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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7

DescriptionRecName: Full=Copine-3 {ECO:0000305}; AltName: Full=Copine III {ECO:0000250|UniProtKB:O75131};
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MyHits synonymsCPNE3_PONAB , Q5RAE1 , 7EF0448F9B15D362
match map segment
ipfam:C2 iprf:C2 ipfam:C2 ipfam:Copine ismart:C2 ismart:VWA ismart:C2 iprf:C2  
Legends: 1, Phosphoserine. {ECO:0000250|UniProtKB:O75131}; 2, C2 1. {ECO:0000255|PROSITE- ProRule:PRU00041}; 3, C2 2. {ECO:0000255|PROSITE- ProRule:PRU00041}.
ID   CPNE3_PONAB             Reviewed;         537 AA.
AC   Q5RAE1;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   30-NOV-2016, entry version 51.
DE   RecName: Full=Copine-3 {ECO:0000305};
DE   AltName: Full=Copine III {ECO:0000250|UniProtKB:O75131};
GN   Name=CPNE3 {ECO:0000250|UniProtKB:O75131};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CR859076; CAH91269.1; -; mRNA.
DR   RefSeq; NP_001127397.1; NM_001133925.1.
DR   ProteinModelPortal; Q5RAE1; -.
DR   STRING; 9601.ENSPPYP00000021004; -.
DR   GeneID; 100174464; -.
DR   KEGG; pon:100174464; -.
DR   CTD; 8895; -.
DR   eggNOG; KOG1327; Eukaryota.
DR   eggNOG; ENOG410XPC8; LUCA.
DR   HOVERGEN; HBG066841; -.
DR   InParanoid; Q5RAE1; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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: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   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Complete proteome; Cytoplasm; Membrane;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN         1    537       Copine-3.
FT                                /FTId=PRO_0000144840.
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:0000250|UniProtKB:O75131}.
FT   MOD_RES     243    243       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O75131}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        13    112       ipfam:C2 [T]
FT   MYHIT         1     99       iprf:C2 [T]
FT   MYHIT       145    239       ipfam:C2 [T]
FT   MYHIT       310    524       ipfam:Copine [T]
FT   MYHIT         7    114       ismart:C2 [T]
FT   MYHIT       289    495       ismart:VWA [T]
FT   MYHIT       139    245       ismart:C2 [T]
FT   MYHIT       138    230       iprf:C2 [T]
SQ   SEQUENCE   537 AA;  60102 MW;  7EF0448F9B15D362 CRC64;
     MAAQCVTKVA LNVSCANLLD KDIGSKSDPL CVLFLNTSGQ QWYEVERTER IKNCLNPQFS
     KTFIIDYYFE VVQKLKFGVY DIDNKTIELS DDDFLGECEC TLGQVVSSKK LTRPLVMKNG
     RPAGKGSITI SAEEIKDNRV VLFEMEARKP DNKDLFGKSD PYLEFHKQTS DGNWLMVHRT
     EVVKNNLNPV WRPFKISLNS LCYGDMDKTI KVECYDYDND GSHDLIGTFQ TTMTKLKEAS
     RCSPVEFECI NEKKRQKKKS YKNSGVISVK QCEITVECTF LDYIMGGCQL NFTVGVDFTG
     SNDDPRSPDS LHYISPNGVN EYLTALWSVG LVIQDYDADK MFPAFGFGAQ IPPQWQVSHE
     FPMNFNPSNP YCNGIQGIVE AYRSCLPQIK LYGPTNFSPI INHVARFAAA AAQQQTASQY
     FVLLIITDGV ITDLDETRQA IVNASRLPMS IIIVGVGGAD FSAMEFLDGD GGGLRSPSGE
     VAIRDIVQFV PFRQFQNAPK EALAQCVLAE IPQQVVGYFN TYKLLPPKNP ATKQQKQ
//