GenomeNet

Database: UniProt
Entry: H0XLV4_OTOGA
LinkDB: H0XLV4_OTOGA
Original site: H0XLV4_OTOGA 
ID   H0XLV4_OTOGA            Unreviewed;       920 AA.
AC   H0XLV4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=BCAR1 scaffold protein, Cas family member {ECO:0000313|Ensembl:ENSOGAP00000017094.1};
GN   Name=BCAR1 {ECO:0000313|Ensembl:ENSOGAP00000017094.1};
OS   Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC   Galagidae; Otolemur.
OX   NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000017094.1, ECO:0000313|Proteomes:UP000005225};
RN   [1] {ECO:0000313|Proteomes:UP000005225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA   Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA   Walker B.J., Sharpe T., Hall G.;
RT   "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSOGAP00000017094.1}
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; AAQR03081526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H0XLV4; -.
DR   STRING; 30611.ENSOGAP00000017094; -.
DR   Ensembl; ENSOGAT00000033540.1; ENSOGAP00000017094.1; ENSOGAG00000033394.1.
DR   eggNOG; ENOG502QQHE; Eukaryota.
DR   GeneTree; ENSGT00950000183008; -.
DR   HOGENOM; CLU_017000_1_0_1; -.
DR   InParanoid; H0XLV4; -.
DR   OMA; THAIDAF; -.
DR   TreeFam; TF328782; -.
DR   Proteomes; UP000005225; Unassembled WGS sequence.
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; 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:UP000005225};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          52..114
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          119..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          176..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          346..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          401..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          658..708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..207
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..427
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..496
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..703
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   920 AA;  98852 MW;  48286593F3BD5352 CRC64;
     LTGREFSCDS LCWHFLWSPG QGLGGPTGQL CILWGHWGRV PGVPPPAPAT GAENVLAKAL
     YDNVAESPDE LSFRKGDIMT VLERDTQGLD GWWLCSLHGR QGIVPGNRLK ILVGMYDKKP
     AGPGPGPPAA AAQPQPGHPQ GLHAAVPPAS QYTPMLPAAY QPDSVYLVPT PSKAQQGLYQ
     APGPSPQFQS PPAKQTSTFS KQTPHHPFPS PATDLYQVPP GPGSPAQDIY QVPPSAGMGH
     DIYQVPLSMD TRNWEGTKPP AKVVVPTRVG QGYVFEASQP EQDEYDIPRH LLAPGPQDIY
     DVPPVRGLLP SQYSQEVYDT PPMAVKGPNG RDPLLDVYDV PPSVEKGLPP SNHHAVYDVP
     PSVSKDVPDG PLLREETYDV PPAFSKTKPF DPARHPLVLA APPADSPPTE DVYDVPPPAP
     DLYDVPPGLR RPGPGTLYDV PRERVLPPEV ADGSVADDGV YAVPPPTERE APADGKRLSA
     SSTGSTRSSQ SVSSLEAPGP GREPLELEVA VEALARLQQG VSATVAHLLD LAGSASGAGG
     WRSTPEPQEP PVQDLRAAVA AVQGAVHELL EFARNAVGNA THTSDRALHA KLSRQLQKME
     DVYQTLVTHG QALDSGRGSG ATPEDLDRLV ACSRAVPEDA KQLASFLHGN ASLLFRRTKA
     PAPGPEGGGP LHPNPADKAN SIQSRPLPSP PKFTSQDSPD GQYENSEGGW MEDYDYVHLQ
     GKEEFEKTQK ELLEKGNIVR QAKSQLELQQ LKQFERLEQE VSRPIDHDLA RWTPAQPLAP
     GRTGSLGPSD RQLLLFYLEQ CEANLTTLTN AVDAFFTAVA TNQPPKIFVA HSKFVILSAH
     KLVFIGDTLS RQAKAADVRS QVTHYSNLLC ELLRGIVATT KAAALQYPSP SAAQDMVDRV
     KELGHSTQQF RRVLGQLAAA
//
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