Full text data of CPNE1
CPNE1
(CPN1)
[Confidence: low (only semi-automatic identification from reviews)]
Copine-1 (Copine I)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Copine-1 (Copine I)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q99829
ID CPNE1_HUMAN Reviewed; 537 AA.
AC Q99829; E1P5Q4; Q6IBL3; Q9H243; Q9NTZ7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1997, sequence version 1.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=Copine-1;
DE AltName: Full=Copine I;
GN Name=CPNE1; Synonyms=CPN1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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-
RT dependent, phospholipid-binding proteins conserved from Paramecium to
RT 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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-171, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [8]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May function in membrane trafficking. Exhibits calcium-
CC dependent phospholipid binding properties.
CC -!- SUBUNIT: Interacts with CCDC22 (By similarity).
CC -!- SIMILARITY: Belongs to the copine family.
CC -!- SIMILARITY: Contains 2 C2 domains.
CC -!- SIMILARITY: Contains 1 VWFA domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U83246; AAC15920.1; -; mRNA.
DR EMBL; CR456790; CAG33071.1; -; mRNA.
DR EMBL; AL109827; CAB87610.2; -; 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 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 UniGene; Hs.246413; -.
DR UniGene; Hs.700188; -.
DR ProteinModelPortal; Q99829; -.
DR IntAct; Q99829; 6.
DR MINT; MINT-4999732; -.
DR STRING; 9606.ENSP00000317257; -.
DR PhosphoSite; Q99829; -.
DR DMDM; 10719953; -.
DR PaxDb; Q99829; -.
DR PRIDE; Q99829; -.
DR DNASU; 8904; -.
DR Ensembl; ENST00000317619; ENSP00000326126; ENSG00000214078.
DR Ensembl; ENST00000352393; ENSP00000336945; ENSG00000214078.
DR Ensembl; ENST00000397443; ENSP00000380585; ENSG00000214078.
DR Ensembl; ENST00000397445; ENSP00000380587; ENSG00000214078.
DR Ensembl; ENST00000397446; ENSP00000380588; ENSG00000214078.
DR GeneID; 8904; -.
DR KEGG; hsa:8904; -.
DR UCSC; uc002xdf.3; human.
DR CTD; 8904; -.
DR GeneCards; GC20M034213; -.
DR HGNC; HGNC:2314; CPNE1.
DR MIM; 604205; gene.
DR neXtProt; NX_Q99829; -.
DR PharmGKB; PA26831; -.
DR eggNOG; NOG269302; -.
DR HOGENOM; HOG000220898; -.
DR HOVERGEN; HBG066841; -.
DR ChiTaRS; CPNE1; human.
DR GeneWiki; CPNE1; -.
DR GenomeRNAi; 8904; -.
DR NextBio; 33439; -.
DR PRO; PR:Q99829; -.
DR ArrayExpress; Q99829; -.
DR Bgee; Q99829; -.
DR CleanEx; HS_CPN1; -.
DR Genevestigator; Q99829; -.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; TAS:ProtInc.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:MGI.
DR GO; GO:0005215; F:transporter activity; TAS:ProtInc.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR010734; Copine.
DR InterPro; IPR002035; VWF_A.
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 PROSITE; PS50004; C2; 1.
DR PROSITE; PS50234; VWFA; FALSE_NEG.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Polymorphism; Reference proteome;
KW Repeat.
FT CHAIN 1 537 Copine-1.
FT /FTId=PRO_0000144834.
FT DOMAIN 1 98 C2 1.
FT DOMAIN 144 228 C2 2.
FT DOMAIN 285 505 VWFA.
FT MOD_RES 171 171 N6-acetyllysine.
FT VARIANT 211 211 Q -> R (in dbSNP:rs6579255).
FT /FTId=VAR_024423.
FT VARIANT 347 347 P -> R (in dbSNP:rs12481228).
FT /FTId=VAR_048846.
FT VARIANT 535 535 P -> L (in dbSNP:rs11543239).
FT /FTId=VAR_048847.
FT CONFLICT 332 339 SDKLFPAF -> NSARAARV (in Ref. 6;
FT AAG49297).
FT CONFLICT 367 367 A -> V (in Ref. 2; CAG33071).
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
//
ID CPNE1_HUMAN Reviewed; 537 AA.
AC Q99829; E1P5Q4; Q6IBL3; Q9H243; Q9NTZ7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1997, sequence version 1.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=Copine-1;
DE AltName: Full=Copine I;
GN Name=CPNE1; Synonyms=CPN1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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-
RT dependent, phospholipid-binding proteins conserved from Paramecium to
RT 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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-171, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [8]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May function in membrane trafficking. Exhibits calcium-
CC dependent phospholipid binding properties.
CC -!- SUBUNIT: Interacts with CCDC22 (By similarity).
CC -!- SIMILARITY: Belongs to the copine family.
CC -!- SIMILARITY: Contains 2 C2 domains.
CC -!- SIMILARITY: Contains 1 VWFA domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U83246; AAC15920.1; -; mRNA.
DR EMBL; CR456790; CAG33071.1; -; mRNA.
DR EMBL; AL109827; CAB87610.2; -; 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 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 UniGene; Hs.246413; -.
DR UniGene; Hs.700188; -.
DR ProteinModelPortal; Q99829; -.
DR IntAct; Q99829; 6.
DR MINT; MINT-4999732; -.
DR STRING; 9606.ENSP00000317257; -.
DR PhosphoSite; Q99829; -.
DR DMDM; 10719953; -.
DR PaxDb; Q99829; -.
DR PRIDE; Q99829; -.
DR DNASU; 8904; -.
DR Ensembl; ENST00000317619; ENSP00000326126; ENSG00000214078.
DR Ensembl; ENST00000352393; ENSP00000336945; ENSG00000214078.
DR Ensembl; ENST00000397443; ENSP00000380585; ENSG00000214078.
DR Ensembl; ENST00000397445; ENSP00000380587; ENSG00000214078.
DR Ensembl; ENST00000397446; ENSP00000380588; ENSG00000214078.
DR GeneID; 8904; -.
DR KEGG; hsa:8904; -.
DR UCSC; uc002xdf.3; human.
DR CTD; 8904; -.
DR GeneCards; GC20M034213; -.
DR HGNC; HGNC:2314; CPNE1.
DR MIM; 604205; gene.
DR neXtProt; NX_Q99829; -.
DR PharmGKB; PA26831; -.
DR eggNOG; NOG269302; -.
DR HOGENOM; HOG000220898; -.
DR HOVERGEN; HBG066841; -.
DR ChiTaRS; CPNE1; human.
DR GeneWiki; CPNE1; -.
DR GenomeRNAi; 8904; -.
DR NextBio; 33439; -.
DR PRO; PR:Q99829; -.
DR ArrayExpress; Q99829; -.
DR Bgee; Q99829; -.
DR CleanEx; HS_CPN1; -.
DR Genevestigator; Q99829; -.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; TAS:ProtInc.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:MGI.
DR GO; GO:0005215; F:transporter activity; TAS:ProtInc.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR010734; Copine.
DR InterPro; IPR002035; VWF_A.
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 PROSITE; PS50004; C2; 1.
DR PROSITE; PS50234; VWFA; FALSE_NEG.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Polymorphism; Reference proteome;
KW Repeat.
FT CHAIN 1 537 Copine-1.
FT /FTId=PRO_0000144834.
FT DOMAIN 1 98 C2 1.
FT DOMAIN 144 228 C2 2.
FT DOMAIN 285 505 VWFA.
FT MOD_RES 171 171 N6-acetyllysine.
FT VARIANT 211 211 Q -> R (in dbSNP:rs6579255).
FT /FTId=VAR_024423.
FT VARIANT 347 347 P -> R (in dbSNP:rs12481228).
FT /FTId=VAR_048846.
FT VARIANT 535 535 P -> L (in dbSNP:rs11543239).
FT /FTId=VAR_048847.
FT CONFLICT 332 339 SDKLFPAF -> NSARAARV (in Ref. 6;
FT AAG49297).
FT CONFLICT 367 367 A -> V (in Ref. 2; CAG33071).
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
//
MIM
604205
*RECORD*
*FIELD* NO
604205
*FIELD* TI
*604205 COPINE I; CPNE1
;;CPN1
*FIELD* TX
Molecular events at the interface of the cell membrane and cytoplasm may
read morebe regulated by proteins that attach to and detach from the membrane
surface in response to signals. Calcium-dependent membrane-binding
proteins may play such a role. To identify proteins that may underlie
membrane trafficking processes in ciliates, Creutz et al. (1998)
isolated calcium-dependent phospholipid-binding proteins from
Paramecium. They named the major protein that they obtained 'copine'
(pronounced 'ko-peen'), the French feminine noun meaning 'friend,'
because it associates like a 'companion' with lipid membranes. The 55-kD
copine protein bound phosphatidylserine in a calcium- but not
magnesium-dependent manner, but it did not bind phosphatidylcholine.
Copine promoted calcium-dependent aggregation of lipid vesicles. The
authors cloned partial cDNAs representing 2 distinct Paramecium copine
genes. By searching sequence databases for genes with sequence
similarity to the Paramecium copine genes, Creutz et al. (1998)
identified human ESTs corresponding to 5 copine genes, named copine I to
V. Two overlapping ESTs contained the complete copine I (CPNE1) coding
sequence. The deduced 537-amino acid CPNE1 protein contains 2 type II C2
domains in its N-terminal half and a domain similar to the A domain,
which is present in a number of extracellular proteins or the
extracellular portions of membrane proteins, in its C-terminal half; it
does not have a predicted signal sequence or transmembrane domains. C2
domains mediate calcium-dependent interactions with phospholipids, and
the A domain of integrins appears to mediate the binding of the integrin
to extracellular ligands. CPNE1 has a broad tissue distribution.
Recombinant CPNE1 expressed in bacteria exhibited calcium-dependent
binding to phosphatidylserine vesicles. Antibody against CPNE1 reacted
with bovine chromobindin-17, which is a 55-kD calcium-dependent
chromaffin vesicle-binding protein, and the authors concluded that
chromobindin-17 is a copine. They suggested that copines function in
membrane trafficking.
*FIELD* RF
1. Creutz, C. E.; Tomsig, J. L.; Snyder, S. L.; Gautier, M.-C.; Skouri,
F.; Beisson, J.; Cohen, J.: The copines, a novel class of C2 domain-containing,
calcium-dependent, phospholipid-binding proteins conserved from Paramecium
to humans. J. Biol. Chem. 273: 1393-1402, 1998.
*FIELD* CD
Patti M. Sherman: 9/29/1999
*FIELD* ED
mgross: 10/01/1999
mgross: 9/30/1999
psherman: 9/30/1999
*RECORD*
*FIELD* NO
604205
*FIELD* TI
*604205 COPINE I; CPNE1
;;CPN1
*FIELD* TX
Molecular events at the interface of the cell membrane and cytoplasm may
read morebe regulated by proteins that attach to and detach from the membrane
surface in response to signals. Calcium-dependent membrane-binding
proteins may play such a role. To identify proteins that may underlie
membrane trafficking processes in ciliates, Creutz et al. (1998)
isolated calcium-dependent phospholipid-binding proteins from
Paramecium. They named the major protein that they obtained 'copine'
(pronounced 'ko-peen'), the French feminine noun meaning 'friend,'
because it associates like a 'companion' with lipid membranes. The 55-kD
copine protein bound phosphatidylserine in a calcium- but not
magnesium-dependent manner, but it did not bind phosphatidylcholine.
Copine promoted calcium-dependent aggregation of lipid vesicles. The
authors cloned partial cDNAs representing 2 distinct Paramecium copine
genes. By searching sequence databases for genes with sequence
similarity to the Paramecium copine genes, Creutz et al. (1998)
identified human ESTs corresponding to 5 copine genes, named copine I to
V. Two overlapping ESTs contained the complete copine I (CPNE1) coding
sequence. The deduced 537-amino acid CPNE1 protein contains 2 type II C2
domains in its N-terminal half and a domain similar to the A domain,
which is present in a number of extracellular proteins or the
extracellular portions of membrane proteins, in its C-terminal half; it
does not have a predicted signal sequence or transmembrane domains. C2
domains mediate calcium-dependent interactions with phospholipids, and
the A domain of integrins appears to mediate the binding of the integrin
to extracellular ligands. CPNE1 has a broad tissue distribution.
Recombinant CPNE1 expressed in bacteria exhibited calcium-dependent
binding to phosphatidylserine vesicles. Antibody against CPNE1 reacted
with bovine chromobindin-17, which is a 55-kD calcium-dependent
chromaffin vesicle-binding protein, and the authors concluded that
chromobindin-17 is a copine. They suggested that copines function in
membrane trafficking.
*FIELD* RF
1. Creutz, C. E.; Tomsig, J. L.; Snyder, S. L.; Gautier, M.-C.; Skouri,
F.; Beisson, J.; Cohen, J.: The copines, a novel class of C2 domain-containing,
calcium-dependent, phospholipid-binding proteins conserved from Paramecium
to humans. J. Biol. Chem. 273: 1393-1402, 1998.
*FIELD* CD
Patti M. Sherman: 9/29/1999
*FIELD* ED
mgross: 10/01/1999
mgross: 9/30/1999
psherman: 9/30/1999