CPNE2_MOUSE
ID CPNE2_MOUSE Reviewed; 548 AA.
AC P59108; Q8K1D7;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Copine-2 {ECO:0000305};
DE AltName: Full=Copine II {ECO:0000250|UniProtKB:Q99829, ECO:0000312|MGI:MGI:2387578};
GN Name=Cpne2 {ECO:0000312|MGI:MGI:2387578};
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, and FVB/N; TISSUE=Liver, and Mammary tumor;
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, Kidney, and Spleen;
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=21087455; DOI=10.1111/j.1742-4658.2010.07935.x;
RA Perestenko P.V., Pooler A.M., Noorbakhshnia M., Gray A., Bauccio C.,
RA Jeffrey McIlhinney R.A.;
RT "Copines-1, -2, -3, -6 and -7 show different calcium-dependent
RT intracellular membrane translocation and targeting.";
RL FEBS J. 277:5174-5189(2010).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF ASP-37; ASP-39;
RP ASP-97; ASP-99; ASP-170; ASP-176; ASP-232 AND ASP-234.
RX PubMed=26175110; DOI=10.1111/febs.13370;
RA Perestenko P., Watanabe M., Beusnard-Bee T., Guna P., McIlhinney J.;
RT "The second C2-domain of copines -2, -6 and -7 is responsible for their
RT calcium-dependent membrane association.";
RL FEBS J. 282:3722-3736(2015).
CC -!- FUNCTION: Calcium-dependent phospholipid-binding protein that plays a
CC role in calcium-mediated intracellular processes. Exhibits calcium-
CC dependent cell membrane binding properties (PubMed:21087455,
CC PubMed:26175110). {ECO:0000269|PubMed:21087455,
CC ECO:0000269|PubMed:26175110}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00041};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21087455,
CC ECO:0000269|PubMed:26175110}. Nucleus {ECO:0000269|PubMed:21087455,
CC ECO:0000269|PubMed:26175110}. Cell membrane
CC {ECO:0000269|PubMed:21087455, ECO:0000269|PubMed:26175110}.
CC Note=Translocates to the cell membrane and the nucleus in a calcium-
CC dependent manner (PubMed:21087455, PubMed:26175110). Colocalizes with
CC CD2 at the cell membrane (PubMed:21087455).
CC {ECO:0000269|PubMed:21087455, ECO:0000269|PubMed:26175110}.
CC -!- DOMAIN: The C2 domain 2, but not the C2 domain 1, is necessary for
CC calcium-mediated membrane association (PubMed:21087455,
CC PubMed:26175110). The linker region is necessary for calcium-dependent
CC cell membrane association (PubMed:21087455).
CC {ECO:0000269|PubMed:21087455, ECO:0000269|PubMed:26175110}.
CC -!- SIMILARITY: Belongs to the copine family. {ECO:0000305}.
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DR EMBL; BC022128; AAH22128.2; -; mRNA.
DR EMBL; BC031801; AAH31801.1; -; mRNA.
DR CCDS; CCDS22543.1; -.
DR RefSeq; NP_705727.1; NM_153507.2.
DR AlphaFoldDB; P59108; -.
DR SMR; P59108; -.
DR BioGRID; 231541; 3.
DR IntAct; P59108; 2.
DR MINT; P59108; -.
DR STRING; 10090.ENSMUSP00000045755; -.
DR iPTMnet; P59108; -.
DR PhosphoSitePlus; P59108; -.
DR SwissPalm; P59108; -.
DR EPD; P59108; -.
DR jPOST; P59108; -.
DR MaxQB; P59108; -.
DR PaxDb; P59108; -.
DR PeptideAtlas; P59108; -.
DR PRIDE; P59108; -.
DR ProteomicsDB; 285292; -.
DR Antibodypedia; 63170; 62 antibodies from 18 providers.
DR DNASU; 234577; -.
DR Ensembl; ENSMUST00000048653; ENSMUSP00000045755; ENSMUSG00000034361.
DR GeneID; 234577; -.
DR KEGG; mmu:234577; -.
DR UCSC; uc009mwm.1; mouse.
DR CTD; 221184; -.
DR MGI; MGI:2387578; Cpne2.
DR VEuPathDB; HostDB:ENSMUSG00000034361; -.
DR eggNOG; KOG1327; Eukaryota.
DR GeneTree; ENSGT00940000157653; -.
DR HOGENOM; CLU_020452_3_2_1; -.
DR InParanoid; P59108; -.
DR OMA; APMKDAH; -.
DR OrthoDB; 1067545at2759; -.
DR PhylomeDB; P59108; -.
DR TreeFam; TF316419; -.
DR BioGRID-ORCS; 234577; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Cpne2; mouse.
DR PRO; PR:P59108; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P59108; protein.
DR Bgee; ENSMUSG00000034361; Expressed in granulocyte and 156 other tissues.
DR ExpressionAtlas; P59108; baseline and differential.
DR Genevisible; P59108; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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; IMP:UniProtKB.
DR CDD; cd04047; C2B_Copine; 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 Calcium; Cell membrane; Cytoplasm; Membrane; Metal-binding; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..548
FT /note="Copine-2"
FT /id="PRO_0000144837"
FT DOMAIN 6..131
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 138..263
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 305..507
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 247..304
FT /note="Linker region"
FT /evidence="ECO:0000269|PubMed:21087455"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 99
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 99
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 99
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 240
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MUTAGEN 37
FT /note="D->N: Does not inhibit calcium-dependent
FT translocation to the cell membrane; when associated with N-
FT 39; N-97 and N-99."
FT /evidence="ECO:0000269|PubMed:26175110"
FT MUTAGEN 39
FT /note="D->N: Does not inhibit calcium-dependent
FT translocation to the cell membrane; when associated with N-
FT 37; N-97 and N-99."
FT /evidence="ECO:0000269|PubMed:26175110"
FT MUTAGEN 97
FT /note="D->N: Does not inhibit calcium-dependent
FT translocation to the cell membrane; when associated with N-
FT 37; N-39 and N-99."
FT /evidence="ECO:0000269|PubMed:26175110"
FT MUTAGEN 99
FT /note="D->N: Does not inhibit calcium-dependent
FT translocation to the cell membrane; when associated with N-
FT 37; N-39 and N-97."
FT /evidence="ECO:0000269|PubMed:26175110"
FT MUTAGEN 170
FT /note="D->N: Leads to a reduction in the amount of calcium-
FT dependent translocation to the cell membrane. Leads to the
FT constitutive (calcium-independent) attachment to the cell
FT membrane; when associated with N-176; N-232 and N-234."
FT /evidence="ECO:0000269|PubMed:26175110"
FT MUTAGEN 176
FT /note="D->N: Does not inhibit calcium-dependent
FT translocation to the cell membrane. Leads to the
FT constitutive (calcium-independent) attachment to the cell
FT membrane; when associated with N-170; N-232 and N-234."
FT /evidence="ECO:0000269|PubMed:26175110"
FT MUTAGEN 232
FT /note="D->N: Leads to a reduction in the amount of calcium-
FT dependent translocation to the cell membrane. Leads to the
FT constitutive (calcium-independent) attachment to the cell
FT membrane; when associated with N-170; N-176 and N-234."
FT /evidence="ECO:0000269|PubMed:26175110"
FT MUTAGEN 234
FT /note="D->N: Leads to a reduction in the amount of calcium-
FT dependent translocation to the cell membrane. Leads to the
FT constitutive (calcium-independent) attachment to the cell
FT membrane; when associated with N-170; N-176 and N-232."
FT /evidence="ECO:0000269|PubMed:26175110"
FT CONFLICT 435
FT /note="Missing (in Ref. 1; AAH22128)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 61036 MW; 796F26124D2A0E13 CRC64;
MAYIPDGGAP TAGAIPLGSQ CCVCKVELSV SGQNLLDRDV TSKSDPFCVL FIEDNGRWME
FDRTETAVNN LNPAFSKKFV LDYHFEEVQK LKFALFDQDK SSAQLDEHDF LGQFSCSLGT
IVSSKKITRP LLLMNDKPAG KGVITIAAQE LSDNRVITLS LAGRKLDKKD LFGKSDPFLE
FYKPGDDGKW MLVHRTEVIK YTLDPVWKPF TVPLVSLCDG DLEKPIQVMC YDYDSNGGHD
FIGEFQTSVL QMSEARDGVP LEIECINPKK QRKKKSYKNS GIIILRSCKI HRNYSFLDYI
LGGCQLMFTV GIDFTASNGN PLDPSSLHYI NPMGTNEYLS AIWAVGQIIQ DYDSDKMFPA
LGFGAQLPPD WKVSHEFAIN FNPTNPFCSG VDGIAQAYSA CLPHIRFYGP TNFSPIVNHV
ARFAAQATQQ QTATQYFILL IITDGVISDM EETRHAVVQA SKLPMSIIIV GVGNADFAAM
EFLDGDNRRL RSHTGEEAAR DIVQFVPFRE FRNAAKETLA KAVLAELPQQ VVQYFKHKNL
PPTNSEPA
