CPNE1_MOUSE
ID CPNE1_MOUSE Reviewed; 536 AA.
AC Q8C166; Q925K4; Q925K5;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Copine-1 {ECO:0000305};
DE AltName: Full=Copine I {ECO:0000250|UniProtKB:Q99829, ECO:0000312|MGI:MGI:2386621};
GN Name=Cpne1 {ECO:0000312|MGI:MGI:2386621};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-454.
RC STRAIN=ILS, and ISS;
RX 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 within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-170, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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 -!- 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; AK028882; BAC26170.1; -; mRNA.
DR EMBL; BC057554; AAH57554.1; -; mRNA.
DR EMBL; AF332057; AAK56086.1; -; mRNA.
DR EMBL; AF332058; AAK56087.1; -; mRNA.
DR CCDS; CCDS16960.1; -.
DR RefSeq; NP_733467.1; NM_170588.3.
DR RefSeq; NP_733469.1; NM_170590.3.
DR AlphaFoldDB; Q8C166; -.
DR SMR; Q8C166; -.
DR BioGRID; 234468; 8.
DR STRING; 10090.ENSMUSP00000105237; -.
DR iPTMnet; Q8C166; -.
DR PhosphoSitePlus; Q8C166; -.
DR SwissPalm; Q8C166; -.
DR REPRODUCTION-2DPAGE; Q8C166; -.
DR EPD; Q8C166; -.
DR jPOST; Q8C166; -.
DR MaxQB; Q8C166; -.
DR PaxDb; Q8C166; -.
DR PeptideAtlas; Q8C166; -.
DR PRIDE; Q8C166; -.
DR ProteomicsDB; 278018; -.
DR Antibodypedia; 11354; 206 antibodies from 33 providers.
DR DNASU; 266692; -.
DR Ensembl; ENSMUST00000109607; ENSMUSP00000105236; ENSMUSG00000074643.
DR Ensembl; ENSMUST00000109608; ENSMUSP00000105237; ENSMUSG00000074643.
DR GeneID; 266692; -.
DR KEGG; mmu:266692; -.
DR UCSC; uc008nmf.2; mouse.
DR CTD; 8904; -.
DR MGI; MGI:2386621; Cpne1.
DR VEuPathDB; HostDB:ENSMUSG00000074643; -.
DR eggNOG; KOG1327; Eukaryota.
DR GeneTree; ENSGT00940000162210; -.
DR HOGENOM; CLU_020452_3_2_1; -.
DR InParanoid; Q8C166; -.
DR OMA; GWAPVKL; -.
DR OrthoDB; 1067545at2759; -.
DR PhylomeDB; Q8C166; -.
DR TreeFam; TF316419; -.
DR Reactome; R-MMU-1483206; Glycerophospholipid biosynthesis.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 266692; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Cpne1; mouse.
DR PRO; PR:Q8C166; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8C166; protein.
DR Bgee; ENSMUSG00000074643; Expressed in granulocyte and 64 other tissues.
DR ExpressionAtlas; Q8C166; baseline and differential.
DR Genevisible; Q8C166; MM.
DR GO; GO:0016235; C:aggresome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0051059; F:NF-kappaB binding; ISO:MGI.
DR GO; GO:0001786; F:phosphatidylserine binding; ISO:MGI.
DR GO; GO:0071277; P:cellular response to calcium ion; ISO:MGI.
DR GO; GO:0043392; P:negative regulation of DNA binding; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:1990138; P:neuron projection extension; ISS:UniProtKB.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR CDD; cd04047; C2B_Copine; 1.
DR CDD; cd01459; vWA_copine_like; 1.
DR Gene3D; 2.60.40.150; -; 2.
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_0000144835"
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 284..504
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:0007744|PubMed:23806337"
FT CONFLICT 43
FT /note="L -> P (in Ref. 2; AAH57554)"
FT /evidence="ECO:0000305"
FT CONFLICT 452..454
FT /note="ADF -> GHS (in Ref. 3; AAK56087)"
FT /evidence="ECO:0000305"
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
