; 533 AA. AC Q8BT60; Q5CZX9; Q5DU22; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 2. DT 30-MAY-2006, entry version 28. DE Copine-3 (Copine III). GN Name=Cpne3; Synonyms=Kiaa0636; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: May function in membrane trafficking. Exhibits calcium- CC dependent phospholipid binding properties (By similarity). CC -!- SIMILARITY: Belongs to the copine family. CC -!- SIMILARITY: Contains 2 C2 domains. CC -!- SIMILARITY: Contains 1 VWFA domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK220348; BAD90244.1; ALT_INIT; mRNA. DR EMBL; AK017651; BAC25524.1; -; mRNA. DR EMBL; BC090632; AAH90632.1; -; mRNA. DR UniGene; Mm.38390; -. DR HSSP; P04410; 1A25. DR Ensembl; ENSMUSG00000028228; Mus musculus. DR MGI; MGI:1917818; Cpne3. DR GO; GO:0005829; C:cytosol; ISS. DR GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS. DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS. DR GO; GO:0005215; F:transporter activity; ISS. DR GO; GO:0006629; P:lipid metabolism; ISS. DR GO; GO:0016192; P:vesicle-mediated transport; ISS. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR010734; Copine. DR InterPro; IPR002035; VWF_A. DR Pfam; PF00168; C2; 2. DR Pfam; PF07002; Copine; 1. DR PRINTS; PR00360; C2DOMAIN. DR SMART; SM00239; C2; 2. DR SMART; SM00327; VWA; 1. DR PROSITE; PS50004; C2_DOMAIN; 2. DR PROSITE; PS50234; VWFA; FALSE_NEG. KW Repeat. FT CHAIN 1 533 Copine-3. FT /FTId=PRO_0000144839. FT DOMAIN 1 99 C2 1. FT DOMAIN 125 230 C2 2. FT DOMAIN 291 513 VWFA. FT CONFLICT 37 37 T -> A (in Ref. 2). FT CONFLICT 471 533 GGSLRAPSGEVAIRDIVQFVPFRQFQNAPKEALAQCVLAEI FT PQQVVGYFNTYKLLPPKNPAVK -> EWKSPCPFRRGGHKR FT YCSVCAFQTVPECSKRSACSVCLGRDSPAGGGLLQHIQTPS FT SQKPSCEVEEPGQLQDFKSCVEQRHLSHRMMYLPSALLTPG FT YMM (in Ref. 2). SQ SEQUENCE 533 AA; 59585 MW; F76A4BDCA11C7F2E CRC64; MAAQCVTKVE LNVSCNNLLD ADVTSKSDPL CVLFLNTSGH QWYEVERTER IKNSLNPKFS KTFVIDYYFE VVQKLKFGIY DIDNKTIELS DDDFLGECEV TLGQIVSSKK LTRPLVLKNG KPAGKGSITI SAEEIKDNRV VLFEMEARKL DNKDLFGKSD PYLEFHKQTS DGHWLMVHRT EVIKNNLNPM WKPFKISLNS LCYGDMDKTI KVECYDYDND GSHDLIGTFQ TTMTKLKEAS RSSPVEYECI NEKKRQKKKS YKNSGVISVK HCEITVECTF LDYIMGGCQL NFTVGVDFTG SNGDPSSPDS LHYISPNGVN EYLTAIWSVG LVIQDYDADK MFPAFGFGAQ VPPQWQVSHE FPMNFNPSNP YCNGIQGIVE AYRTCLPQIR LYGPTNFSPI INHVARFAAA ATQQQTASQY FVLLIITDGV ITDLDETRQA IVNAAKLPMS IIIVGVGGAD FSAMEFLDGD GGSLRAPSGE VAIRDIVQFV PFRQFQNAPK EALAQCVLAE IPQQVVGYFN TYKLLPPKNP AVK // ID CPNE3_PONPY STANDARD; PRT; 537 AA. AC Q5RAE1; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 30-MAY-2006, entry version 12. DE Copine-3 (Copine III). GN Name=CPNE3; OS Pongo pygmaeus (Orangutan). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9600; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: May function in membrane trafficking. Exhibits calcium- CC dependent phospholipid binding properties (By similarity). CC -!- SIMILARITY: Belongs to the copine family. CC -!- SIMILARITY: Contains 2 C2 domains. CC -!- SIMILARITY: Contains 1 VWFA domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR859076; CAH91269.1; -; mRNA. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR010734; Copine. DR InterPro; IPR002035; VWF_A. DR Pfam; PF00168; C2; 2. DR Pfam; PF07002; Copine; 1. DR PRINTS; PR00360; C2DOMAIN. DR SMART; SM00239; C2; 2. DR SMART; SM00327; VWA; 1. DR PROSITE; PS50004; C2_DOMAIN; 2. DR PROSITE; PS50234; VWFA; FALSE_NEG. KW Repeat. FT CHAIN 1 537 Copine-3. FT /FTId=PRO_0000144840. FT DOMAIN 1 99 C2 1. FT DOMAIN 125 230 C2 2. FT DOMAIN 291 513 VWFA. SQ SEQUENCE 537 AA; 60102 MW; 7EF0448F9B15D362 CRC64; MAAQCVTKVA LNVSCANLLD KDIGSKSDPL CVLFLNTSGQ QWYEVERTER IKNCLNPQFS KTFIIDYYFE VVQKLKFGVY DIDNKTIELS DDDFLGECEC TLGQVVSSKK LTRPLVMKNG RPAGKGSITI SAEEIKDNRV VLFEMEARKP DNKDLFGKSD PYLEFHKQTS DGNWLMVHRT EVVKNNLNPV WRPFKISLNS LCYGDMDKTI KVECYDYDND GSHDLIGTFQ TTMTKLKEAS RCSPVEFECI NEKKRQKKKS YKNSGVISVK QCEITVECTF LDYIMGGCQL NFTVGVDFTG SNDDPRSPDS LHYISPNGVN EYLTALWSVG LVIQDYDADK MFPAFGFGAQ IPPQWQVSHE FPMNFNPSNP YCNGIQGIVE AYRSCLPQIK LYGPTNFSPI INHVARFAAA AAQQQTASQY FVLLIITDGV ITDLDETRQA IVNASRLPMS IIIVGVGGAD FSAMEFLDGD GGGLRSPSGE VAIRDIVQFV PFRQFQNAPK EALAQCVLAE IPQQVVGYFN TYKLLPPKNP ATKQQKQ // ID CPNE4_HUMAN STANDARD; PRT; 557 AA. AC Q96A23; Q8TEX1; DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 30-MAY-2006, entry version 34. DE Copine-4 (Copine IV) (Copine-8). GN Name=CPNE4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Prostate; RX PubMed=12670487; DOI=10.1016/S0006-291X(03)00445-5; RA Maitra R., Grigoryev D.N., Bera T.K., Pastan I.H., Lee B.; RT "Cloning, molecular characterization, and expression analysis of RT copine 8."; RL Biochem. Biophys. Res. Commun. 303:842-847(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: May function in membrane trafficking. Exhibits calcium- CC dependent phospholipid binding properties (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96A23-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96A23-2; Sequence=VSP_001214; CC -!- SIMILARITY: Belongs to the copine family. CC -!- SIMILARITY: Contains 2 C2 domains. CC -!- SIMILARITY: Contains 1 VWFA domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF465770; AAL74190.1; -; mRNA. DR EMBL; AF465771; AAL74191.1; -; mRNA. DR EMBL; AK056175; BAB71111.1; -; mRNA. DR EMBL; BC014396; AAH14396.1; -; mRNA. DR EMBL; BC075046; AAH75046.1; -; mRNA. DR UniGene; Hs.199877; -. DR HSSP; P21707; 1BYN. DR Ensembl; ENSG00000196353; Homo sapiens. DR HGNC; HGNC:2317; CPNE4. DR MIM; 604208; gene. DR LinkHub; Q96A23; -. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR010734; Copine. DR InterPro; IPR002035; VWF_A. DR Pfam; PF00168; C2; 2. DR Pfam; PF07002; Copine; 1. DR PRINTS; PR00360; C2DOMAIN. DR SMART; SM00239; C2; 2. DR SMART; SM00327; VWA; 1. DR PROSITE; PS50004; C2_DOMAIN; 1. DR PROSITE; PS50234; VWFA; FALSE_NEG. KW Alternative splicing; Repeat. FT CHAIN 1 557 Copine-4. FT /FTId=PRO_0000144841. FT DOMAIN 24 130 C2 1. FT DOMAIN 141 246 C2 2. FT DOMAIN 305 507 VWFA. FT VAR_SEQ 1 1 M -> MAVEPSSSESIKRRAGRRM (in isoform 2). FT /FTId=VSP_001214. SQ SEQUENCE 557 AA; 62395 MW; 34AA5F103FE3C7BD CRC64; MKKMSNIYES AANTLGIFNS PCLTKVELRV ACKGISDRDA LSKPDPCVIL KMQSHGQWFE VDRTEVIRTC INPVYSKLFT VDFYFEEVQR LRFEVHDISS NHNGLKEADF LGGMECTLGQ IVSQRKLSKS LLKHGNTAGK SSITVIAEEL SGNDDYVELA FNARKLDDKD FFSKSDPFLE IFRMNDDATQ QLVHRTEVVM NNLSPAWKSF KVSVNSLCSG DPDRRLKCIV WDWDSNGKHD FIGEFTSTFK EMRGAMEGKQ VQWECINPKY KAKKKNYKNS GTVILNLCKI HKMHSFLDYI MGGCQIQFTV AIDFTASNGD PRNSCSLHYI HPYQPNEYLK ALVAVGEICQ DYDSDKMFPA FGFGARIPPE YTVSHDFAIN FNEDNPECAG IQGVVEAYQS CLPKLQLYGP TNIAPIIQKV AKSASEETNT KEASQYFILL ILTDGVITDM ADTREAIVHA SHLPMSVIIV GVGNADFSDM QMLDGDDGIL RSPKGEPVLR DIVQFVPFRN FKHASPAALA KSVLAEVPNQ VVDYYNGKGI KPKCSSEMYE SSRTLAP // ID CPNE4_MOUSE STANDARD; PRT; 557 AA. AC Q8BLR2; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 30-MAY-2006, entry version 29. DE Copine-4 (Copine IV). GN Name=Cpne4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain cortex; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: May function in membrane trafficking. Exhibits calcium- CC dependent phospholipid binding properties (By similarity). CC -!- SIMILARITY: Belongs to the copine family. CC -!- SIMILARITY: Contains 2 C2 domains. CC -!- SIMILARITY: Contains 1 VWFA domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK043692; BAC31619.1; -; mRNA. DR EMBL; BC043087; AAH43087.1; -; mRNA. DR EMBL; BC063081; AAH63081.1; -; mRNA. DR UniGene; Mm.326240; -. DR HSSP; P21707; 1BYN. DR Ensembl; ENSMUSG00000032564; Mus musculus. DR MGI; MGI:1921270; Cpne4. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR010734; Copine. DR InterPro; IPR002035; VWF_A. DR Pfam; PF00168; C2; 2. DR Pfam; PF07002; Copine; 1. DR PRINTS; PR00360; C2DOMAIN. DR SMART; SM00239; C2; 2. DR SMART; SM00327; VWA; 1. DR PROSITE; PS50004; C2_DOMAIN; 1. DR PROSITE; PS50234; VWFA; FALSE_NEG. KW Repeat. FT CHAIN 1 557 Copine-4. FT /FTId=PRO_0000144842. FT DOMAIN 24 130 C2 1. FT DOMAIN 141 246 C2 2. FT DOMAIN 305 507 VWFA. SQ SEQUENCE 557 AA; 62408 MW; B9AAD11F3777F14F CRC64; MKKMSNIYES AANTLGIFNS PCLTKVELRV ACKGISDRDA LSKPDPCVIL KMQSHGQWFE VDRTEVIRTC INPVYSKLFT VDFYFEEVQR LRFEVHDISS NHNGLKEADF LGGMECTLGQ IVSQRKLSKS LLKHGNTAGK SSITVIAEEL SGNDDYVELA FNARKLDDKD FFSKSDPFLE IFRMNDDATQ QLVHRTEVVM NNLSPAWKSF KVSVNSLCSG DPDRRLKCIV WDWDSNGKHD FIGEFTSTFK EMRGAMEGKQ VQWECINPKY KAKKKNYKNS GMVILNQCKI HKMHSFLDYI MGGCQIQFTV AIDFTASNGD PRNSCSLHYI HPYQPNEYLK ALVAVGEICQ DYDSDKMFPA FGFGARIPPE YTVSHDFAIN FNEDNPECAG IQGVVEAYQS CLPKLQLYGP TNIAPIIQKV AKSASEETNT KEASQYFILL ILTDGVITDM ADTREAIVHA SHLPMSVIIV GVGNADFSDM QMLDGDDGIL RSPKGEPVLR DIVQFVPFRN FKHASPAALA KSVLAEVPNQ VVDYYNGKGI KPKCSSEVYE SSRTLAP // ID CPNE5_HUMAN STANDARD; PRT; 593 AA. AC Q9HCH3; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 2. DT 30-MAY-2006, entry version 35. DE Copine-5 (Copine V). GN Name=CPNE5; Synonyms=KIAA1599; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX MEDLINE=20450683; PubMed=10997877; DOI=10.1093/dnares/7.4.271; RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. RT XVIII. The complete sequences of 100 new cDNA clones from brain which RT code for large proteins in vitro."; RL DNA Res. 7:273-281(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22935763; PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). CC -!- FUNCTION: May function in membrane trafficking. Exhibits calcium- CC dependent phospholipid binding properties (By similarity). CC -!- SIMILARITY: Belongs to the copine family. CC -!- SIMILARITY: Contains 2 C2 domains. CC -!- SIMILARITY: Contains 1 VWFA domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB046819; BAB13425.1; ALT_INIT; mRNA. DR EMBL; Z85996; CAD92810.1; -; Genomic_DNA. DR UniGene; Hs.372129; -. DR HSSP; P05696; 1DSY. DR Ensembl; ENSG00000124772; Homo sapiens. DR H-InvDB; HIX0005825; -. DR HGNC; HGNC:2318; CPNE5. DR MIM; 604209; gene. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR010734; Copine. DR InterPro; IPR002035; VWF_A. DR Pfam; PF00168; C2; 2. DR Pfam; PF07002; Copine; 1. DR PRINTS; PR00360; C2DOMAIN. DR SMART; SM00239; C2; 2. DR SMART; SM00327; VWA; 1. DR PROSITE; PS50004; C2_DOMAIN; 2. DR PROSITE; PS50234; VWFA; 1. KW Polymorphism; Repeat. FT CHAIN 1 593 Copine-5. FT /FTId=PRO_0000144843. FT DOMAIN 29 116 C2 1. FT DOMAIN 147 268 C2 2. FT DOMAIN 328 554 VWFA. FT VARIANT 33 33 N -> S (in dbSNP:3734334). FT /FTId=VAR_020358. FT VARIANT 582 582 R -> H (in dbSNP:3830138). FT /FTId=VAR_021954. SQ SEQUENCE 593 AA; 65734 MW; 7C470A51B70A5162 CRC64; MEQPEDMASL SEFDSLAGSI PATKVEITVS CRNLLDKDMF SKSDPLCVMY TQGMENKQWR EFGRTEVIDN TLNPDFVRKF IVDYFFEEKQ NLRFDLYDVD SKSPDLSKHD FLGQAFCTLG EIVGSPGSRL EKPLTIGAFS LNSRTGKPMP AVSNGGVPGK KCGTIILSAE ELSNCRDVAT MQFCANKLDK KDFFGKSDPF LVFYRSNEDG TFTICHKTEV MKNTLNPVWQ TFSIPVRALC NGDYDRTIKV EVYDWDRDGS HDFIGEFTTS YRELARGQSQ FNIYEVVNPK KKMKKKKYVN SGTVTLLSFA VESECTFLDY IKGGTQINFT VAIDFTASNG NPSQSTSLHY MSPYQLNAYA LALTAVGEII QHYDSDKMFP ALGFGAKLPP DGRVSHEFPL NGNQENPSCC GIDGILEAYH RSLRTVQLYG PTNFAPVVTH VARNAAAVQD GSQYSVLLII TDGVISDMAQ TKEAIVNAAK LPMSIIIVGV GQAEFDAMVE LDGDDVRISS RGKLAERDIV QFVPFRDYVD RTGNHVLSMA RLARDVLAEI PDQLVSYMKA QGIRPRPPPA APTHSPSQSP ARTPPASPLH THI // ID CPNE5_MOUSE STANDARD; PRT; 593 AA. AC Q8JZW4; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 30-MAY-2006, entry version 26. DE Copine-5 (Copine V). GN Name=Cpne5; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain cortex; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Retina; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: May function in membrane trafficking. Exhibits calcium- CC dependent phospholipid binding properties (By similarity). CC -!- SIMILARITY: Belongs to the copine family. CC -!- SIMILARITY: Contains 2 C2 domains. CC -!- SIMILARITY: Contains 1 VWFA domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK044042; BAC31750.1; -; mRNA. DR EMBL; BC036971; AAH36971.1; -; mRNA. DR UniGene; Mm.39905; -. DR HSSP; P05696; 1DSY. DR Ensembl; ENSMUSG00000024008; Mus musculus. DR MGI; MGI:2385908; Cpne5. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR010734; Copine. DR InterPro; IPR002035; VWF_A. DR Pfam; PF00168; C2; 2. DR Pfam; PF07002; Copine; 1. DR PRINTS; PR00360; C2DOMAIN. DR SMART; SM00239; C2; 2. DR SMART; SM00327; VWA; 1. DR PROSITE; PS50004; C2_DOMAIN; 2. DR PROSITE; PS50234; VWFA; 1. KW Repeat. FT CHAIN 1 593 Copine-5. FT /FTId=PRO_0000144844. FT DOMAIN 9 116 C2 1. FT DOMAIN 147 268 C2 2. FT DOMAIN 328 554 VWFA. SQ SEQUENCE 593 AA; 65592 MW; 0B0BF66A852EACC2 CRC64; MEQPEDMASL SEFDSLAGSI PATKVEITVS CRNLLDKDMF SKSDPLCVMY TQGMENKQWR EFGRTEVIDN TLNPDFVRKF IVDYFFEEKQ NLRFDLYDVD SKSPDLSKHD FLGQAFCTLG EIVGSSGSRL EKPLTIGTFS LNSRTGKPMP AVSNGGVPGK KCGTIILSAE ELSNCRDVAT MQFCANKLDK KDFFGKSDPF LVFYRSNEDG TFTICHKTEV MKNTLNPVWQ TFSIPVRALC NGDYDRTIKV EVYDWDRDGS HDFIGEFTTS YRELARGQSQ FNIYEVINPK KKMKKKKYVN SGTVTLLSFA VESESTFLDY IKGGTQINFT VAIDFTASNG NPSQSTSLHY MSPYQLNAYA LALTAVGEII QHYDSDKMFP ALGFGAKLPP DGRVSHEFPL NGNQENPSCC GIDGILEAYH SSLRTVQLYG PTNFAPVVTH VARNAAAVQD GSQYSVLLII TDGVISDMAQ TKEAIVNAAK LPMSIIIVGV GQAEFDAMVE LDGDDVRISS RGKLAERDIV QFVPFRDYVD RTGNHVLSMA RLARDVLAEI PDQLVSYMKA QGIRPRPPPA APAQSPPQSP AHSPPGSPVH THI // ID CPNE6_HUMAN STANDARD; PRT; 557 AA. AC O95741; Q53HA6; Q8WVG1; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 3. DT 30-MAY-2006, entry version 44. DE Copine-6 (Copine VI) (Neuronal-copine) (N-copine). GN Name=CPNE6; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=98307387; PubMed=9645480; DOI=10.1016/S0014-5793(98)00497-9; RA Nakayama T., Yaoi T., Yasui M., Kuwajima G.; RT "N-copine: a novel two C2-domain-containing protein with neuronal RT activity-regulated expression."; RL FEBS Lett. 428:80-84(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: May function in membrane trafficking. Exhibits calcium- CC dependent phospholipid binding properties. May have a role in CC synaptic plasticity (By similarity). CC -!- SIMILARITY: Belongs to the copine family. CC -!- SIMILARITY: Contains 2 C2 domains. CC -!- SIMILARITY: Contains 1 VWFA domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB009288; BAA75899.1; -; mRNA. DR EMBL; AK222675; BAD96395.1; -; mRNA. DR EMBL; BC018046; AAH18046.1; -; mRNA. DR UniGene; Hs.6132; -. DR HSSP; P10688; 1DJH. DR Ensembl; ENSG00000100884; Homo sapiens. DR H-InvDB; HIX0011550; -. DR HGNC; HGNC:2319; CPNE6. DR MIM; 605688; gene. DR GO; GO:0005509; F:calcium ion binding; TAS. DR GO; GO:0005215; F:transporter activity; TAS. DR GO; GO:0006629; P:lipid metabolism; TAS. DR GO; GO:0007399; P:nervous system development; TAS. DR GO; GO:0007268; P:synaptic transmission; TAS. DR GO; GO:0016192; P:vesicle-mediated transport; TAS. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR010734; Copine. DR InterPro; IPR002035; VWF_A. DR Pfam; PF00168; C2; 2. DR Pfam; PF07002; Copine; 1. DR PRINTS; PR00360; C2DOMAIN. DR SMART; SM00239; C2; 2. DR SMART; SM00327; VWA; 1. DR PROSITE; PS50004; C2_DOMAIN; 1. DR PROSITE; PS50234; VWFA; 1. KW Repeat. FT CHAIN 1 557 Copine-6. FT /FTId=PRO_0000144845. FT DOMAIN 24 111 C2 1. FT DOMAIN 138 243 C2 2. FT DOMAIN 306 526 VWFA. FT CONFLICT 13 13 P -> Q (in Ref. 3). FT CONFLICT 87 87 L -> V (in Ref. 3). FT CONFLICT 331 331 P -> H (in Ref. 2). SQ SEQUENCE 557 AA; 61991 MW; CA1ECA3560926FC2 CRC64; MSDPEMGWVP EPPTMTLGAS RVELRVSCHG LLDRDTLTKP HPCVLLKLYS DEQWVEVERT EVLRSCSSPV FSRVLALEYF FEEKQPLQFH VFDAEDGATS PRNDTFLGST ECTLGQIVSQ TKVTKPLLLK NGKTAGKSTI TIVAEEVSGT NDYVQLTFRA YKLDNKDLFS KSDPFMEIYK TNEDQSDQLV WRTEVVKNNL NPSWEPFRLS LHSLCSCDVH RPLKFLVYDY DSSGKHDFIG EFTSTFQEMQ EGTANPGQEM QWDCINPKYR DKKKNYKSSG TVVLAQCTVE KVHTFLDYIM GGCQISFTVA IDFTASNGDP RSSQSLHCLS PRQPNHYLQA LRAVGGICQD YDSDKRFPAF GFGARIPPNF EVSHDFAINF DPENPECEEI SGVIASYRRC LPQIQLYGPT NVAPIINRVA EPAQREQSTG QATKYSVLLV LTDGVVSDMA ETRTAIVRAS RLPMSIIIVG VGNADFSDMR LLDGDDGPLR CPRGVPAARD IVQFVPFRDF KDAAPSALAK CVLAEVPRQV VEYYASQGIS PGAPRPCTLA TTPSPSP // ID CPNE6_MOUSE STANDARD; PRT; 557 AA. AC Q9Z140; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 30-MAY-2006, entry version 40. DE Copine-6 (Copine VI) (Neuronal-copine) (N-copine). GN Name=Cpne6; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=98307387; PubMed=9645480; DOI=10.1016/S0014-5793(98)00497-9; RA Nakayama T., Yaoi T., Yasui M., Kuwajima G.; RT "N-copine: a novel two C2-domain-containing protein with neuronal RT activity-regulated expression."; RL FEBS Lett. 428:80-84(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: May function in membrane trafficking. Exhibits calcium- CC dependent phospholipid binding properties (By similarity). May CC have a role in synaptic plasticity. CC -!- SIMILARITY: Belongs to the copine family. CC -!- SIMILARITY: Contains 2 C2 domains. CC -!- SIMILARITY: Contains 1 VWFA domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB008893; BAA75898.1; -; mRNA. DR EMBL; BC050766; AAH50766.1; -; mRNA. DR UniGene; Mm.5249; -. DR HSSP; P10688; 1DJH. DR Ensembl; ENSMUSG00000022212; Mus musculus. DR MGI; MGI:1334445; Cpne6. DR GO; GO:0030424; C:axon; IDA. DR GO; GO:0030425; C:dendrite; IDA. DR GO; GO:0005624; C:membrane fraction; IDA. DR GO; GO:0001786; F:phosphatidylserine binding; IDA. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR010734; Copine. DR InterPro; IPR002035; VWF_A. DR Pfam; PF00168; C2; 2. DR Pfam; PF07002; Copine; 1. DR PRINTS; PR00360; C2DOMAIN. DR SMART; SM00239; C2; 2. DR SMART; SM00327; VWA; 1. DR PROSITE; PS50004; C2_DOMAIN; 1. DR PROSITE; PS50234; VWFA; 1. KW Repeat. FT CHAIN 1 557 Copine-6. FT /FTId=PRO_0000144846. FT DOMAIN 24 111 C2 1. FT DOMAIN 138 243 C2 2. FT DOMAIN 306 526 VWFA. SQ SEQUENCE 557 AA; 61781 MW; 043D6C1487E2ECAC CRC64; MSDPEMGWVP EPPAMTLGAS RVELRVSCHG LLDRDTLTKP HPCVLLKLYS DEQWVEVERT EVLRSCSSPV FSRVLAIEYF FEEKQPLQFH VFDAEDGATS PSSDTFLGST ECTLGQIVSQ TKVTKPLLLK NGKTAGKSTI TIVAEEVSGT NDYVQLTFRA HKLDNKDLFS KSDPFMEIYK TNGDQSDQLV WRTEVVKNNL NPSWEPFRLS LHSLCSCDIH RPLKFLVYDY DSSGKHDFIG EFTSTFQEMQ EGTANPGQEM QWDCINPKYR DKKKNYKSSG TVVLAQCTVE KVHTFLDYIM GGCQISFTVA IDFTASNGDP RSSQSLHCLS PRQPNHYLQA LRTVGGICQD YDSDKRFPAF GFGARIPPNF EVSHDFAINF DPENPECEEI SGVIASYRRC LPQIQLYGPT NVAPIINRVA EPAQREQSTG QATKYSVLLV LTDGVVSDMA ETRTAIVRAS RLPMSIIIVG VGNADFSDMR LLDGDDGPLR CPKGVPAARD IVQFVPFRDF KDAAPSALAK CVLAEVPRQV VEYYASQGIS PGAPRPSTPA MTPSPSP // ID CPNE6_PONPY STANDARD; PRT; 557 AA. AC Q5R4W6; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 30-MAY-2006, entry version 12. DE Copine-6 (Copine VI). GN Name=CPNE6; OS Pongo pygmaeus (Orangutan). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9600; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain cortex; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: May function in membrane trafficking. Exhibits calcium- CC dependent phospholipid binding properties. May have a role in CC synaptic plasticity (By similarity). CC -!- SIMILARITY: Belongs to the copine family. CC -!- SIMILARITY: Contains 2 C2 domains. CC -!- SIMILARITY: Contains 1 VWFA domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR861125; CAH93200.1; -; mRNA. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR010734; Copine. DR InterPro; IPR002035; VWF_A. DR Pfam; PF00168; C2; 2. DR Pfam; PF07002; Copine; 1. DR PRINTS; PR00360; C2DOMAIN. DR SMART; SM00239; C2; 2. DR SMART; SM00327; VWA; 1. DR PROSITE; PS50004; C2_DOMAIN; 1. DR PROSITE; PS50234; VWFA; 1. KW Repeat. FT CHAIN 1 557 Copine-6. FT /FTId=PRO_0000144847. FT DOMAIN 24 111 C2 1. FT DOMAIN 138 243 C2 2. FT DOMAIN 306 526 VWFA. SQ SEQUENCE 557 AA; 62028 MW; F75867E0BB1632E5 CRC64; MSDPEMGWVP EPPTMTLGAS RVELRVSCHG LLDRDTLTKP HPCVLLKLYS DEQWVEVERT EVLRSCSSPV FSRVLALEYF FEEKQPLQFH VFDAEDGATS PRNDTFLGST ECTLGQIVSQ TKVTKPLLLK NGKTAGKSTI TIVAEEVSGT NDYVQLTFRA YKLDNKDPFS KSDPFMEIYK TNEDQSDQLV WRTEVVKNNL NPSWEPFRLS LHSLCSCDVH RPLKFLVYDY DSSGKHDFIG EFTSTFQEMQ EGTANPGQEM QWDCINPKYR DKKKNYKSSG TVVLAQCTVE KVHTFLDYIM GGCQISFTVA IDFTASNGDP RSSQSLHCLS PRQPNHYLQA LRAVGGICQD YDSDKRFPAF GFGARIPPNF EVSHDFAINF DPENPECEEI SGVIASYRRC LPQIQLYGPT NVAPIINRVA EPAQREQSTG QATKYSVLLV LTDGVVSDMA ETRTAIVRAS RLPMSIIIVG VGNADFSDMR LLDGDDGPLR CPRGVPAARD IVQFVPFRDF KDAAPSALAK RVLAEVPRQV VEYYASQGIS PGAPRPCTLA TTPSPSP // ID CPNE7_HUMAN STANDARD; PRT; 633 AA. AC Q9UBL6; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 30-MAY-2006, entry version 39. DE Copine-7 (Copine VII). GN Name=CPNE7; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). RX MEDLINE=20005944; PubMed=10534407; DOI=10.1006/geno.1999.5958; RA Savino M., D'Apolito M., Centra M., van Beerendonk H.M., RA Cleton Jansen A., Whitmore S.A., Crawford J., Callen D.F., Zelante L., RA Savoia A.; RT "Characterization of copine VII, a new member of the copine family, RT and its exclusion as a candidate in sporadic breast cancers with loss RT of heterozygosity at 16q24.3."; RL Genomics 61:219-226(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: May function in membrane trafficking. Exhibits calcium- CC dependent phospholipid binding properties (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UBL6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UBL6-2; Sequence=VSP_001215; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the copine family. CC -!- SIMILARITY: Contains 2 C2 domains. CC -!- SIMILARITY: Contains 1 VWFA domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ133798; CAB61431.1; -; mRNA. DR EMBL; AJ133799; CAB61446.1; -; Genomic_DNA. DR EMBL; AJ133800; CAB61446.1; JOINED; Genomic_DNA. DR EMBL; AJ133801; CAB61446.1; JOINED; Genomic_DNA. DR EMBL; AJ133802; CAB61446.1; JOINED; Genomic_DNA. DR EMBL; AJ133803; CAB61446.1; JOINED; Genomic_DNA. DR EMBL; AJ133804; CAB61446.1; JOINED; Genomic_DNA. DR EMBL; AJ133805; CAB61446.1; JOINED; Genomic_DNA. DR EMBL; AJ133806; CAB61446.1; JOINED; Genomic_DNA. DR EMBL; AJ133807; CAB61446.1; JOINED; Genomic_DNA. DR EMBL; AJ133808; CAB61446.1; JOINED; Genomic_DNA. DR EMBL; AJ133809; CAB61446.1; JOINED; Genomic_DNA. DR EMBL; AJ133810; CAB61446.1; JOINED; Genomic_DNA. DR EMBL; BC035334; AAH35334.1; -; mRNA. DR EMBL; BC064577; AAH64577.1; -; mRNA. DR UniGene; Hs.461775; -. DR HSSP; P04410; 1A25. DR Ensembl; ENSG00000178773; Homo sapiens. DR HGNC; HGNC:2320; CPNE7. DR MIM; 605689; gene. DR GO; GO:0005215; F:transporter activity; TAS. DR GO; GO:0006629; P:lipid metabolism; TAS. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR010734; Copine. DR InterPro; IPR002035; VWF_A. DR Pfam; PF00168; C2; 2. DR Pfam; PF07002; Copine; 1. DR PRINTS; PR00360; C2DOMAIN. DR SMART; SM00239; C2; 2. DR SMART; SM00327; VWA; 1. DR PROSITE; PS50004; C2_DOMAIN; 2. DR PROSITE; PS50234; VWFA; 1. KW Alternative splicing; Polymorphism; Repeat. FT CHAIN 1 633 Copine-7. FT /FTId=PRO_0000144848. FT DOMAIN 28 114 C2 1. FT DOMAIN 237 321 C2 2. FT DOMAIN 382 581 VWFA. FT VAR_SEQ 120 194 Missing (in isoform 2). FT /FTId=VSP_001215. FT VARIANT 77 77 F -> L (in dbSNP:455527). FT /FTId=VAR_021955. FT VARIANT 633 633 P -> L (in dbSNP:3751682). FT /FTId=VAR_021956. SQ SEQUENCE 633 AA; 70294 MW; 8AF4B68D3EFC51BB CRC64; MSAGSERGAA ATPGGLPAPC ASKVELRLSC RHLLDRDPLT KSDPSVALLQ QAQGQWVQVG RTEVVRSSLH PVFSKVFTVD YYFEEVQRLR FEVYDTHGPS GFSCQEDDFL GGMECTLGQP AQKWLLQVVM RVSVDVLGPA GHCAKHFLCC TESSHLARTG PSFLLRYDDL CLPWATAGAV RWWTCRGGHT QGWQIVAQKK VTRPLLLKFG RNAGKSTITV IAEDISGNNG YVELSFRARK LDDKDLFSKS DPFLELYRVN DDQGLQLVYR TEVVKNNLNP VWEAFKVSLS SLCSCEETRP LKCLVWDYDS RGKHDFIGEF STTFEEMQKA FEEGQAQWDC VNPKYKQKRR SYKNSGVVVL ADLKFHRVYS FLDYIMGGCQ IHFTVAIDFT ASNGDPRNSC SLHYINPYQP NEYLKALVSV GEICQDYDSD KRFSALGFGA RIPPKYEVSH DFAINFNPED DECEGIQGVV EAYQNCLPRV QLYGPTNVAP IISKVARVAA AEESTGKASQ YYILLILTDG VVTDMADTRE AIVRASRLPM SIIIVGVGNA DFTDMQVLDG DDGVLRSPRG EPALRDIVQF VPFRELKNAS PAALAKCVLA EVPKQVVEYY SHRGLPPRSL GVPAGEASPG CTP // ID CPNE8_HUMAN STANDARD; PRT; 564 AA. AC Q86YQ8; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 30-MAY-2006, entry version 20. DE Copine-8 (Copine VIII). GN Name=CPNE8; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Hromas R.A., Ramsey H., Richkind K.; RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: May function in membrane trafficking. Exhibits calcium- CC dependent phospholipid binding properties (By similarity). CC -!- SIMILARITY: Belongs to the copine family. CC -!- SIMILARITY: Contains 2 C2 domains. CC -!- SIMILARITY: Contains 1 VWFA domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY177785; AAO21123.1; -; mRNA. DR UniGene; Hs.40910; -. DR HSSP; P21707; 1BYN. DR Ensembl; ENSG00000139117; Homo sapiens. DR HGNC; HGNC:23498; CPNE8. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR010734; Copine. DR InterPro; IPR002035; VWF_A. DR Pfam; PF00168; C2; 2. DR Pfam; PF07002; Copine; 1. DR PRINTS; PR00360; C2DOMAIN. DR SMART; SM00239; C2; 2. DR SMART; SM00327; VWA; 1. DR PROSITE; PS50004; C2_DOMAIN; 2. DR PROSITE; PS50234; VWFA; 1. KW Repeat. FT CHAIN 1 564 Copine-8. FT /FTId=PRO_0000144849. FT DOMAIN 10 117 C2 1. FT DOMAIN 144 249 C2 2. FT DOMAIN 309 510 VWFA. SQ SEQUENCE 564 AA; 63122 MW; AD0DDAA905EF369A CRC64; MDSRYNSTAG IGDLNQLSAA IPATRVEVSV SCRNLLDRDT FSKSDPICVL YVQGVGNKEW REFGRTEVID NTLNPDFVRK FILDYFFEER ENLRFDLYDV DSKSPNLSKH DFLGQVFCTL GEIVGSQGSR LEKPIVGIPG KKCGTIILTA EELNCCRDAV LMQFCANKLD KKDFFGKSDP FLVFYRSNED GSFTICHKTE VVKNTLNPVW QAFKISVRAL CNGDYDRTIK VEVYDWDRDG SHDFIGEFTT SYRELSRGQS QFNVYEVVNP KKKGKKKKYT NSGTVTLLSF LVETEVSFLD YIKGGTQINF TVAIDFTASN GNPAQPTSLH YMNPYQLNAY GMALKAVGEI VQDYDSDKMF PALGFGAKLP PDGRISHEFA LNGNPQNPYC DGIEGVMEAY YRSLKSVQLY GPTNFAPVIN HVARYASSVK DGSQYFVLLI VTDGIISDMA QTKESIVNAS KLPMSIIIVG VGPAEFDAMV ELDGDDVRVS SRGKYAERDI VQFVPFRDYI DRSGNHILSM ARLAKDVLAE IPEQFLSYMR ARGIKPSPAP PPYTPPTHVL QTQI // ID CPNE8_MOUSE STANDARD; PRT; 564 AA. AC Q9DC53; Q9CUZ8; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 16-JAN-2004, sequence version 2. DT 30-MAY-2006, entry version 30. DE Copine-8 (Copine VIII). GN Name=Cpne8; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Lung, and Tongue; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). CC -!- FUNCTION: May function in membrane trafficking. Exhibits calcium- CC dependent phospholipid binding properties (By similarity). CC -!- SIMILARITY: Belongs to the copine family. CC -!- SIMILARITY: Contains 2 C2 domains. CC -!- SIMILARITY: Contains 1 VWFA domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK004559; BAB23372.1; ALT_INIT; mRNA. DR EMBL; AK010227; BAB26781.1; ALT_INIT; mRNA. DR UniGene; Mm.290991; -. DR HSSP; P21707; 1BYN. DR Ensembl; ENSMUSG00000052560; Mus musculus. DR MGI; MGI:1914121; Cpne8. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR010734; Copine. DR InterPro; IPR002035; VWF_A. DR Pfam; PF00168; C2; 2. DR Pfam; PF07002; Copine; 1. DR PRINTS; PR00360; C2DOMAIN. DR SMART; SM00239; C2; 2. DR SMART; SM00327; VWA; 1. DR PROSITE; PS50004; C2_DOMAIN; 2. DR PROSITE; PS50234; VWFA; 1. KW Repeat. FT CHAIN 1 564 Copine-8. FT /FTId=PRO_0000144850. FT DOMAIN 10 117 C2 1. FT DOMAIN 144 249 C2 2. FT DOMAIN 309 510 VWFA. SQ SEQUENCE 564 AA; 63123 MW; 6F1D0ACF01725418 CRC64; MDSRYTSATG IGDLNQLSAA IPATRVEVSV SCRNLLDRDT FSKSDPICVL YTQAVGNKEW REFGRTEVID NTLNPDFVRK FILDYFFEER ENLRFDLYDV DSKSPNLSKH DFLGQVFCTL GEIVGSQGSR LEKPIVGIPG RKCGTIILTA EELNCCRDAV LMQFCANKLD KKDFFGKSDP FLVFYRSNED GSFTICHKTE VVKNTLNPVW QAFKISVRAL CNGDYDRTIK VEVYDWDRDG SHDFIGEFTT SYRELARGQS QFNVYEVVNP KKKGKKKKYT NSGTVTLLSF LVETEVSFLD YIKGGTQINF TVAIDFTASN GNPAQPTSLH YMNPYQLNAY GMALKAVGEI VQDYDSDKMF PALGFGAKLP PDGRISHEFA LNGNPQNPYC DGIEGVMEAY YRSLKSVQLY GPTNFAPVIN HVARYASSVK DGSQYFVLLI VTDGVISDMA QTKESIVNAS KLPMSIIIVG VGPAEFDAMV ELDGDDVRVS SRGKYAERDI VQFVPFRDYI DRSGNHILSM ARLAKDVLAE IPEQFLSYMR ARGIKPSPAP PPYTPPTHVL QTQI // ID DOC2A_HUMAN STANDARD; PRT; 400 AA. AC Q14183; Q6P4G4; Q7Z5G0; Q8IVX0; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 3. DT 30-MAY-2006, entry version 42. DE Double C2-like domain-containing protein alpha (Doc2-alpha) (Doc2). GN Name=DOC2A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT SER-48. RC TISSUE=Brain; RX MEDLINE=95126937; PubMed=7826360; RA Orita S., Sasaki T., Naito A., Maeda M., Igarashi H., Takai Y.; RT "Doc2, a novel synaptic vesicle protein with two repeated C2-like RT domains."; RL Biochem. Biophys. Res. Commun. 206:439-448(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Mammary gland; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.