Entry sw: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   30-NOV-2016, entry version 108.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; 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.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Spleen, and 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Calcium-dependent phospholipid-binding protein that
CC       plays a role in ERBB2-mediated tumor cell migration in response to
CC       growth factor heregulin stimulation.
CC       {ECO:0000250|UniProtKB:O75131}.
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
CC       binding of CPNE3 with ERBB2. Interacts with RACK1.
CC       {ECO:0000250|UniProtKB:O75131}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75131}.
CC       Cytoplasm {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
CC       a calcium-dependent manner. Translocates to the cell membrane and
CC       the nucleus in a calcium- or growth factor heregulin-dependent
CC       manner. Colocalizes with the tyrosine phosphorylated ERBB2 form at
CC       cell membrane and focal adhesions in a calcium- or growth factor
CC       heregulin-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   -!- SIMILARITY: Contains 2 C2 domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00041}.
CC   -!- SIMILARITY: Contains 1 VWFA domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00219}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90244.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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   UniGene; Mm.38390; -.
DR   ProteinModelPortal; Q8BT60; -.
DR   SMR; Q8BT60; -.
DR   IntAct; Q8BT60; 2.
DR   MINT; MINT-4091865; -.
DR   STRING; 10090.ENSMUSP00000029885; -.
DR   iPTMnet; Q8BT60; -.
DR   PhosphoSitePlus; Q8BT60; -.
DR   EPD; Q8BT60; -.
DR   MaxQB; Q8BT60; -.
DR   PaxDb; Q8BT60; -.
DR   PeptideAtlas; Q8BT60; -.
DR   PRIDE; Q8BT60; -.
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   eggNOG; KOG1327; Eukaryota.
DR   eggNOG; ENOG410XPC8; LUCA.
DR   GeneTree; ENSGT00760000119085; -.
DR   HOGENOM; HOG000220898; -.
DR   HOVERGEN; HBG066841; -.
DR   InParanoid; Q8BT60; -.
DR   OMA; IDYYFEL; -.
DR   OrthoDB; EOG091G05IT; -.
DR   PhylomeDB; Q8BT60; -.
DR   TreeFam; TF316419; -.
DR   Reactome; R-MMU-1483206; Glycerophospholipid biosynthesis.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   PRO; PR:Q8BT60; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   Bgee; ENSMUSG00000028228; -.
DR   CleanEx; MM_CPNE3; -.
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:0070062; C:extracellular exosome; ISO:MGI.
DR   GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
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:0044822; F:poly(A) RNA binding; ISO:MGI.
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; cd01459; vWA_copine_like; 1.
DR   Gene3D; 2.60.40.150; -; 2.
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   SUPFAM; SSF53300; SSF53300; 1.
DR   PROSITE; PS50004; C2; 2.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Complete proteome; Cytoplasm; Membrane;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN         1    533       Copine-3.
FT                                /FTId=PRO_0000144839.
FT   DOMAIN        2     99       C2 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00041}.
FT   DOMAIN      125    230       C2 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00041}.
FT   DOMAIN      291    513       VWFA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   MOD_RES      14     14       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O75131}.
FT   MOD_RES     197    197       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     243    243       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O75131}.
FT   CONFLICT     37     37       T -> A (in Ref. 2; BAC25524).
FT                                {ECO:0000305}.
FT   CONFLICT    471    533       GGSLRAPSGEVAIRDIVQFVPFRQFQNAPKEALAQCVLAEI
FT                                PQQVVGYFNTYKLLPPKNPAVK -> EWKSPCPFRRGGHKR
FT                                YCSVCAFQTVPECSKRSACSVCLGRDSPAGGGLLQHIQTPS
FT                                SQKPSCEVEEPGQLQDFKSCVEQRHLSHRMMYLPSALLTPG
FT                                YMM (in Ref. 2; BAC25524). {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       289    495       ismart:VWA [T]
FT   MYHIT       139    245       ismart:C2 [T]
FT   MYHIT       145    239       ipfam:C2 [T]
FT   MYHIT       138    230       iprf:C2 [T]
FT   MYHIT       310    524       ipfam:Copine [T]
FT   MYHIT        13    113       ipfam:C2 [T]
FT   MYHIT         7    114       ismart:C2 [T]
FT   MYHIT         1     99       iprf:C2 [T]
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
//