CPNE3_PONAB
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 03-AUG-2022, entry version 68.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 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}.
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DR EMBL; CR859076; CAH91269.1; -; mRNA.
DR RefSeq; NP_001127397.1; NM_001133925.1.
DR AlphaFoldDB; Q5RAE1; -.
DR SMR; Q5RAE1; -.
DR STRING; 9601.ENSPPYP00000021004; -.
DR GeneID; 100174464; -.
DR KEGG; pon:100174464; -.
DR CTD; 8895; -.
DR eggNOG; KOG1327; Eukaryota.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Calcium; Cell junction; Cell membrane; Cytoplasm; Membrane; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..537
FT /note="Copine-3"
FT /id="PRO_0000144840"
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:0000250|UniProtKB:O75131"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75131"
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
