CPNE7_MOUSE
ID CPNE7_MOUSE Reviewed; 557 AA.
AC Q0VE82;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Copine-7 {ECO:0000305};
DE AltName: Full=Copine VII {ECO:0000250|UniProtKB:Q99829, ECO:0000312|MGI:MGI:2142747};
GN Name=Cpne7 {ECO:0000312|MGI:MGI:2142747};
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] {ECO:0000312|EMBL:AAI19329.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAI19329.1};
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Calcium-dependent phospholipid-binding protein that may play
CC a role in calcium-mediated intracellular processes.
CC {ECO:0000250|UniProtKB:Q99829}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UBL6}. Nucleus
CC {ECO:0000250|UniProtKB:Q9UBL6}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9UBL6}. Note=Translocates to the cell membrane
CC in a calcium-dependent manner. {ECO:0000250|UniProtKB:Q9UBL6}.
CC -!- DOMAIN: The C2 domain 1 is not necessary for calcium-mediated
CC translocation and association to the plasma membrane. The C2 domain 2
CC is necessary for calcium-mediated translocation and association to the
CC plasma membrane. {ECO:0000250|UniProtKB:H1UBN0}.
CC -!- SIMILARITY: Belongs to the copine family. {ECO:0000305}.
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DR EMBL; BC119328; AAI19329.1; -; mRNA.
DR EMBL; BC137595; AAI37596.1; -; mRNA.
DR CCDS; CCDS22748.1; -.
DR RefSeq; NP_733785.1; NM_170684.2.
DR AlphaFoldDB; Q0VE82; -.
DR SMR; Q0VE82; -.
DR BioGRID; 221837; 6.
DR IntAct; Q0VE82; 1.
DR STRING; 10090.ENSMUSP00000042159; -.
DR iPTMnet; Q0VE82; -.
DR PhosphoSitePlus; Q0VE82; -.
DR jPOST; Q0VE82; -.
DR MaxQB; Q0VE82; -.
DR PaxDb; Q0VE82; -.
DR PeptideAtlas; Q0VE82; -.
DR PRIDE; Q0VE82; -.
DR ProteomicsDB; 278019; -.
DR Antibodypedia; 30877; 64 antibodies from 21 providers.
DR DNASU; 102278; -.
DR Ensembl; ENSMUST00000037900; ENSMUSP00000042159; ENSMUSG00000034796.
DR GeneID; 102278; -.
DR KEGG; mmu:102278; -.
DR UCSC; uc009nuf.1; mouse.
DR CTD; 27132; -.
DR MGI; MGI:2142747; Cpne7.
DR VEuPathDB; HostDB:ENSMUSG00000034796; -.
DR eggNOG; KOG1327; Eukaryota.
DR GeneTree; ENSGT00940000160442; -.
DR HOGENOM; CLU_020452_4_0_1; -.
DR InParanoid; Q0VE82; -.
DR OMA; HCSIGSQ; -.
DR OrthoDB; 1067545at2759; -.
DR PhylomeDB; Q0VE82; -.
DR TreeFam; TF316419; -.
DR Reactome; R-MMU-1483206; Glycerophospholipid biosynthesis.
DR BioGRID-ORCS; 102278; 5 hits in 77 CRISPR screens.
DR PRO; PR:Q0VE82; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q0VE82; protein.
DR Bgee; ENSMUSG00000034796; Expressed in subiculum and 106 other tissues.
DR Genevisible; Q0VE82; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071277; P:cellular response to calcium ion; ISO:MGI.
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.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Cytoplasm; Membrane; Metal-binding; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..557
FT /note="Copine-7"
FT /id="PRO_0000375983"
FT DOMAIN 1..128
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 135..263
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 306..505
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
SQ SEQUENCE 557 AA; 61891 MW; 8CD71A284EE112C4 CRC64;
MSGDSERAVA PGVVPAPCAS KVELRLSCRH LLDRDPLTKS DPSVVLLQQA QGQWLQVDRT
EVVKSSLHPV FSKVFTVDYY FEGVQKLRFE VYDTHGPSGL TCQDDDFLGG MECTLGQIVA
QKKMTRPLLL RFGRNAGKST ITVIAEDISG NNGYVELSFQ ARKLDDKDLF SKSDPFLELY
RVNDDGSEQL VYRTEVVKNN LNPVWEPFKV SLNSLCSCEE TRPLKCLVWD YDSRGKHDFI
GDFTTTFAEM QKAFEEEQQA QWDCVNAKYK QKKRNYKNSG VVILADLKLH RVHSFLDYIM
GGCQIHCTVA IDFTASNGDP RNSCSLHHIN PYQPNEYLRA LVAVGEVCQD YDSDKRFSAL
GFGARIPPKY EVSHDFAINF NPEDDECEGI QGVVEAYQNC LPKVQLYGPT NVAPIISKVA
RMAAAEESTG EASQYYILLI LTDGVVTDMS DTREAIVRAS HLPMSVIIVG VGNADFTDMQ
ILDGDDGVLR SPRGEPALRD IVQFVPFREL KNASPAALAK CVLAEVPKQV VEYYSHKELP
PRSLGAQTGE AAASSAP
