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Breast cancer anti-estrogen resistance protein 1 (CRK-associated substrate) (p130cas)

 BCAR1_RAT               Reviewed;         968 AA.
Q63767; Q63766;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 153.
RecName: Full=Breast cancer anti-estrogen resistance protein 1;
AltName: Full=CRK-associated substrate;
AltName: Full=p130cas;
Name=Bcar1; Synonyms=Cas, Crkas;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Fibroblast;
PubMed=8070403;
Sakai R., Iwamatsu A., Hirano N., Ogawa S., Tanaka T., Mano H.,
Yazaki Y., Hirai H.;
"A novel signaling molecule, p130, forms stable complexes in vivo with
v-Crk and v-Src in a tyrosine phosphorylation-dependent manner.";
EMBO J. 13:3748-3756(1994).
[2]
PHOSPHORYLATION AT TYR-347 BY ABL1.
PubMed=7780740; DOI=10.1016/S0960-9822(95)00060-1;
Mayer B.J., Hirai H., Sakai R.;
"Evidence that SH2 domains promote processive phosphorylation by
protein-tyrosine kinases.";
Curr. Biol. 5:296-305(1995).
[3]
PHOSPHORYLATION AT TYROSINE RESIDUES BY PTK2/FAK1.
PubMed=9360983; DOI=10.1074/jbc.272.46.29083;
Tachibana K., Urano T., Fujita H., Ohashi Y., Kamiguchi K., Iwata S.,
Hirai H., Morimoto C.;
"Tyrosine phosphorylation of Crk-associated substrates by focal
adhesion kinase. A putative mechanism for the integrin-mediated
tyrosine phosphorylation of Crk-associated substrates.";
J. Biol. Chem. 272:29083-29090(1997).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-737, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Docking protein which plays a central coordinating role
for tyrosine-kinase-based signaling related to cell adhesion.
Implicated in induction of cell migration (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Forms complexes in vivo with PTK2/FAK1, adapter protein
CRKL and LYN kinase. Can heterodimerize with NEDD9. Interacts with
activated CSPG4. Interacts with BCAR3, the interaction regulates
adhesion-dependent serine phosphorylation. Interacts with NPHP1,
PTK2B/PYK2 and SH2D3C. Interacts with BMX, INPPL1/SHIP2 and PEAK1
(By similarity). Part of a collagen stimulated complex involved in
cell migration composed of CDC42, CRK, TNK2 and BCAR1/p130cas (By
similarity). {ECO:0000250}.
-!- INTERACTION:
P18031:PTPN1 (xeno); NbExp=5; IntAct=EBI-1176801, EBI-968788;
P05480:Src (xeno); NbExp=2; IntAct=EBI-1176801, EBI-298680;
-!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cytoplasm.
Note=Localizes at focal adhesions and stress fibers.
Unphosphorylated form localizes in the cytoplasm and can move to
the membrane upon tyrosine phosphorylation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=Q63767-1; Sequence=Displayed;
Name=Short;
IsoId=Q63767-2; Sequence=VSP_004135;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Higher expression in lung,
intestine and testis.
-!- DOMAIN: Contains a central domain (substrate domain) containing
multiple potential SH2-binding sites and a C-terminal domain
containing a divergent helix-loop-helix (HLH) motif. The SH2-
binding sites putatively bind CRK, NCK and ABL SH2 domains. The
HLH motif is absolutely required for the induction of pseudohyphal
growth in yeast and mediates heterodimerization with NEDD9.
-!- DOMAIN: A serine-rich region promotes activation of the serum
response element (SRE).
-!- DOMAIN: The SH3 domain is necessary for the localization of the
protein to focal adhesions and interacts with one proline-rich
region of PTK2/FAK1.
-!- PTM: PTK2/FAK1 activation mediates phosphorylation at the YDYVHL
motif; phosphorylation is most likely catalyzed by SRC family
members. SRC-family kinases are recruited to the phosphorylated
sites and can phosphorylate other tyrosine residues. Tyrosine
phosphorylation is triggered by integrin mediated adhesion of
cells to the extracellular matrix. {ECO:0000269|PubMed:7780740,
ECO:0000269|PubMed:9360983}.
-!- PTM: Dephosphorylated by PTPN14 at Tyr-226. {ECO:0000250}.
-!- SIMILARITY: Belongs to the CAS family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D29766; BAA06169.1; -; mRNA.
EMBL; D29766; BAA06170.1; -; mRNA.
PIR; S46992; S46992.
RefSeq; NP_037063.1; NM_012931.1. [Q63767-1]
UniGene; Rn.40101; -.
PDB; 1X27; X-ray; 2.70 A; I/J/K/L/M/N=759-767.
PDB; 1Z23; NMR; -; A=546-708.
PDBsum; 1X27; -.
PDBsum; 1Z23; -.
ProteinModelPortal; Q63767; -.
SMR; Q63767; -.
BioGrid; 247449; 5.
IntAct; Q63767; 7.
MINT; MINT-93469; -.
STRING; 10116.ENSRNOP00000039940; -.
iPTMnet; Q63767; -.
PhosphoSitePlus; Q63767; -.
PaxDb; Q63767; -.
PRIDE; Q63767; -.
GeneID; 25414; -.
KEGG; rno:25414; -.
UCSC; RGD:2406; rat. [Q63767-1]
CTD; 9564; -.
RGD; 2406; Bcar1.
eggNOG; ENOG410IEDD; Eukaryota.
eggNOG; ENOG410ZSUM; LUCA.
HOGENOM; HOG000261698; -.
HOVERGEN; HBG004354; -.
InParanoid; Q63767; -.
KO; K05726; -.
PhylomeDB; Q63767; -.
EvolutionaryTrace; Q63767; -.
PRO; PR:Q63767; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; ISO:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0001726; C:ruffle; ISS:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
GO; GO:0019901; F:protein kinase binding; ISO:RGD.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
GO; GO:0030036; P:actin cytoskeleton organization; IMP:RGD.
GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
GO; GO:0050851; P:antigen receptor-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0050853; P:B cell receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0060326; P:cell chemotaxis; ISO:RGD.
GO; GO:0016477; P:cell migration; IMP:RGD.
GO; GO:1990859; P:cellular response to endothelin; IPI:RGD.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; ISO:RGD.
GO; GO:0071732; P:cellular response to nitric oxide; IPI:RGD.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; ISO:RGD.
GO; GO:0008286; P:insulin receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; IMP:RGD.
GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; IDA:UniProtKB.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:RGD.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; ISO:RGD.
CDD; cd12001; SH3_BCAR1; 1.
InterPro; IPR028848; BCAR1.
InterPro; IPR035745; BCAR1_SH3.
InterPro; IPR021901; CAS_C.
InterPro; IPR014928; Serine_rich.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR10654:SF15; PTHR10654:SF15; 1.
Pfam; PF12026; DUF3513; 1.
Pfam; PF08824; Serine_rich; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell adhesion;
Cell junction; Complete proteome; Cytoplasm;
Direct protein sequencing; Phosphoprotein; Reference proteome;
SH3 domain; SH3-binding.
CHAIN 1 968 Breast cancer anti-estrogen resistance
protein 1.
/FTId=PRO_0000064856.
DOMAIN 97 159 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
REGION 213 514 Substrate for kinases.
REGION 844 894 Divergent helix-loop-helix motif.
MOTIF 733 741 SH3-binding. {ECO:0000255}.
COMPBIAS 168 181 Pro-rich.
COMPBIAS 520 712 Ser-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P56945}.
MOD_RES 226 226 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P56945}.
MOD_RES 237 237 Phosphoserine.
{ECO:0000250|UniProtKB:P56945}.
MOD_RES 332 332 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q61140}.
MOD_RES 347 347 Phosphotyrosine; by ABL1.
{ECO:0000269|PubMed:7780740}.
MOD_RES 367 367 Phosphothreonine.
{ECO:0000250|UniProtKB:P56945}.
MOD_RES 390 390 Phosphoserine.
{ECO:0000250|UniProtKB:P56945}.
MOD_RES 460 460 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q61140}.
MOD_RES 470 470 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q61140}.
MOD_RES 508 508 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q61140}.
MOD_RES 526 526 Phosphoserine.
{ECO:0000250|UniProtKB:P56945}.
MOD_RES 535 535 Phosphoserine.
{ECO:0000250|UniProtKB:P56945}.
MOD_RES 737 737 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
VAR_SEQ 5 98 Missing (in isoform Short).
{ECO:0000305}.
/FTId=VSP_004135.
HELIX 554 581 {ECO:0000244|PDB:1Z23}.
STRAND 591 594 {ECO:0000244|PDB:1Z23}.
HELIX 599 624 {ECO:0000244|PDB:1Z23}.
HELIX 634 661 {ECO:0000244|PDB:1Z23}.
STRAND 664 666 {ECO:0000244|PDB:1Z23}.
HELIX 671 702 {ECO:0000244|PDB:1Z23}.
SEQUENCE 968 AA; 104262 MW; E861641BFD68D377 CRC64;
MKYLVSVGAG PARRAGGLED VSWGPRVSRR PQSYRAARHV NESLPRSAFR VPAAHGASVT
PSAALGSGLP ETQPEAVCRG TEKPRFAEGC KPAASRDKNV LAKALYDNVA ESPDELSFRK
GDIMTVLERD TQGLDGWWLC SLHGRQGIVP GNRLKILVGM YDKKPAAPGP GPPATPPQPQ
PSLPQGVHTP VPPASQYSPM LPTAYQPQPD NVYLVPTPSK TQQGLYQAPG PNPQFQSPPA
KQTSTFSKQT PHHSFPSPAT DLYQVPPGPG SPAQDIYQVP PSAGTGHDIY QVPPSLDTRS
WEGTKPPAKV VVPTRVGQGY VYEASQAEQD EYDTPRHLLA PGSQDIYDVP PVRGLLPNQY
GQEVYDTPPM AVKGPNGRDP LLDVYDVPPS VEKGLPPSNH HSVYDVPPSV SKDVPDGPLL
REETYDVPPA FAKPKPFDPT RHPLILAAPP PDSPPAEDVY DVPPPAPDLY DVPPGLRRPG
PGTLYDVPRE RVLPPEVADG SVIDDGVYAV PPPAEREAPT DGKRLSASST GSTRSSQSAS
SLEVVVPGRE PLELEVAVET LARLQQGVST TVAHLLDLVG SASGPGGWRS TSEPQEPPVQ
DLKAAVAAVH GAVHELLEFA RSAVSSATHT SDRTLHAKLS RQLQKMEDVY QTLVVHGQVL
DSGRGGPGFT LDDLDRLVAC SRAVPEDAKQ LASFLHGNAS LLFRRTKAPG PGPEGSSSLH
LNPTDKASSI QSRPLPSPPK FTSQDSPDGQ YENSEGGWME DYDYVHLQGK EEFEKTQKEL
LEKGNIVRQG KGQLELQQLK QFERLEQEVS RPIDHDLANW TPAQPLVPGR TGGLGPSDRQ
LLLFYLEQCE ANLTTLTDAV DAFFTAVATN QPPKIFVAHS KFVILSAHKL VFIGDTLSRQ
AKAADVRSKV THYSNLLCDL LRGIVATTKA AALQYPSPSA AQDMVDRVKE LGHSTQQFRR
VLGQLAAA


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