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-MAR-2024, entry version 167.
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; 39.
DR IntAct; Q9HCH3; 32.
DR STRING; 9606.ENSP00000244751; -.
DR iPTMnet; Q9HCH3; -.
DR PhosphoSitePlus; Q9HCH3; -.
DR BioMuta; CPNE5; -.
DR DMDM; 13626179; -.
DR jPOST; Q9HCH3; -.
DR MassIVE; Q9HCH3; -.
DR MaxQB; Q9HCH3; -.
DR PaxDb; 9606-ENSP00000244751; -.
DR PeptideAtlas; Q9HCH3; -.
DR ProteomicsDB; 69394; -.
DR ProteomicsDB; 81717; -. [Q9HCH3-1]
DR Pumba; Q9HCH3; -.
DR Antibodypedia; 29719; 111 antibodies from 21 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 Genevisible; Q9HCH3; HS.
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 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; 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
//
