CPNE1_BOVIN
ID CPNE1_BOVIN Reviewed; 537 AA.
AC Q08DB4;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Copine-1 {ECO:0000305};
DE AltName: Full=Copine I {ECO:0000250|UniProtKB:Q99829};
GN Name=CPNE1 {ECO:0000250|UniProtKB:Q99829};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI23846.1};
RC TISSUE=Fetal skin {ECO:0000312|EMBL:AAI23846.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PARTIAL PROTEIN SEQUENCE, SUBUNIT, AND 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, spleen, muscle, testis, adrenal
CC (at protein level) (PubMed:11123945). {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; DAAA02036525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC123845; AAI23846.1; -; mRNA.
DR RefSeq; NP_001070408.1; NM_001076940.1.
DR AlphaFoldDB; Q08DB4; -.
DR SMR; Q08DB4; -.
DR STRING; 9913.ENSBTAP00000009138; -.
DR PaxDb; Q08DB4; -.
DR PRIDE; Q08DB4; -.
DR Ensembl; ENSBTAT00000009138; ENSBTAP00000009138; ENSBTAG00000006955.
DR Ensembl; ENSBTAT00000066589; ENSBTAP00000071076; ENSBTAG00000006955.
DR Ensembl; ENSBTAT00000084477; ENSBTAP00000059671; ENSBTAG00000006955.
DR GeneID; 615677; -.
DR KEGG; bta:615677; -.
DR CTD; 8904; -.
DR VEuPathDB; HostDB:ENSBTAG00000006955; -.
DR VGNC; VGNC:27658; CPNE1.
DR eggNOG; KOG1327; Eukaryota.
DR GeneTree; ENSGT00940000162210; -.
DR HOGENOM; CLU_020452_3_2_1; -.
DR InParanoid; Q08DB4; -.
DR OMA; GWAPVKL; -.
DR OrthoDB; 1067545at2759; -.
DR TreeFam; TF316419; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000006955; Expressed in blood and 107 other tissues.
DR ExpressionAtlas; Q08DB4; baseline and differential.
DR GO; GO:0016235; C:aggresome; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0051059; F:NF-kappaB binding; IEA:Ensembl.
DR GO; GO:0001786; F:phosphatidylserine binding; IEA:Ensembl.
DR GO; GO:0071277; P:cellular response to calcium ion; IBA:GO_Central.
DR GO; GO:0043392; P:negative regulation of DNA binding; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:1990138; P:neuron projection extension; IEA:Ensembl.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:Ensembl.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
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;
KW Direct protein sequencing; Membrane; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..537
FT /note="Copine-1"
FT /id="PRO_0000434559"
FT DOMAIN 1..114
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 123..245
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 285..505
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 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 171
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99829"
SQ SEQUENCE 537 AA; 58923 MW; BE9B50220A6E9CB7 CRC64;
MAHCVTLVQL SVSCDHLIDK DIGSKSDPLC VLLQDVGGGN WTELGRTERV QNCSSPEFSK
TLQLEYHFET VQKLRFGIYD IDNKTPELGD DDFLGGAECS LGQIVSSRML TLPLMLKPGK
PAGRGTITVS AQELKDNRVV TMEVEARNLD KKDFLGKSDP FLEFFRQGDG KWHLAYRSEV
IKNNLNPTWK RFSVPLQHFC GGDASTPIQV RCSDYDSDGS HDLIGTFHTS LAQLQAAPAE
FECIHPEKQQ KKKSYKNSGT ICVKMCQVET EHSFLDYVMG GCQINFTVGV DFTGSNGDPS
SPDSLHYLSP TGVNEYLTAL WSVGSVVQDY DSDKLFPAFG FGAQVPPDWQ VSHEFALNFN
PSNPFCAGIQ GIVDAYRQAL PQVRLFGPTN FAPIINHVAR FAAQAANQRN ASQYFVLLLL
TDGAVTDVEA TREAVVRASY LPMSVIIVGV GCADFEAMEQ LDADGGPLHT RSGEAAARDI
VQFVPYRRFQ NAPREALAQT VLAEVPTQLV SYFRAQGWAP FKPPPPAAKG PAQAPQA
