ID A0A2K5MY94_CERAT Unreviewed; 888 AA.
AC A0A2K5MY94;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=BCAR1 scaffold protein, Cas family member {ECO:0000313|Ensembl:ENSCATP00000030184.1};
GN Name=BCAR1 {ECO:0000313|Ensembl:ENSCATP00000030184.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000030184.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000030184.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_011888259.1; XM_012032869.1.
DR AlphaFoldDB; A0A2K5MY94; -.
DR Ensembl; ENSCATT00000054446.1; ENSCATP00000030184.1; ENSCATG00000038291.1.
DR GeneID; 105572979; -.
DR CTD; 9564; -.
DR GeneTree; ENSGT00950000183008; -.
DR OrthoDB; 2902504at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000038291; Expressed in skeletal muscle tissue and 10 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd11569; FAT-like_BCAR1_C; 1.
DR CDD; cd11552; Serine_rich_BCAR1; 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:UP000233060};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 21..83
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 89..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..110
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 888 AA; 95411 MW; 3825E26205AF273D CRC64;
MLTHRPQAAE QRGQTPAPSF GWNVLAKALY DNVAESPDEL SFRKGDIMTV LEQDTQGLDG
WWLCSLHGRQ GIVPGNRLKI LVGMYDKKPA GPGPGPPTIP AQPQPGLHAP APPASQYTPM
LPTTYQPQPD SVYLVPTPSK AQQGLYQAPG PSPQFQSPPA KQTSTFSKQT PHHQFPSPAA
DLYQVPPGPG GPAQDIYQVP PSAGMGHDIY QVPPSMDTRS WEGTKPPAKV VVPTRVGQGY
VYEAAQPEQD EYDIPRHLLA PGSQDIYDVP PVRGLLPSQY GQEVYDTPPM AVKGPNGRDP
LLEVYDVPPS VEKGLPLSSH HAVYDVPPSV SKDVPDGPLL REETYDVPPA FAKTKPFDPA
RTPLVLAVPP PDSPPAEDVY DVPPPAPDLY DVPPGLRRPG PGTLYDVPRE RVLPPEVADG
GTVDNGVYAV PPPAEREAPA DGKRLSASST GSTRSSQSAS SLEVAGPGRE PLELEVAVEA
LARLQQGVST TVAHLLDLAG SAGGTGSWRN PSEPQEPLVQ DLQAAVAAVQ SAVHELLEFA
RSAVGNAAHT SDRALHAKLS RQLQKMEDVH QTLVAHGQAL DAGRGGPGAT PEDLDRLVAC
SRAVPEDAKQ LASFLHGNAS LLFRRTKAPA LGPEGGGTLH PNPTDKTSSI QSRPLPSPPK
FTSQDSPDGQ YENSEGGWME DYDYVHLQGK EEFEKTQKEL LEKGSITRQG KSQLELQQLK
QFERLEQEVS RPIDHDLANW TPAQPLAPGR TGGLGPSDRQ LLLFYLEQCE ANLTTLTNAV
DAFFTAVATN QPPKIFVAHS KFVILSAHKL VFIGDTLSRQ AKAADVRSQV THYSNLLCNL
LRGIVATTKA AALQYPSPAA AQDMVERVKE LGHSTQQFRR VLGQLAAA
//
