ID W5MMY1_LEPOC Unreviewed; 936 AA.
AC W5MMY1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=BCAR1 scaffold protein, Cas family member {ECO:0000313|Ensembl:ENSLOCP00000009740.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000009740.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000009740.1}
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; AHAT01020787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01020788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01020789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015224078.1; XM_015368592.1.
DR AlphaFoldDB; W5MMY1; -.
DR STRING; 7918.ENSLOCP00000009740; -.
DR Ensembl; ENSLOCT00000009751.1; ENSLOCP00000009740.1; ENSLOCG00000008018.1.
DR GeneID; 102692374; -.
DR KEGG; loc:102692374; -.
DR CTD; 9564; -.
DR eggNOG; ENOG502QQHE; Eukaryota.
DR GeneTree; ENSGT00950000183008; -.
DR HOGENOM; CLU_017000_1_0_1; -.
DR InParanoid; W5MMY1; -.
DR OMA; THAIDAF; -.
DR OrthoDB; 2902504at2759; -.
DR Proteomes; UP000018468; Linkage group LG23.
DR Bgee; ENSLOCG00000008018; Expressed in zone of skin and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:1901490; P:regulation of lymphangiogenesis; IEA:Ensembl.
DR GO; GO:1903670; P:regulation of sprouting angiogenesis; IEA:Ensembl.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
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; 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:UP000018468};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 3..65
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 73..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 936 AA; 103542 MW; 0005D58ACE354707 CRC64;
MNYLNVLAKA LYDNVAESPD ELSFRKGDIM TVLERDTQGL DGWWLCSLHG RQGIVPGNRL
KILVGMYDKK QPAGMGPGVQ QGTPTQSPLP FPQQNAYTKP PPSSQYTAMH PAYPSQPDSV
YMLPPNHAKG PQSLYQVPTG PQFPAGQGKA PALLQKQGTQ SSGQDIYQVP PSLGPSQDIY
QVPPTSKGSP QDIYQVPPSA GGPGQDIYQV PPSMNQTQDI YQTPPSLEKG SWDSPKPPGK
VVVPTRVGQV YVYENPKTEQ DEYDVPRHLP PSQEIYDVPP TRGQYNQQVY DTPPMVVKGP
PSREGVQEIY DTPPIVEKSH VHVQQTVYDF PPSVSKDVPD GLIREETYDV PPHFVKMKKS
PESKPHQPPV QPQHPDDVYD VPPLSGKQGD ATAAQEIYDI PPSLRKERPQ DVYDFPREHP
AGGRPLGGED MGDYIYDVPP QVVRDAASTE ELTISFKRLS ASSTGSTRSN LSTSSLDIIP
VKESSVTAKP SGRELQLDLD VAMEVLVKLQ HSVESSVSSL MSFISSSWRS PEQMEANLQG
IRAAVERVKS SVKDLLEFAR GAVANAAQAT DRTLQAKLSK QVQKMEEGYQ GLLKHSQALD
NCNWALSVLV AGKTSSGDDL DRLVMCSRGV PDDTKQLASF LHGNASLLFK RTKQQAPHTP
QLGDSRHTFS QAGLESLGQV TNNNNISAYQ TGLPEKPNIQ SRPLPSPPKF MAEDTLDSQY
ENTEGGWMED YDYVHLQGKE EFEKNQKELL EKGNIIRQGK AQLAQQQLKQ FERLEQEVTR
PIDNDMTNWT APSHYPPSRS KLSPGDRQLL LFYAEQCEAN ITTLNNAIDA FYSSINNNQP
PKIFVAHSKF VILSAHKLVF IGDTLSRQAK ALEIRNKVTQ HSNLLCDKLK EIVVTTKTAA
LQYPSATAAK DMIDRVRDLA NSTQQFRMVL SQMASL
//
