CPNE7_RAT
ID CPNE7_RAT Reviewed; 556 AA.
AC H1UBN0;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Copine-7 {ECO:0000305};
DE AltName: Full=Copine VII {ECO:0000250|UniProtKB:Q99829, ECO:0000312|RGD:1307466};
GN Name=Cpne7 {ECO:0000312|RGD:1307466};
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 {ECO:0000312|EMBL:CAO00508.1};
RN [1] {ECO:0000312|EMBL:CAO00508.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar {ECO:0000312|EMBL:CAO00508.1};
RC TISSUE=Brain {ECO:0000312|EMBL:CAO00508.1};
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 SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF ASP-33; ASP-35; ASP-93;
RP ASP-104; ASP-168; ASP-174; ASP-230 AND ASP-232.
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 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:0000269|PubMed:26175110}. Note=Translocates to the cell membrane
CC in a calcium-dependent manner. {ECO:0000269|PubMed:26175110}.
CC -!- DOMAIN: The C2 domain 1 is not necessary for calcium-mediated
CC translocation and association to the plasma membrane (PubMed:26175110).
CC The C2 domain 2 is necessary for calcium-mediated translocation and
CC association to the plasma membrane (PubMed:26175110).
CC {ECO:0000269|PubMed:26175110}.
CC -!- SIMILARITY: Belongs to the copine family. {ECO:0000305}.
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DR EMBL; AM747283; CAO00508.1; -; mRNA.
DR EMBL; AC119635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006255836.1; XM_006255774.3.
DR AlphaFoldDB; H1UBN0; -.
DR SMR; H1UBN0; -.
DR jPOST; H1UBN0; -.
DR PRIDE; H1UBN0; -.
DR Ensembl; ENSRNOT00000077701; ENSRNOP00000068558; ENSRNOG00000015397.
DR GeneID; 361433; -.
DR CTD; 27132; -.
DR RGD; 1307466; Cpne7.
DR GeneTree; ENSGT00940000160442; -.
DR HOGENOM; CLU_020452_4_0_1; -.
DR OMA; HCSIGSQ; -.
DR OrthoDB; 1067545at2759; -.
DR Reactome; R-RNO-1483206; Glycerophospholipid biosynthesis.
DR PRO; PR:H1UBN0; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000015397; Expressed in spleen and 19 other tissues.
DR ExpressionAtlas; H1UBN0; baseline and differential.
DR Genevisible; H1UBN0; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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:RGD.
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..556
FT /note="Copine-7"
FT /id="PRO_0000434561"
FT DOMAIN 1..128
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 135..262
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 305..504
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 536..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT MUTAGEN 33
FT /note="D->N: Does not inhibit calcium-dependent
FT translocation to the cell membrane; when associated with N-
FT 35; N-93 and N-104."
FT /evidence="ECO:0000269|PubMed:26175110"
FT MUTAGEN 35
FT /note="D->N: Does not inhibit calcium-dependent
FT translocation to the cell membrane; when associated with N-
FT 33; N-93 and N-104."
FT /evidence="ECO:0000269|PubMed:26175110"
FT MUTAGEN 93
FT /note="D->N: Does not inhibit calcium-dependent
FT translocation to the cell membrane; when associated with N-
FT 33; N-35 and N-104."
FT /evidence="ECO:0000269|PubMed:26175110"
FT MUTAGEN 104
FT /note="D->N: Does not inhibit calcium-dependent
FT translocation to the cell membrane; when associated with N-
FT 33; N-35 and N-93."
FT /evidence="ECO:0000269|PubMed:26175110"
FT MUTAGEN 168
FT /note="D->N: Inhibits strongly calcium-dependent
FT translocation to the cell membrane. Inhibits strongly
FT calcium-dependent translocation to the cell membrane; when
FT associated with N-173. Leads to the constitutive (calcium-
FT independent) attachment to the cell membrane; when
FT associated with N-174; N-230 and N-232."
FT /evidence="ECO:0000269|PubMed:26175110"
FT MUTAGEN 174
FT /note="D->N: Inhibits strongly calcium-dependent
FT translocation to the cell membrane. Inhibits strongly
FT calcium-dependent translocation to the cell membrane; when
FT associated with N-167. Leads to the constitutive (calcium-
FT independent) attachment to the cell membrane; when
FT associated with N-167; N-230 and N-232."
FT /evidence="ECO:0000269|PubMed:26175110"
FT MUTAGEN 230
FT /note="D->N: Inhibits strongly calcium-dependent
FT translocation to the cell membrane; when associated with N-
FT 231. Leads to the constitutive (calcium-independent)
FT attachment to the cell membrane; when associated with N-
FT 167; N-174 and N-232."
FT /evidence="ECO:0000269|PubMed:26175110"
FT MUTAGEN 232
FT /note="D->N: Does not inhibit calcium-dependent
FT translocation to the cell membrane. Inhibits strongly
FT calcium-dependent translocation to the cell membrane; when
FT associated with N-229. Leads to the constitutive (calcium-
FT independent) attachment to the cell membrane; when
FT associated with N-168; N-174 and N-230."
FT /evidence="ECO:0000269|PubMed:26175110"
SQ SEQUENCE 556 AA; 61978 MW; 5CEB5CED22B6197A CRC64;
MSGDSERTVA PGVVPAPCAS KVELRLSCRH LLDRDPLTKS DPSVVLLQQA QGQWLQVDRT
EVVKSSLHPV FSKVFTMDYY FEEVQKLRFE VYDTHGPSGL SCQDDDFLGG MECTLGQIVA
QKKMTRPLLL RFGRNAGKST ITVIAEDISG NNGYVELSFQ ARKLDDKDLF SKSDPFLELY
RVNDDGSEQL VYRTEVVKNN LNPVWEPFKV SLNSLCSCEE TRPLKCLVWD YDSRGKHDFI
GDFTTTFAEM QKAFEEEQAQ WDCVNAKYKQ KKRNYKNSGV VILADLKLHR VHSFLDYIMG
GCQIHCTVAI DFTASNGDPR NSCSLHHINP YQPNEYLRAL VAVGEVCQDY DSDKRFSALG
FGARIPPKYE VSHDFAINFN PEDDECEGIQ GVVEAYQNCL PRVQLYGPTN VAPIISKVAR
MAAAEERTGE ASQYYILLIL TDGVVTDMSD TREAIVRASH LPMSVIIVGV GNADFTDMQI
LDGDDGILRS PRGEPALRDI VQFVPFRELK NASPAALAKC VLAEVPKQVV EYYSHKDLPP
RSLGGQTGEA GPSSAP
