ID A0A2K6EG91_PROCO Unreviewed; 902 AA.
AC A0A2K6EG91;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=BCAR1 scaffold protein, Cas family member {ECO:0000313|Ensembl:ENSPCOP00000000754.1};
GN Name=BCAR1 {ECO:0000313|Ensembl:ENSPCOP00000000754.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000000754.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000000754.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}.
CC -!- SIMILARITY: Belongs to the CAS family. {ECO:0000256|ARBA:ARBA00007848}.
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DR AlphaFoldDB; A0A2K6EG91; -.
DR STRING; 379532.ENSPCOP00000000754; -.
DR Ensembl; ENSPCOT00000002756.1; ENSPCOP00000000754.1; ENSPCOG00000002318.1.
DR GeneTree; ENSGT00950000183008; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0001726; C:ruffle; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0060326; P:cell chemotaxis; IEA:Ensembl.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEA:Ensembl.
DR GO; GO:0086100; P:endothelin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IEA:Ensembl.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IEA:Ensembl.
DR CDD; cd11569; FAT-like_BCAR1_C; 1.
DR CDD; cd12001; SH3_BCAR1; 1.
DR Gene3D; 1.20.120.230; Alpha-catenin/vinculin-like; 1.
DR Gene3D; 1.20.120.830; Serine-rich domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR046976; BCAR1_C.
DR InterPro; IPR035745; BCAR1_SH3.
DR InterPro; IPR021901; CAS_C.
DR InterPro; IPR037362; CAS_fam.
DR InterPro; IPR014928; Serine_rich_dom.
DR InterPro; IPR038319; Serine_rich_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10654:SF15; BREAST CANCER ANTI-ESTROGEN RESISTANCE PROTEIN 1; 1.
DR PANTHER; PTHR10654; CAS SCAFFOLDING PROTEIN; 1.
DR Pfam; PF12026; CAS_C; 1.
DR Pfam; PF08824; Serine_rich; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR01887; SPECTRNALPHA.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 35..97
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 101..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..121
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..408
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 902 AA; 96766 MW; 666BF913EFA8DE6E CRC64;
LPASTSLLSL AQGHQGTDQS CSCGHCSERQ GGPPEPNVLA KALYDNVAES PDELSFRKGD
IMTVLERDTQ GLDGWWLCSL HGRQGIVPGN RLKILVGMYD KKPAGPGPGP PTTPPGHPQG
LHVAVPPASQ YTPMLPAAYQ PQPDSVYLVP TPSKAQQGLY QAPGPSPQFQ SPPAKQTSTF
PKQTPHHPFP SPATDLYQVP PGPGSPAQDI YQVPPSAGIG HDIYQVPLSM DTRSWEGTKT
PAKVVVPTRV GQGYVYEASQ PEQDEYDIPR HLLAPGPQDI YDVPPVRGLL PNQYGQEVYD
TPPMAVKGPN GRDPLLDVYD VPPSVEKGLP PSSHHAVYDV PPSVSKDVPD GPLLREETYD
VPPAFAKAKP FDPARHPLVL AAPPPDSPPA EDVYDVPPPA PDLYDVPPGL RRPGPGTLYD
VPRERALPPE VADGGVADDG VYSVPPPAER EPQADAKRLS ASSTGSTRSS QSVSSLEVAG
PGREPLELEV AVETLARLQQ SVSTTVAHLL DLAGSAGGAG GWRSTPELQE PPVQDLRAAV
AAVQGAVYEL LEFARSAVGN AAHTSDRALH AKLSRQLQKM EDVYQTLVAH GQALDSGRGG
PGATPEDLDR LVACSRAVPE DAKQLASFLH GNASLLFRRT KAPAPGPEGG GPLHPNPTDK
ASSIQSRPLP SPPKFTSQDS PDGQYENSEG GWMEDYDYVH LQGKEEFEKT QKELLEKGNI
VRQAKSQLEL QQLKQFERLE QEVSRPIDHD LARWTPAQPL GPGRTGSLGP SDRQLLLFYL
EQCEANLTTL TNAVDAFFTA VATNQPPKIF VAHSKFVILS AHKLVFIGDT LSRQAKAADV
RSQVTHYSNL LCDLLRGIVA TTKAAALQYP SPSAAQDMVD RVKELGHSTQ QFRRVLGQLA
AA
//