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 24-JAN-2024, entry version 93.
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 GlyGen; D4A1R8; 1 site, 1 O-linked glycan (1 site).
DR PhosphoSitePlus; D4A1R8; -.
DR jPOST; D4A1R8; -.
DR PaxDb; 10116-ENSRNOP00000026657; -.
DR PeptideAtlas; D4A1R8; -.
DR Ensembl; ENSRNOT00000067490.4; ENSRNOP00000059795.2; ENSRNOG00000069087.1.
DR GeneID; 362249; -.
DR KEGG; rno:362249; -.
DR AGR; RGD:1311148; -.
DR AGR; RGD:1594333; -.
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 InParanoid; D4A1R8; -.
DR OrthoDB; 5402241at2759; -.
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 cell types or tissues.
DR Genevisible; D4A1R8; RN.
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: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:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:1901223; P:negative regulation of non-canonical NF-kappaB signal transduction; 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 phosphatidylinositol 3-kinase/protein kinase B signal transduction; 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 canonical NF-kappaB signal transduction; ISO:RGD.
DR CDD; cd04048; C2A_Copine; 1.
DR CDD; cd04047; C2B_Copine; 1.
DR CDD; cd01459; vWA_copine_like; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 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; COPINE; 1.
DR PANTHER; PTHR10857:SF2; COPINE-1; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF07002; Copine; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF53300; vWA-like; 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
//
