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Database: UniProt
Entry: A0A2I3RWP5_PANTR
LinkDB: A0A2I3RWP5_PANTR
Original site: A0A2I3RWP5_PANTR 
ID   A0A2I3RWP5_PANTR        Unreviewed;       868 AA.
AC   A0A2I3RWP5; A0A2J8Q6C3;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=BCAR1 scaffold protein, Cas family member {ECO:0000313|Ensembl:ENSPTRP00000069143.1};
GN   Name=BCAR1 {ECO:0000313|Ensembl:ENSPTRP00000069143.1,
GN   ECO:0000313|VGNC:VGNC:10129};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000069143.1, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000069143.1, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|Ensembl:ENSPTRP00000069143.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   EMBL; AACZ04039444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_016785677.1; XM_016930188.1.
DR   AlphaFoldDB; A0A2I3RWP5; -.
DR   Ensembl; ENSPTRT00000088550.1; ENSPTRP00000069143.1; ENSPTRG00000008357.6.
DR   GeneID; 454246; -.
DR   CTD; 9564; -.
DR   VGNC; VGNC:10129; BCAR1.
DR   GeneTree; ENSGT00950000183008; -.
DR   OrthoDB; 2902504at2759; -.
DR   Proteomes; UP000002277; Chromosome 16.
DR   Bgee; ENSPTRG00000008357; Expressed in cortex of kidney and 20 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:UP000002277};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          1..63
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          68..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          409..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          606..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          713..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..97
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..443
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..651
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   868 AA;  93149 MW;  DA51918D07A2016B CRC64;
     MENVLAKALY DNVAESPDEL SFRKGDIMTV LEQDTQGLDG WWLCSLHGRQ GIVPGNRLKI
     LVGMYDKKPA GPGPGPPATP AQPQPGLHAP APPASQYTPM LPNTYQPQPD SVYLVPTPSK
     AQQGLYQVPG PSPQFQSPPA KQTSTFSKQT PHHPFPSPAT DLYQVPPGPG GPAQDIYQVP
     PSAGMGHDIY QVPPSMDTRS WEGTKPPAKV VVPTRVGQGY VYEAAQPEQD EYDIPRHLLA
     PGPQDIYDVP PVRGLLPSQY GQEVYDTPPM AVKGPNGRDP LLEVYDVPPS VEKGLPPSNH
     HAVYDVPPSV SKDVPDGPLL REETYDVPPA FAKTKPFDPA RTPLVLAAPP PDSPPAEDVY
     DVPPPAPDLY DVPPGLRRPG PGTLYDVPRE RVLPPEVADG GVVDSGVYAV PPPAEREAPA
     EGKRLSASST GSTRSSQSAS SLEVAGPGRE PLELEVAVEA LARLQQGVSA TVAHLLDLAG
     SAGGTGSWRS PSEPQEPLVQ DLQAAVAAVQ SAVHELLEFA RSAVGNAAHT SDRALHAKLS
     RQLQKMEDVH QTLVAHGQAL DAGRGGSGAT LEDLDRLVAC SRAVPEDAKQ LASFLHGNAS
     LLFRRTKAPA PGPEGGGTLH PNPTDKTSSI QSRPLPSPPK FTSQDSPDGQ YENSEGGWME
     DYDYVHLQGK EEFEKTQKEL LEKGSITRQG KSQLELQQLK QFERLEQEVS RPIDHDLANW
     TPAQPLAPGR TGGLGPSDRQ LLLFYLEQCE ANLTTLTNAV DAFFTAVATN QPPKIFVAHS
     KFVILSAHKL VFIGDTLSRQ AKAADVRSQV THYSNLLCDL LRGIVATTKA AALQYPSPSA
     AQDMVERVKE LGHSTQQFRR VLGQLAAA
//
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