ID   CPNE5_HUMAN             Reviewed;         593 AA.
AC   Q9HCH3; Q7Z6C8;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   27-NOV-2024, entry version 171.
DE   RecName: Full=Copine-5 {ECO:0000305};
DE   AltName: Full=Copine V {ECO:0000250|UniProtKB:Q99829, ECO:0000312|HGNC:HGNC:2318};
GN   Name=CPNE5 {ECO:0000312|HGNC:HGNC:2318};
GN   Synonyms=KIAA1599 {ECO:0000303|PubMed:10997877};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA   Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:273-281(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Lymph;
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   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=12949241; DOI=10.1189/jlb.0203083;
RA   Cowland J.B., Carter D., Bjerregaard M.D., Johnsen A.H., Borregaard N.,
RA   Lollike K.;
RT   "Tissue expression of copines and isolation of copines I and III from the
RT   cytosol of human neutrophils.";
RL   J. Leukoc. Biol. 74:379-388(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [7]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=23999003; DOI=10.1016/j.jdermsci.2013.07.010;
RA   Yoo J.C., Lim T.Y., Park J.S., Hah Y.S., Park N., Hong S.G., Park J.Y.,
RA   Yoon T.J.;
RT   "SYT14L, especially its C2 domain, is involved in regulating melanocyte
RT   differentiation.";
RL   J. Dermatol. Sci. 72:246-251(2013).
CC   -!- FUNCTION: Probable calcium-dependent phospholipid-binding protein that
CC       may play a role in calcium-mediated intracellular processes (By
CC       similarity). Plays a role in dendrite formation by melanocytes
CC       (PubMed:23999003). {ECO:0000250|UniProtKB:Q99829,
CC       ECO:0000269|PubMed:23999003}.
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: Perikaryon {ECO:0000250|UniProtKB:Q8JZW4}. Cell
CC       projection {ECO:0000250|UniProtKB:Q8JZW4}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9HCH3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9HCH3-2; Sequence=VSP_056535;
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, heart, stomach, spleen,
CC       lymph node and testis (PubMed:12949241). Expressed in melanocytes
CC       (PubMed:23999003). {ECO:0000269|PubMed:12949241,
CC       ECO:0000269|PubMed:23999003}.
CC   -!- SIMILARITY: Belongs to the copine family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB13425.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB046819; BAB13425.1; ALT_INIT; mRNA.
DR   EMBL; Z85996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX03914.1; -; Genomic_DNA.
DR   EMBL; BC053872; AAH53872.1; -; mRNA.
DR   CCDS; CCDS4825.1; -. [Q9HCH3-1]
DR   CCDS; CCDS83078.1; -. [Q9HCH3-2]
DR   RefSeq; NP_001300947.1; NM_001314018.1. [Q9HCH3-2]
DR   RefSeq; NP_001300948.1; NM_001314019.1.
DR   RefSeq; NP_001300949.1; NM_001314020.1.
DR   RefSeq; NP_065990.1; NM_020939.1. [Q9HCH3-1]
DR   AlphaFoldDB; Q9HCH3; -.
DR   SMR; Q9HCH3; -.
DR   BioGRID; 121724; 40.
DR   IntAct; Q9HCH3; 37.
DR   STRING; 9606.ENSP00000244751; -.
DR   iPTMnet; Q9HCH3; -.
DR   PhosphoSitePlus; Q9HCH3; -.
DR   BioMuta; CPNE5; -.
DR   DMDM; 13626179; -.
DR   jPOST; Q9HCH3; -.
DR   MassIVE; Q9HCH3; -.
DR   PaxDb; 9606-ENSP00000244751; -.
DR   PeptideAtlas; Q9HCH3; -.
DR   ProteomicsDB; 69394; -.
DR   ProteomicsDB; 81717; -. [Q9HCH3-1]
DR   Pumba; Q9HCH3; -.
DR   Antibodypedia; 29719; 103 antibodies from 20 providers.
DR   DNASU; 57699; -.
DR   Ensembl; ENST00000244751.7; ENSP00000244751.2; ENSG00000124772.12. [Q9HCH3-1]
DR   Ensembl; ENST00000393189.2; ENSP00000376885.2; ENSG00000124772.12. [Q9HCH3-2]
DR   GeneID; 57699; -.
DR   KEGG; hsa:57699; -.
DR   MANE-Select; ENST00000244751.7; ENSP00000244751.2; NM_020939.2; NP_065990.1.
DR   UCSC; uc003omp.2; human. [Q9HCH3-1]
DR   AGR; HGNC:2318; -.
DR   CTD; 57699; -.
DR   DisGeNET; 57699; -.
DR   GeneCards; CPNE5; -.
DR   HGNC; HGNC:2318; CPNE5.
DR   HPA; ENSG00000124772; Group enriched (brain, heart muscle).
DR   MIM; 604209; gene.
DR   neXtProt; NX_Q9HCH3; -.
DR   OpenTargets; ENSG00000124772; -.
DR   PharmGKB; PA26835; -.
DR   VEuPathDB; HostDB:ENSG00000124772; -.
DR   eggNOG; KOG1327; Eukaryota.
DR   GeneTree; ENSGT00940000156194; -.
DR   HOGENOM; CLU_020452_3_2_1; -.
DR   InParanoid; Q9HCH3; -.
DR   OMA; CHKTEYV; -.
DR   OrthoDB; 672483at2759; -.
DR   PhylomeDB; Q9HCH3; -.
DR   TreeFam; TF316419; -.
DR   PathwayCommons; Q9HCH3; -.
DR   SignaLink; Q9HCH3; -.
DR   BioGRID-ORCS; 57699; 20 hits in 1140 CRISPR screens.
DR   ChiTaRS; CPNE5; human.
DR   GenomeRNAi; 57699; -.
DR   Pharos; Q9HCH3; Tbio.
DR   PRO; PR:Q9HCH3; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9HCH3; protein.
DR   Bgee; ENSG00000124772; Expressed in cardiac muscle of right atrium and 147 other cell types or tissues.
DR   ExpressionAtlas; Q9HCH3; baseline and differential.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0071277; P:cellular response to calcium ion; IBA:GO_Central.
DR   GO; GO:1903861; P:positive regulation of dendrite extension; IDA:UniProtKB.
DR   CDD; cd04048; C2A_Copine; 1.
DR   CDD; cd04047; C2B_Copine; 1.
DR   CDD; cd01459; vWA_copine_like; 1.
DR   FunFam; 2.60.40.150:FF:000117; copine-5 isoform X1; 1.
DR   FunFam; 2.60.40.150:FF:000013; copine-9 isoform X1; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 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; COPINE; 1.
DR   PANTHER; PTHR10857:SF51; COPINE-5; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF07002; Copine; 1.
DR   SMART; SM00239; C2; 2.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50234; VWFA; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell projection; Differentiation;
KW   Metal-binding; Phosphoprotein; Proteomics identification;
KW   Reference proteome; Repeat.
FT   CHAIN           1..593
FT                   /note="Copine-5"
FT                   /id="PRO_0000144843"
FT   DOMAIN          2..134
FT                   /note="C2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          161..284
FT                   /note="C2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          328..554
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   REGION          562..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..583
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         38
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         38
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         44
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         98
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         98
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         100
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         100
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         100
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         103
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         108
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         110
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         110
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         192
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         192
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         198
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         254
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         254
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         256
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         256
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         262
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         103
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JZW4"
FT   MOD_RES         140
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JZW4"
FT   VAR_SEQ         1..292
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056535"
FT   VARIANT         33
FT                   /note="N -> S (in dbSNP:rs3734334)"
FT                   /id="VAR_020358"
FT   VARIANT         582
FT                   /note="R -> H (in dbSNP:rs3830138)"
FT                   /id="VAR_021954"
SQ   SEQUENCE   593 AA;  65734 MW;  7C470A51B70A5162 CRC64;
     MEQPEDMASL SEFDSLAGSI PATKVEITVS CRNLLDKDMF SKSDPLCVMY TQGMENKQWR
     EFGRTEVIDN TLNPDFVRKF IVDYFFEEKQ NLRFDLYDVD SKSPDLSKHD FLGQAFCTLG
     EIVGSPGSRL EKPLTIGAFS LNSRTGKPMP AVSNGGVPGK KCGTIILSAE ELSNCRDVAT
     MQFCANKLDK KDFFGKSDPF LVFYRSNEDG TFTICHKTEV MKNTLNPVWQ TFSIPVRALC
     NGDYDRTIKV EVYDWDRDGS HDFIGEFTTS YRELARGQSQ FNIYEVVNPK KKMKKKKYVN
     SGTVTLLSFA VESECTFLDY IKGGTQINFT VAIDFTASNG NPSQSTSLHY MSPYQLNAYA
     LALTAVGEII QHYDSDKMFP ALGFGAKLPP DGRVSHEFPL NGNQENPSCC GIDGILEAYH
     RSLRTVQLYG PTNFAPVVTH VARNAAAVQD GSQYSVLLII TDGVISDMAQ TKEAIVNAAK
     LPMSIIIVGV GQAEFDAMVE LDGDDVRISS RGKLAERDIV QFVPFRDYVD RTGNHVLSMA
     RLARDVLAEI PDQLVSYMKA QGIRPRPPPA APTHSPSQSP ARTPPASPLH THI
//