Full text data of CPNE3
CPNE3
(CPN3, KIAA0636)
[Confidence: high (present in two of the MS resources)]
Copine-3 (Copine III)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Copine-3 (Copine III)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00024403
IPI00024403 Copine III Copine III membrane n/a 2 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 2 3 Membrane binding is Ca++ dependent n/a found at its expected molecular weight found at molecular weight
IPI00024403 Copine III Copine III membrane n/a 2 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 2 3 Membrane binding is Ca++ dependent n/a found at its expected molecular weight found at molecular weight
UniProt
O75131
ID CPNE3_HUMAN Reviewed; 537 AA.
AC O75131; A8KA47; Q8IYA1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1998, sequence version 1.
DT 22-JAN-2014, entry version 118.
DE RecName: Full=Copine-3;
DE AltName: Full=Copine III;
GN Name=CPNE3; Synonyms=CPN3, KIAA0636;
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], PARTIAL PROTEIN SEQUENCE, AND
RP PHOSPHORYLATION.
RX PubMed=11041869; DOI=10.1021/bi001250v;
RA Caudell E.G., Caudell J.J., Tang C.-H., Yu T.-K., Frederick M.J.,
RA Grimm E.A.;
RT "Characterization of human copine III as a phosphoprotein with
RT associated kinase activity.";
RL Biochemistry 39:13034-13043(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-412.
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Skin;
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 [5]
RP IDENTIFICATION BY 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 [6]
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 (By similarity).
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Phosphorylated on serine and threonine residues.
CC -!- SIMILARITY: Belongs to the copine family.
CC -!- SIMILARITY: Contains 2 C2 domains.
CC -!- SIMILARITY: Contains 1 VWFA domain.
CC -!- CAUTION: Was reported (PubMed:11041869) to have a protein kinase
CC activity.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31611.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF077226; AAD46074.2; -; mRNA.
DR EMBL; AB014536; BAA31611.2; ALT_INIT; mRNA.
DR EMBL; AK292912; BAF85601.1; -; mRNA.
DR EMBL; BC036242; AAH36242.1; -; mRNA.
DR EMBL; BC066597; AAH66597.1; -; mRNA.
DR RefSeq; NP_003900.1; NM_003909.3.
DR RefSeq; XP_005251150.1; XM_005251093.1.
DR UniGene; Hs.191219; -.
DR ProteinModelPortal; O75131; -.
DR SMR; O75131; 17-239.
DR IntAct; O75131; 4.
DR MINT; MINT-4526920; -.
DR STRING; 9606.ENSP00000198765; -.
DR PhosphoSite; O75131; -.
DR PaxDb; O75131; -.
DR PeptideAtlas; O75131; -.
DR PRIDE; O75131; -.
DR DNASU; 8895; -.
DR Ensembl; ENST00000198765; ENSP00000198765; ENSG00000085719.
DR Ensembl; ENST00000521271; ENSP00000430934; ENSG00000085719.
DR GeneID; 8895; -.
DR KEGG; hsa:8895; -.
DR UCSC; uc003ydv.2; human.
DR CTD; 8895; -.
DR GeneCards; GC08P087497; -.
DR HGNC; HGNC:2316; CPNE3.
DR HPA; HPA029552; -.
DR MIM; 604207; gene.
DR neXtProt; NX_O75131; -.
DR PharmGKB; PA26833; -.
DR eggNOG; NOG269302; -.
DR HOGENOM; HOG000220898; -.
DR HOVERGEN; HBG066841; -.
DR InParanoid; O75131; -.
DR OMA; TKVELNV; -.
DR OrthoDB; EOG77DJ57; -.
DR GenomeRNAi; 8895; -.
DR NextBio; 33407; -.
DR PRO; PR:O75131; -.
DR ArrayExpress; O75131; -.
DR Bgee; O75131; -.
DR CleanEx; HS_CPNE3; -.
DR Genevestigator; O75131; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; TAS:UniProtKB.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
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; 2.
DR PROSITE; PS50234; VWFA; FALSE_NEG.
PE 1: Evidence at protein level;
KW Complete proteome; Direct protein sequencing; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 537 Copine-3.
FT /FTId=PRO_0000144838.
FT DOMAIN 2 99 C2 1.
FT DOMAIN 125 230 C2 2.
FT DOMAIN 291 513 VWFA.
FT VARIANT 252 252 E -> D (in dbSNP:rs41333046).
FT /FTId=VAR_048848.
FT VARIANT 412 412 T -> M (in dbSNP:rs2304789).
FT /FTId=VAR_024424.
FT CONFLICT 394 394 P -> Q (in Ref. 4; AAH36242).
FT CONFLICT 419 419 Q -> R (in Ref. 4; AAH36242).
FT CONFLICT 475 475 R -> H (in Ref. 4; AAH36242).
SQ SEQUENCE 537 AA; 60131 MW; 91F2C5EAD611B842 CRC64;
MAAQCVTKVA LNVSCANLLD KDIGSKSDPL CVLFLNTSGQ QWYEVERTER IKNCLNPQFS
KTFIIDYYFE VVQKLKFGVY DIDNKTIELS DDDFLGECEC TLGQIVSSKK LTRPLVMKTG
RPAGKGSITI SAEEIKDNRV VLFEMEARKL DNKDLFGKSD PYLEFHKQTS DGNWLMVHRT
EVVKNNLNPV WRPFKISLNS LCYGDMDKTI KVECYDYDND GSHDLIGTFQ TTMTKLKEAS
RSSPVEFECI NEKKRQKKKS YKNSGVISVK QCEITVECTF LDYIMGGCQL NFTVGVDFTG
SNGDPRSPDS LHYISPNGVN EYLTALWSVG LVIQDYDADK MFPAFGFGAQ IPPQWQVSHE
FPMNFNPSNP YCNGIQGIVE AYRSCLPQIK LYGPTNFSPI INHVARFAAA ATQQQTASQY
FVLLIITDGV ITDLDETRQA IVNASRLPMS IIIVGVGGAD FSAMEFLDGD GGSLRSPLGE
VAIRDIVQFV PFRQFQNAPK EALAQCVLAE IPQQVVGYFN TYKLLPPKNP ATKQQKQ
//
ID CPNE3_HUMAN Reviewed; 537 AA.
AC O75131; A8KA47; Q8IYA1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1998, sequence version 1.
DT 22-JAN-2014, entry version 118.
DE RecName: Full=Copine-3;
DE AltName: Full=Copine III;
GN Name=CPNE3; Synonyms=CPN3, KIAA0636;
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], PARTIAL PROTEIN SEQUENCE, AND
RP PHOSPHORYLATION.
RX PubMed=11041869; DOI=10.1021/bi001250v;
RA Caudell E.G., Caudell J.J., Tang C.-H., Yu T.-K., Frederick M.J.,
RA Grimm E.A.;
RT "Characterization of human copine III as a phosphoprotein with
RT associated kinase activity.";
RL Biochemistry 39:13034-13043(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-412.
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Skin;
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 [5]
RP IDENTIFICATION BY 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 [6]
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 (By similarity).
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Phosphorylated on serine and threonine residues.
CC -!- SIMILARITY: Belongs to the copine family.
CC -!- SIMILARITY: Contains 2 C2 domains.
CC -!- SIMILARITY: Contains 1 VWFA domain.
CC -!- CAUTION: Was reported (PubMed:11041869) to have a protein kinase
CC activity.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31611.2; Type=Erroneous initiation;
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; AF077226; AAD46074.2; -; mRNA.
DR EMBL; AB014536; BAA31611.2; ALT_INIT; mRNA.
DR EMBL; AK292912; BAF85601.1; -; mRNA.
DR EMBL; BC036242; AAH36242.1; -; mRNA.
DR EMBL; BC066597; AAH66597.1; -; mRNA.
DR RefSeq; NP_003900.1; NM_003909.3.
DR RefSeq; XP_005251150.1; XM_005251093.1.
DR UniGene; Hs.191219; -.
DR ProteinModelPortal; O75131; -.
DR SMR; O75131; 17-239.
DR IntAct; O75131; 4.
DR MINT; MINT-4526920; -.
DR STRING; 9606.ENSP00000198765; -.
DR PhosphoSite; O75131; -.
DR PaxDb; O75131; -.
DR PeptideAtlas; O75131; -.
DR PRIDE; O75131; -.
DR DNASU; 8895; -.
DR Ensembl; ENST00000198765; ENSP00000198765; ENSG00000085719.
DR Ensembl; ENST00000521271; ENSP00000430934; ENSG00000085719.
DR GeneID; 8895; -.
DR KEGG; hsa:8895; -.
DR UCSC; uc003ydv.2; human.
DR CTD; 8895; -.
DR GeneCards; GC08P087497; -.
DR HGNC; HGNC:2316; CPNE3.
DR HPA; HPA029552; -.
DR MIM; 604207; gene.
DR neXtProt; NX_O75131; -.
DR PharmGKB; PA26833; -.
DR eggNOG; NOG269302; -.
DR HOGENOM; HOG000220898; -.
DR HOVERGEN; HBG066841; -.
DR InParanoid; O75131; -.
DR OMA; TKVELNV; -.
DR OrthoDB; EOG77DJ57; -.
DR GenomeRNAi; 8895; -.
DR NextBio; 33407; -.
DR PRO; PR:O75131; -.
DR ArrayExpress; O75131; -.
DR Bgee; O75131; -.
DR CleanEx; HS_CPNE3; -.
DR Genevestigator; O75131; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; TAS:UniProtKB.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
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; 2.
DR PROSITE; PS50234; VWFA; FALSE_NEG.
PE 1: Evidence at protein level;
KW Complete proteome; Direct protein sequencing; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 537 Copine-3.
FT /FTId=PRO_0000144838.
FT DOMAIN 2 99 C2 1.
FT DOMAIN 125 230 C2 2.
FT DOMAIN 291 513 VWFA.
FT VARIANT 252 252 E -> D (in dbSNP:rs41333046).
FT /FTId=VAR_048848.
FT VARIANT 412 412 T -> M (in dbSNP:rs2304789).
FT /FTId=VAR_024424.
FT CONFLICT 394 394 P -> Q (in Ref. 4; AAH36242).
FT CONFLICT 419 419 Q -> R (in Ref. 4; AAH36242).
FT CONFLICT 475 475 R -> H (in Ref. 4; AAH36242).
SQ SEQUENCE 537 AA; 60131 MW; 91F2C5EAD611B842 CRC64;
MAAQCVTKVA LNVSCANLLD KDIGSKSDPL CVLFLNTSGQ QWYEVERTER IKNCLNPQFS
KTFIIDYYFE VVQKLKFGVY DIDNKTIELS DDDFLGECEC TLGQIVSSKK LTRPLVMKTG
RPAGKGSITI SAEEIKDNRV VLFEMEARKL DNKDLFGKSD PYLEFHKQTS DGNWLMVHRT
EVVKNNLNPV WRPFKISLNS LCYGDMDKTI KVECYDYDND GSHDLIGTFQ TTMTKLKEAS
RSSPVEFECI NEKKRQKKKS YKNSGVISVK QCEITVECTF LDYIMGGCQL NFTVGVDFTG
SNGDPRSPDS LHYISPNGVN EYLTALWSVG LVIQDYDADK MFPAFGFGAQ IPPQWQVSHE
FPMNFNPSNP YCNGIQGIVE AYRSCLPQIK LYGPTNFSPI INHVARFAAA ATQQQTASQY
FVLLIITDGV ITDLDETRQA IVNASRLPMS IIIVGVGGAD FSAMEFLDGD GGSLRSPLGE
VAIRDIVQFV PFRQFQNAPK EALAQCVLAE IPQQVVGYFN TYKLLPPKNP ATKQQKQ
//
MIM
604207
*RECORD*
*FIELD* NO
604207
*FIELD* TI
*604207 COPINE III; CPNE3
;;CPN3
*FIELD* TX
Copines are calcium-dependent phospholipid-binding proteins. See CPNE1
read more(604205) for background information.
CLONING
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, including copine III (GenBank GENBANK
N72351).
By screening human brain cDNAs for the potential to encode proteins
larger than 50 kD, Ishikawa et al. (1998) identified a CPNE3 cDNA, which
they called KIAA0636. The deduced 537-amino acid CPNE3 protein is 65.7%
identical to CPNE1. By SDS-PAGE, the in vitro transcribed/translated
product of the CPNE3 cDNA had a molecular mass of 65 kD. RT-PCR detected
CPNE3 expression in all human tissues examined.
By immunoprecipitation and kinase assays, Caudell et al. (2000)
serendipitously identified a 60-kD protein identical to CPNE3. CPNE3
contains 2 N-terminal C2 domains, like CPNE1, CPNE6 (605688), and CPNE7
(605689), but these 4 copines have divergent C termini. CPNE3 is 63%,
52%, and 47% identical to CPNE1, CPNE6, and CPNE7, respectively.
Northern blot analysis revealed ubiquitous expression of a 5.0-kb
transcript. Biochemical analysis showed that CPNE3 appears to possess
endogenous kinase activity, although it lacks a classic kinase domain.
CPNE3 is phosphorylated on both serine and threonine residues but not on
tyrosine residues.
MAPPING
Ishikawa et al. (1998) mapped the CPNE3 gene to chromosome 8 using a
radiation hybrid mapping panel.
*FIELD* RF
1. Caudell, E. G.; Caudell, J. J.; Tang, C.-H.; Yu, T.-K.; Frederick,
M. J.; Grimm, E. A.: Characterization of human copine III as a phosphoprotein
with associated kinase activity. Biochemistry 39: 13034-13043, 2000.
2. 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.
3. Ishikawa, K.; Nagase, T.; Suyama, M.; Miyajima, N.; Tanaka, A.;
Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the coding sequences
of unidentified human genes. X. The complete sequences of 100 new
cDNA clones from brain which can code for large proteins in vitro. DNA
Res. 5: 169-176, 1998.
*FIELD* CN
Paul J. Converse - updated: 3/15/2001
*FIELD* CD
Patti M. Sherman: 9/29/1999
*FIELD* ED
alopez: 04/17/2008
mgross: 3/15/2001
mgross: 9/30/1999
psherman: 9/30/1999
*RECORD*
*FIELD* NO
604207
*FIELD* TI
*604207 COPINE III; CPNE3
;;CPN3
*FIELD* TX
Copines are calcium-dependent phospholipid-binding proteins. See CPNE1
read more(604205) for background information.
CLONING
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, including copine III (GenBank GENBANK
N72351).
By screening human brain cDNAs for the potential to encode proteins
larger than 50 kD, Ishikawa et al. (1998) identified a CPNE3 cDNA, which
they called KIAA0636. The deduced 537-amino acid CPNE3 protein is 65.7%
identical to CPNE1. By SDS-PAGE, the in vitro transcribed/translated
product of the CPNE3 cDNA had a molecular mass of 65 kD. RT-PCR detected
CPNE3 expression in all human tissues examined.
By immunoprecipitation and kinase assays, Caudell et al. (2000)
serendipitously identified a 60-kD protein identical to CPNE3. CPNE3
contains 2 N-terminal C2 domains, like CPNE1, CPNE6 (605688), and CPNE7
(605689), but these 4 copines have divergent C termini. CPNE3 is 63%,
52%, and 47% identical to CPNE1, CPNE6, and CPNE7, respectively.
Northern blot analysis revealed ubiquitous expression of a 5.0-kb
transcript. Biochemical analysis showed that CPNE3 appears to possess
endogenous kinase activity, although it lacks a classic kinase domain.
CPNE3 is phosphorylated on both serine and threonine residues but not on
tyrosine residues.
MAPPING
Ishikawa et al. (1998) mapped the CPNE3 gene to chromosome 8 using a
radiation hybrid mapping panel.
*FIELD* RF
1. Caudell, E. G.; Caudell, J. J.; Tang, C.-H.; Yu, T.-K.; Frederick,
M. J.; Grimm, E. A.: Characterization of human copine III as a phosphoprotein
with associated kinase activity. Biochemistry 39: 13034-13043, 2000.
2. 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.
3. Ishikawa, K.; Nagase, T.; Suyama, M.; Miyajima, N.; Tanaka, A.;
Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the coding sequences
of unidentified human genes. X. The complete sequences of 100 new
cDNA clones from brain which can code for large proteins in vitro. DNA
Res. 5: 169-176, 1998.
*FIELD* CN
Paul J. Converse - updated: 3/15/2001
*FIELD* CD
Patti M. Sherman: 9/29/1999
*FIELD* ED
alopez: 04/17/2008
mgross: 3/15/2001
mgross: 9/30/1999
psherman: 9/30/1999