CPNE1_HUMAN
ID CPNE1_HUMAN Reviewed; 537 AA.
AC Q99829; E1P5Q4; Q6IBL3; Q9H243; Q9NTZ7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Copine-1 {ECO:0000305};
DE AltName: Full=Chromobindin 17 {ECO:0000303|PubMed:9430674};
DE AltName: Full=Copine I {ECO:0000303|PubMed:9430674, ECO:0000312|HGNC:HGNC:2314};
GN Name=CPNE1 {ECO:0000312|HGNC:HGNC:2314}; Synonyms=CPN1;
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 [MRNA], AND FUNCTION.
RX PubMed=9430674; DOI=10.1074/jbc.273.3.1393;
RA Creutz C.E., Tomsig J.L., Snyder S.L., Gautier M.-C., Skouri F.,
RA Beisson J., Cohen J.;
RT "The copines, a novel class of C2 domain-containing, calcium-dependent,
RT phospholipid-binding proteins conserved from Paramecium to humans.";
RL J. Biol. Chem. 273:1393-1402(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 332-537.
RA Jeon J., Sohn U.;
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND INTERACTION WITH ACTB; MYCBP2; PPP5C; RDX AND UBE2O.
RX PubMed=12522145; DOI=10.1074/jbc.m212632200;
RA Tomsig J.L., Snyder S.L., Creutz C.E.;
RT "Identification of targets for calcium signaling through the copine family
RT of proteins. Characterization of a coiled-coil copine-binding motif.";
RL J. Biol. Chem. 278:10048-10054(2003).
RN [8]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
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 [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=14674885; DOI=10.1042/bj20031654;
RA Tomsig J.L., Sohma H., Creutz C.E.;
RT "Calcium-dependent regulation of tumour necrosis factor-alpha receptor
RT signalling by copine.";
RL Biochem. J. 378:1089-1094(2004).
RN [10]
RP FUNCTION, SUBUNIT, INTERACTION WITH RELA, AND SUBCELLULAR LOCATION.
RX PubMed=18212740; DOI=10.1038/sj.onc.1211030;
RA Ramsey C.S., Yeung F., Stoddard P.B., Li D., Creutz C.E., Mayo M.W.;
RT "Copine-I represses NF-kappaB transcription by endoproteolysis of p65.";
RL Oncogene 27:3516-3526(2008).
RN [11]
RP FUNCTION.
RX PubMed=19539605; DOI=10.1016/j.bbamem.2009.06.009;
RA Creutz C.E., Edwardson J.M.;
RT "Organization and synergistic binding of copine I and annexin A1 on
RT supported lipid bilayers observed by atomic force microscopy.";
RL Biochim. Biophys. Acta 1788:1950-1961(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-171, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP SUBCELLULAR LOCATION.
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP FUNCTION, AND INDUCTION.
RX PubMed=23263657; DOI=10.1007/s10059-012-0235-7;
RA Park N., Yoo J.C., Ryu J., Hong S.G., Hwang E.M., Park J.Y.;
RT "Copine1 enhances neuronal differentiation of the hippocampal progenitor
RT HiB5 cells.";
RL Mol. Cells 34:549-554(2012).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF ASP-21; ASP-90;
RP ASP-216 AND ASP-222.
RX PubMed=25450385; DOI=10.1016/j.bbrc.2014.10.075;
RA Park N., Yoo J.C., Lee Y.S., Choi H.Y., Hong S.G., Hwang E.M., Park J.Y.;
RT "Copine1 C2 domains have a critical calcium-independent role in the
RT neuronal differentiation of hippocampal progenitor HiB5 cells.";
RL Biochem. Biophys. Res. Commun. 454:228-233(2014).
CC -!- FUNCTION: Calcium-dependent phospholipid-binding protein that plays a
CC role in calcium-mediated intracellular processes (PubMed:14674885).
CC Involved in the TNF-alpha receptor signaling pathway in a calcium-
CC dependent manner (PubMed:14674885). Exhibits calcium-dependent
CC phospholipid binding properties (PubMed:9430674, PubMed:19539605).
CC Plays a role in neuronal progenitor cell differentiation; induces
CC neurite outgrowth via a AKT-dependent signaling cascade and calcium-
CC independent manner (PubMed:23263657, PubMed:25450385). May recruit
CC target proteins to the cell membrane in a calcium-dependent manner
CC (PubMed:12522145). May function in membrane trafficking
CC (PubMed:9430674). Involved in TNF-alpha-induced NF-kappa-B
CC transcriptional repression by inducing endoprotease processing of the
CC transcription factor NF-kappa-B p65/RELA subunit (PubMed:18212740).
CC Also induces endoprotease processing of NF-kappa-B p50/NFKB1,
CC p52/NFKB2, RELB and REL (PubMed:18212740).
CC {ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:14674885,
CC ECO:0000269|PubMed:18212740, ECO:0000269|PubMed:19539605,
CC ECO:0000269|PubMed:23263657, ECO:0000269|PubMed:25450385,
CC ECO:0000269|PubMed:9430674}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBUNIT: Homodimer; homodimerizes via its C2 domains (PubMed:18212740).
CC Interacts with p65/RELA (via N-terminus); this interaction induces
CC proteolytic cleavage of p65/RELA subunit and inhibition of NF-kappa-B
CC transcriptional activity (PubMed:18212740). Interacts (via VWFA domain)
CC with ACTB, CCDC22, MYCBP2, PPP5C, RDX and UBE2O (PubMed:12522145).
CC {ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:18212740}.
CC -!- INTERACTION:
CC Q99829; Q9UPM6: LHX6; NbExp=3; IntAct=EBI-1642542, EBI-10258746;
CC Q99829; O60504: SORBS3; NbExp=3; IntAct=EBI-1642542, EBI-741237;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18212740,
CC ECO:0000269|PubMed:21087455}. Cytoplasm {ECO:0000269|PubMed:12949241,
CC ECO:0000269|PubMed:18212740, ECO:0000269|PubMed:21087455,
CC ECO:0000269|PubMed:25450385}. Cell membrane
CC {ECO:0000269|PubMed:21087455, ECO:0000269|PubMed:25450385}.
CC Note=Translocates to the cell membrane in a calcium-dependent manner
CC (PubMed:21087455, PubMed:25450385). {ECO:0000269|PubMed:21087455,
CC ECO:0000269|PubMed:25450385}.
CC -!- TISSUE SPECIFICITY: Expressed in neutrophils (at protein level)
CC (PubMed:12949241). Widely expressed. Expressed in the brain. Expressed
CC in neutrophil precursors from bone marrow and peripheral blood
CC (PubMed:12949241). {ECO:0000269|PubMed:12949241}.
CC -!- INDUCTION: Up-regulated by the inflammatory cytokine TNF-alpha
CC (PubMed:14674885). Up-regulated during neuronal progenitor cell
CC differentiation (PubMed:23263657). {ECO:0000269|PubMed:14674885,
CC ECO:0000269|PubMed:23263657}.
CC -!- DOMAIN: C2 domains are necessary for calcium-dependent cell membrane
CC association. C2 domains are necessary for neuronal progenitor cell
CC differentiation in a calcium-independent manner (PubMed:25450385).
CC {ECO:0000269|PubMed:25450385}.
CC -!- SIMILARITY: Belongs to the copine family. {ECO:0000305}.
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DR EMBL; U83246; AAC15920.1; -; mRNA.
DR EMBL; CR456790; CAG33071.1; -; mRNA.
DR EMBL; AL109827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76173.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76174.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76175.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76177.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76178.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76179.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76183.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76185.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76186.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76187.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76189.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76190.1; -; Genomic_DNA.
DR EMBL; BC001142; AAH01142.1; -; mRNA.
DR EMBL; AF314092; AAG49297.1; -; mRNA.
DR CCDS; CCDS13260.1; -.
DR RefSeq; NP_003906.2; NM_003915.5.
DR RefSeq; NP_690902.1; NM_152925.2.
DR RefSeq; NP_690903.1; NM_152926.2.
DR RefSeq; NP_690904.1; NM_152927.2.
DR RefSeq; NP_690905.1; NM_152928.2.
DR AlphaFoldDB; Q99829; -.
DR SMR; Q99829; -.
DR BioGRID; 114418; 57.
DR IntAct; Q99829; 12.
DR MINT; Q99829; -.
DR STRING; 9606.ENSP00000317257; -.
DR DrugBank; DB00277; Theophylline.
DR GlyGen; Q99829; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q99829; -.
DR MetOSite; Q99829; -.
DR PhosphoSitePlus; Q99829; -.
DR BioMuta; CPNE1; -.
DR DMDM; 10719953; -.
DR CPTAC; CPTAC-484; -.
DR CPTAC; CPTAC-485; -.
DR EPD; Q99829; -.
DR jPOST; Q99829; -.
DR MassIVE; Q99829; -.
DR MaxQB; Q99829; -.
DR PaxDb; Q99829; -.
DR PeptideAtlas; Q99829; -.
DR PRIDE; Q99829; -.
DR ProteomicsDB; 78494; -.
DR Antibodypedia; 11354; 206 antibodies from 33 providers.
DR DNASU; 8904; -.
DR Ensembl; ENST00000352393.8; ENSP00000336945.4; ENSG00000214078.13.
DR Ensembl; ENST00000397443.7; ENSP00000380585.1; ENSG00000214078.13.
DR GeneID; 8904; -.
DR KEGG; hsa:8904; -.
DR MANE-Select; ENST00000397443.7; ENSP00000380585.1; NM_152925.3; NP_690902.1.
DR UCSC; uc002xdf.4; human.
DR CTD; 8904; -.
DR DisGeNET; 8904; -.
DR GeneCards; CPNE1; -.
DR HGNC; HGNC:2314; CPNE1.
DR HPA; ENSG00000214078; Low tissue specificity.
DR MalaCards; CPNE1; -.
DR MIM; 604205; gene.
DR neXtProt; NX_Q99829; -.
DR OpenTargets; ENSG00000214078; -.
DR PharmGKB; PA26831; -.
DR VEuPathDB; HostDB:ENSG00000214078; -.
DR eggNOG; KOG1327; Eukaryota.
DR GeneTree; ENSGT00940000162210; -.
DR InParanoid; Q99829; -.
DR OMA; GWAPVKL; -.
DR OrthoDB; 1067545at2759; -.
DR PhylomeDB; Q99829; -.
DR PathwayCommons; Q99829; -.
DR Reactome; R-HSA-1483206; Glycerophospholipid biosynthesis.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q99829; -.
DR BioGRID-ORCS; 8904; 9 hits in 1074 CRISPR screens.
DR ChiTaRS; CPNE1; human.
DR GeneWiki; CPNE1; -.
DR GenomeRNAi; 8904; -.
DR Pharos; Q99829; Tbio.
DR PRO; PR:Q99829; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q99829; protein.
DR Bgee; ENSG00000214078; Expressed in granulocyte and 188 other tissues.
DR ExpressionAtlas; Q99829; baseline and differential.
DR Genevisible; Q99829; HS.
DR GO; GO:0016235; C:aggresome; IDA:HPA.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IMP:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:MGI.
DR GO; GO:0071277; P:cellular response to calcium ion; IMP:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:1990138; P:neuron projection extension; IDA:UniProtKB.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
DR GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IMP:UniProtKB.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.
DR CDD; cd04047; C2B_Copine; 1.
DR CDD; cd01459; vWA_copine_like; 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 Acetylation; Calcium; Cell membrane; Cytoplasm; Differentiation; Membrane;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..537
FT /note="Copine-1"
FT /id="PRO_0000144834"
FT DOMAIN 1..114
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 123..245
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 285..505
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 171
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 211
FT /note="Q -> R (in dbSNP:rs6579255)"
FT /id="VAR_024423"
FT VARIANT 347
FT /note="P -> R (in dbSNP:rs12481228)"
FT /id="VAR_048846"
FT VARIANT 535
FT /note="P -> L (in dbSNP:rs11543239)"
FT /id="VAR_048847"
FT MUTAGEN 21
FT /note="D->A: Inhibits translocation to the cell membrane in
FT a calcium-dependent manner and does not inhibit neuronal
FT progenitor cell differentiation; when associated with A-
FT 90."
FT /evidence="ECO:0000269|PubMed:25450385"
FT MUTAGEN 90
FT /note="D->A: Inhibits translocation to the cell membrane in
FT a calcium-dependent manner and does not inhibit neuronal
FT progenitor cell differentiation; when associated with A-
FT 21."
FT /evidence="ECO:0000269|PubMed:25450385"
FT MUTAGEN 216
FT /note="D->A: Inhibits translocation to the cell membrane in
FT a calcium-dependent manner and does not inhibit neuronal
FT progenitor cell differentiation; when associated with A-
FT 222."
FT /evidence="ECO:0000269|PubMed:25450385"
FT MUTAGEN 222
FT /note="D->A: Inhibits translocation to the cell membrane in
FT a calcium-dependent manner and does not inhibit neuronal
FT progenitor cell differentiation; when associated with A-
FT 216."
FT /evidence="ECO:0000269|PubMed:25450385"
FT CONFLICT 332..339
FT /note="SDKLFPAF -> NSARAARV (in Ref. 6; AAG49297)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="A -> V (in Ref. 2; CAG33071)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 537 AA; 59059 MW; F078D9046C2AAB06 CRC64;
MAHCVTLVQL SISCDHLIDK DIGSKSDPLC VLLQDVGGGS WAELGRTERV RNCSSPEFSK
TLQLEYRFET VQKLRFGIYD IDNKTPELRD DDFLGGAECS LGQIVSSQVL TLPLMLKPGK
PAGRGTITVS AQELKDNRVV TMEVEARNLD KKDFLGKSDP FLEFFRQGDG KWHLVYRSEV
IKNNLNPTWK RFSVPVQHFC GGNPSTPIQV QCSDYDSDGS HDLIGTFHTS LAQLQAVPAE
FECIHPEKQQ KKKSYKNSGT IRVKICRVET EYSFLDYVMG GCQINFTVGV DFTGSNGDPS
SPDSLHYLSP TGVNEYLMAL WSVGSVVQDY DSDKLFPAFG FGAQVPPDWQ VSHEFALNFN
PSNPYCAGIQ GIVDAYRQAL PQVRLYGPTN FAPIINHVAR FAAQAAHQGT ASQYFMLLLL
TDGAVTDVEA TREAVVRASN LPMSVIIVGV GGADFEAMEQ LDADGGPLHT RSGQAAARDI
VQFVPYRRFQ NAPREALAQT VLAEVPTQLV SYFRAQGWAP LKPLPPSAKD PAQAPQA
