CPNE3_MOUSE
ID CPNE3_MOUSE Reviewed; 533 AA.
AC Q8BT60; Q5CZX9; Q5DU22;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Copine-3 {ECO:0000305};
DE AltName: Full=Copine III {ECO:0000250|UniProtKB:O75131, ECO:0000312|MGI:MGI:1917818};
GN Name=Cpne3 {ECO:0000312|MGI:MGI:1917818}; Synonyms=Kiaa0636;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Calcium-dependent phospholipid-binding protein that plays a
CC role in ERBB2-mediated tumor cell migration in response to growth
CC factor heregulin stimulation. {ECO:0000250|UniProtKB:O75131}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBUNIT: Monomer. Interacts with ERBB2 (preferentially with the
CC tyrosine phosphorylated form); this interaction occurs at the cell
CC membrane and is increased in a growth factor heregulin-dependent
CC manner. Interacts with SHC1; this interaction may mediate the binding
CC of CPNE3 with ERBB2. Interacts with RACK1.
CC {ECO:0000250|UniProtKB:O75131}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75131}. Cytoplasm
CC {ECO:0000250|UniProtKB:O75131}. Cell membrane
CC {ECO:0000250|UniProtKB:O75131}. Cell junction
CC {ECO:0000250|UniProtKB:O75131}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:O75131}. Note=Associates to the membrane in a
CC calcium-dependent manner. Translocates to the cell membrane and the
CC nucleus in a calcium- or growth factor heregulin-dependent manner.
CC Colocalizes with the tyrosine phosphorylated ERBB2 form at cell
CC membrane and focal adhesions in a calcium- or growth factor heregulin-
CC dependent manner. {ECO:0000250|UniProtKB:O75131}.
CC -!- PTM: Phosphorylated on serine and threonine residues.
CC {ECO:0000250|UniProtKB:O75131}.
CC -!- SIMILARITY: Belongs to the copine family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90244.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK220348; BAD90244.1; ALT_INIT; mRNA.
DR EMBL; AK017651; BAC25524.1; -; mRNA.
DR EMBL; BC090632; AAH90632.1; -; mRNA.
DR CCDS; CCDS17991.1; -.
DR RefSeq; NP_082045.1; NM_027769.2.
DR AlphaFoldDB; Q8BT60; -.
DR SMR; Q8BT60; -.
DR BioGRID; 214140; 5.
DR IntAct; Q8BT60; 1.
DR STRING; 10090.ENSMUSP00000029885; -.
DR iPTMnet; Q8BT60; -.
DR PhosphoSitePlus; Q8BT60; -.
DR EPD; Q8BT60; -.
DR jPOST; Q8BT60; -.
DR MaxQB; Q8BT60; -.
DR PaxDb; Q8BT60; -.
DR PeptideAtlas; Q8BT60; -.
DR PRIDE; Q8BT60; -.
DR ProteomicsDB; 285293; -.
DR Antibodypedia; 25495; 165 antibodies from 29 providers.
DR DNASU; 70568; -.
DR Ensembl; ENSMUST00000029885; ENSMUSP00000029885; ENSMUSG00000028228.
DR GeneID; 70568; -.
DR KEGG; mmu:70568; -.
DR UCSC; uc008sby.1; mouse.
DR CTD; 8895; -.
DR MGI; MGI:1917818; Cpne3.
DR VEuPathDB; HostDB:ENSMUSG00000028228; -.
DR eggNOG; KOG1327; Eukaryota.
DR GeneTree; ENSGT00940000154968; -.
DR HOGENOM; CLU_020452_3_2_1; -.
DR InParanoid; Q8BT60; -.
DR OMA; EMAAQCV; -.
DR OrthoDB; 1067545at2759; -.
DR PhylomeDB; Q8BT60; -.
DR TreeFam; TF316419; -.
DR Reactome; R-MMU-1483206; Glycerophospholipid biosynthesis.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 70568; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Cpne3; mouse.
DR PRO; PR:Q8BT60; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BT60; protein.
DR Bgee; ENSMUSG00000028228; Expressed in substantia propria of cornea and 245 other tissues.
DR Genevisible; Q8BT60; MM.
DR GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0038128; P:ERBB2 signaling pathway; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
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 Calcium; Cell junction; Cell membrane; Cytoplasm; Membrane; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..533
FT /note="Copine-3"
FT /id="PRO_0000144839"
FT DOMAIN 1..115
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 124..247
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 291..513
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT BINDING 22
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 22
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 160
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="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 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75131"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75131"
FT CONFLICT 37
FT /note="T -> A (in Ref. 2; BAC25524)"
FT /evidence="ECO:0000305"
FT CONFLICT 471..533
FT /note="GGSLRAPSGEVAIRDIVQFVPFRQFQNAPKEALAQCVLAEIPQQVVGYFNTY
FT KLLPPKNPAVK -> EWKSPCPFRRGGHKRYCSVCAFQTVPECSKRSACSVCLGRDSPA
FT GGGLLQHIQTPSSQKPSCEVEEPGQLQDFKSCVEQRHLSHRMMYLPSALLTPGYMM
FT (in Ref. 2; BAC25524)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 533 AA; 59585 MW; F76A4BDCA11C7F2E CRC64;
MAAQCVTKVE LNVSCNNLLD ADVTSKSDPL CVLFLNTSGH QWYEVERTER IKNSLNPKFS
KTFVIDYYFE VVQKLKFGIY DIDNKTIELS DDDFLGECEV TLGQIVSSKK LTRPLVLKNG
KPAGKGSITI SAEEIKDNRV VLFEMEARKL DNKDLFGKSD PYLEFHKQTS DGHWLMVHRT
EVIKNNLNPM WKPFKISLNS LCYGDMDKTI KVECYDYDND GSHDLIGTFQ TTMTKLKEAS
RSSPVEYECI NEKKRQKKKS YKNSGVISVK HCEITVECTF LDYIMGGCQL NFTVGVDFTG
SNGDPSSPDS LHYISPNGVN EYLTAIWSVG LVIQDYDADK MFPAFGFGAQ VPPQWQVSHE
FPMNFNPSNP YCNGIQGIVE AYRTCLPQIR LYGPTNFSPI INHVARFAAA ATQQQTASQY
FVLLIITDGV ITDLDETRQA IVNAAKLPMS IIIVGVGGAD FSAMEFLDGD GGSLRAPSGE
VAIRDIVQFV PFRQFQNAPK EALAQCVLAE IPQQVVGYFN TYKLLPPKNP AVK
