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CPNE1_RAT
ID   CPNE1_RAT               Reviewed;         536 AA.
AC   D4A1R8; D3ZSJ8; H1UBM6;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Copine-1 {ECO:0000305};
DE   AltName: Full=Copine I {ECO:0000250|UniProtKB:Q99829, ECO:0000312|RGD:1311148};
GN   Name=Cpne1 {ECO:0000312|RGD:1311148};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000312|EMBL:CAO00504.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar {ECO:0000312|EMBL:CAO00504.1};
RC   TISSUE=Brain {ECO:0000312|EMBL:CAO00504.1};
RA   Galic M., Kriz A., Vigot R., Reinhard J., Zhang Y.P., Bezakova G.,
RA   Bentzinger C.F., Cloetta D., Stebler M., Bettler B., Oertner T.G.,
RA   Ruegg M.A.;
RT   "Regulation of dendritic spine morphogenesis and synapse formation by
RT   Copine family members.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000312|EMBL:EDL85869.1};
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=11123945; DOI=10.1021/bi0019949;
RA   Tomsig J.L., Creutz C.E.;
RT   "Biochemical characterization of copine: a ubiquitous Ca2+-dependent,
RT   phospholipid-binding protein.";
RL   Biochemistry 39:16163-16175(2000).
CC   -!- FUNCTION: Calcium-dependent phospholipid-binding protein that plays a
CC       role in calcium-mediated intracellular processes. Involved in the TNF-
CC       alpha receptor signaling pathway in a calcium-dependent manner.
CC       Exhibits calcium-dependent phospholipid binding properties. Plays a
CC       role in neuronal progenitor cell differentiation; induces neurite
CC       outgrowth via a AKT-dependent signaling cascade and calcium-independent
CC       manner. May recruit target proteins to the cell membrane in a calcium-
CC       dependent manner. May function in membrane trafficking. Involved in
CC       TNF-alpha-induced NF-kappa-B transcriptional repression by inducing
CC       endoprotease processing of the transcription factor NF-kappa-B p65/RELA
CC       subunit. Also induces endoprotease processing of NF-kappa-B p50/NFKB1,
CC       p52/NFKB2, RELB and REL. {ECO:0000250|UniProtKB:Q99829}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC   -!- SUBUNIT: Homodimer; homodimerizes via its C2 domains. Interacts with
CC       p65/RELA (via N-terminus); this interaction induces proteolytic
CC       cleavage of p65/RELA subunit and inhibition of NF-kappa-B
CC       transcriptional activity. Interacts (via VWFA domain) with ACTB,
CC       CCDC22, MYCBP2, PPP5C, RDX and UBE2O. {ECO:0000250|UniProtKB:Q99829}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99829}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q99829}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q99829}. Note=Translocates to the cell membrane
CC       in a calcium-dependent manner. {ECO:0000250|UniProtKB:Q99829}.
CC   -!- TISSUE SPECIFICITY: Expressed in liver, brain, heart, intestine, kidney
CC       and lung (at protein level) (PubMed:11123945).
CC       {ECO:0000269|PubMed:11123945}.
CC   -!- DOMAIN: C2 domains are necessary for calcium-dependent cell membrane
CC       association. C2 domains are necessary for neuronal progenitor cell
CC       differentiation in a calcium-independent manner.
CC       {ECO:0000250|UniProtKB:Q99829}.
CC   -!- SIMILARITY: Belongs to the copine family. {ECO:0000305}.
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DR   EMBL; AM747279; CAO00504.1; -; mRNA.
DR   EMBL; AABR07054396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC118414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH474050; EDL85869.1; -; Genomic_DNA.
DR   EMBL; CH474050; EDL85870.1; -; Genomic_DNA.
DR   EMBL; CH474050; EDL85872.1; -; Genomic_DNA.
DR   EMBL; CH474050; EDL85873.1; -; Genomic_DNA.
DR   RefSeq; NP_001243394.1; NM_001256465.1.
DR   RefSeq; XP_003749656.1; XM_003749608.4.
DR   RefSeq; XP_006235518.1; XM_006235456.3.
DR   RefSeq; XP_006235519.1; XM_006235457.3.
DR   RefSeq; XP_008760635.1; XM_008762413.2.
DR   RefSeq; XP_017447524.1; XM_017592035.1.
DR   RefSeq; XP_017447525.1; XM_017592036.1.
DR   RefSeq; XP_017447747.1; XM_017592258.1.
DR   RefSeq; XP_017447748.1; XM_017592259.1.
DR   AlphaFoldDB; D4A1R8; -.
DR   SMR; D4A1R8; -.
DR   STRING; 10116.ENSRNOP00000026657; -.
DR   jPOST; D4A1R8; -.
DR   PaxDb; D4A1R8; -.
DR   PeptideAtlas; D4A1R8; -.
DR   PRIDE; D4A1R8; -.
DR   Ensembl; ENSRNOT00000067490; ENSRNOP00000059795; ENSRNOG00000069087.
DR   GeneID; 362249; -.
DR   GeneID; 652928; -.
DR   KEGG; rno:362249; -.
DR   CTD; 10137; -.
DR   CTD; 8904; -.
DR   RGD; 1311148; Cpne1.
DR   eggNOG; KOG1327; Eukaryota.
DR   GeneTree; ENSGT00940000162210; -.
DR   HOGENOM; CLU_020452_3_2_1; -.
DR   OMA; GWAPVKL; -.
DR   OrthoDB; 1067545at2759; -.
DR   Reactome; R-RNO-1483206; Glycerophospholipid biosynthesis.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   PRO; PR:D4A1R8; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Proteomes; UP000234681; Chromosome 3.
DR   Bgee; ENSRNOG00000046990; Expressed in spleen and 18 other tissues.
DR   Genevisible; D4A1R8; RN.
DR   GO; GO:0016235; C:aggresome; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR   GO; GO:0004175; F:endopeptidase activity; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0051059; F:NF-kappaB binding; ISO:RGD.
DR   GO; GO:0001786; F:phosphatidylserine binding; ISO:RGD.
DR   GO; GO:0071277; P:cellular response to calcium ion; ISO:RGD.
DR   GO; GO:0043392; P:negative regulation of DNA binding; ISO:RGD.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR   GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISO:RGD.
DR   GO; GO:1990138; P:neuron projection extension; ISO:RGD.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:RGD.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
DR   GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; ISO:RGD.
DR   GO; GO:0006508; P:proteolysis; ISO:RGD.
DR   GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR   CDD; cd04047; C2B_Copine; 1.
DR   CDD; cd01459; vWA_copine_like; 1.
DR   Gene3D; 2.60.40.150; -; 2.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR037768; C2B_Copine.
DR   InterPro; IPR045052; Copine.
DR   InterPro; IPR010734; Copine_C.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR10857; PTHR10857; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF07002; Copine; 1.
DR   SMART; SM00239; C2; 2.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF49562; SSF49562; 2.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   PROSITE; PS50004; C2; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Calcium; Cell membrane; Cytoplasm; Differentiation; Membrane;
KW   Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..536
FT                   /note="Copine-1"
FT                   /id="PRO_0000434560"
FT   DOMAIN          1..113
FT                   /note="C2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          122..244
FT                   /note="C2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          282..484
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   BINDING         21
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         21
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         27
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         79
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         79
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         81
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         81
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         91
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         152
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         152
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         158
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         213
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         213
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         215
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         215
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         221
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   MOD_RES         170
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99829"
SQ   SEQUENCE   536 AA;  58844 MW;  772EF9E3E44009D4 CRC64;
     MAHCVTLVQL SVSCDHLIDK DIGSKSDPLC VLLQDVGGAW AELCRTERVR NCSSPAFSKT
     LQIEYYFETV QKLRFGIYDI DNKTPELGDD DFLGGAECSL GQIVSSQTLT LPLMLKPGKP
     AGRGTITVSA QELKDSRVVT MEVEARNLDK KDFLGKSDPF LEFFRQGDGK WHLAYRTEVV
     KNNLNPTWKR FSVSLQHFCG GDLNTPIQVR CSDYDSDGSH DLIGTFHTTL AQLQAVPAEF
     ECIHPEKQQR KKSYKNSGTV CVKTCRVETE YSFLDYVMGG CQINFTVGVD FTGSNGDPSS
     PDSLHYLSPT GVNEYLTALW SVGSVVQDYD SDKLFPAFGF GAQVPPDWQV SHEFALNFNP
     SNPYCAGIQG IVDAYRQALP QVRLYGPTNF APIINHVARF AAQAAQQRTA SQYFVLLLLT
     DGAVTDVEAT CKAVVEASKL PMSVIIVGVG GADFEVMEQL DADGGPLRTR SGEAAARDIV
     QFVPYRRFQN APRETLAMTV LAEVPTQMVS YFKAQGWAPL KTLPAPAKGP AQAPQV
 
 
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