VAV_BOVIN
ID VAV_BOVIN Reviewed; 844 AA.
AC Q08DN7;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Proto-oncogene vav;
GN Name=VAV1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Couples tyrosine kinase signals with the activation of the
CC Rho/Rac GTPases, thus leading to cell differentiation and/or
CC proliferation. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SHB (By similarity). Interacts with APS, DOCK2,
CC GRB2, GRB3, DOCK2, SLA, TEC and ZNF655/VIK. Interacts with SIAH2;
CC without leading to its degradation. Associates with BLNK, PLCG1, GRB2
CC and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with
CC CBLB; which inhibits tyrosine phosphorylation and down-regulates
CC activity. May interact with CCPG1. Interacts with CLNK. Interacts with
CC THEMIS2 (By similarity). Interacts with NEK3 and this interaction is
CC prolactin-dependent. Interacts with ITK. Interacts with PTK2B/PYK2 (By
CC similarity). Interacts with HCK. Interacts with PTK2B/PYK2. Interacts
CC (via SH2 domain) with SYK (By similarity). Interacts with ANKRD54.
CC Interacts with CD6 (By similarity). {ECO:0000250|UniProtKB:P15498,
CC ECO:0000250|UniProtKB:P27870}.
CC -!- DOMAIN: The DH domain is involved in interaction with CCPG1.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by FYN. Phosphorylated on tyrosine residues by HCK
CC in response to IFNG and bacterial lipopolysaccharide (LPS) (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: 'Vav' stands for the sixth letter of the Hebrew
CC alphabet.
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DR EMBL; BC123646; AAI23647.1; -; mRNA.
DR RefSeq; NP_001071542.1; NM_001078074.1.
DR AlphaFoldDB; Q08DN7; -.
DR BMRB; Q08DN7; -.
DR SMR; Q08DN7; -.
DR PRIDE; Q08DN7; -.
DR Ensembl; ENSBTAT00000056825; ENSBTAP00000050922; ENSBTAG00000039160.
DR GeneID; 617345; -.
DR KEGG; bta:617345; -.
DR CTD; 7409; -.
DR VEuPathDB; HostDB:ENSBTAG00000039160; -.
DR VGNC; VGNC:36772; VAV1.
DR GeneTree; ENSGT00940000159125; -.
DR InParanoid; Q08DN7; -.
DR OMA; PYISRPT; -.
DR OrthoDB; 710582at2759; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000039160; Expressed in neutrophil and 105 other tissues.
DR ExpressionAtlas; Q08DN7; baseline and differential.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140031; F:phosphorylation-dependent protein binding; IEA:Ensembl.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0030593; P:neutrophil chemotaxis; IEA:Ensembl.
DR GO; GO:0006909; P:phagocytosis; IEA:Ensembl.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IEA:Ensembl.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
DR GO; GO:0008361; P:regulation of cell size; IEA:Ensembl.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
DR CDD; cd00029; C1; 1.
DR CDD; cd01223; PH_Vav; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd10405; SH2_Vav1; 1.
DR CDD; cd11979; SH3_VAV1_1; 1.
DR CDD; cd11976; SH3_VAV1_2; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR022613; CAMSAP-like_CH_dom.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037832; PH_Vav.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR003096; SM22_calponin.
DR InterPro; IPR028530; Vav1.
DR InterPro; IPR035879; VAV1_SH2.
DR InterPro; IPR035730; VAV1_SH3_1.
DR InterPro; IPR035729; VAV1_SH3_2.
DR PANTHER; PTHR45818:SF2; PTHR45818:SF2; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF11971; CAMSAP_CH; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 2.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00888; SM22CALPONIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 2: Evidence at transcript level;
KW Guanine-nucleotide releasing factor; Metal-binding; Phosphoprotein;
KW Proto-oncogene; Reference proteome; Repeat; SH2 domain; SH3 domain; Zinc;
KW Zinc-finger.
FT CHAIN 1..844
FT /note="Proto-oncogene vav"
FT /id="PRO_0000343900"
FT DOMAIN 1..119
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 193..372
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 401..503
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 591..659
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 670..764
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 781..841
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 514..563
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 567..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 825
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P15498"
FT MOD_RES 843
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P27870"
SQ SEQUENCE 844 AA; 98243 MW; 0A9C26F419D23BC6 CRC64;
MELWRQCTHW LIQCRVLPPS HRVTWDGAQV CELAQALRDG VLLCQLLNNL LPHAINLREV
NLRPQMSQFL CLKNIRTFLS TCYEKFGLKR SELFEAFDLF DVQDFGKVIY TLSALSWTPI
AQNKGIMPFP TEESVGDEDI YSGLSDQIDD TVEEDEDLYD CVENEEAEGD EVYEDLMRSE
PVPMPPKMTE YDKRCCCLRE IQQTEEKYTD TLGSIQQHFM KPLQRFLKPQ DVEIIFINIE
DLLRVHTHFL KEMKEALANP GASTLYQVFI KYKERFLIYG RYCSQVESAS KHLDRVATAR
EDVQMKLEEC SQRANNGRFT LRDLLMVPMQ RVLKYHLLLQ ELVKHTQDAM EKDNLRLALD
AMRDLAQCVN EVKRDNETLR QITNFQLSIE NLDQSLAHYG RPKIDGELKI TSVERRSKMD
RYAFLLDKAL LICKRRGDTY DLKDFVNLHS FQVRDDSSGE RDNKKWTHMF LLIEDQGAQG
YELFFKTREL KKKWMEQFEM AISNIYPENA TANGHDFQMF SFEETTSCKA CQMLLRGTFY
QGYRCQRCRA PAHKECLGRV PPCGRHGQDY SGTMKKDKPH RRAQDKKRNE LGLPKMEVCQ
EYYGLPPPPG AIGPFLRLNP GDIVELTKAE AEQNWWEGRN ISTNEVGWFP CNRVKPYVHG
PPQDLSVHLW YAGPMERAGA ESILTNRSDG TFLVRQRVKD AAEFAISIKY NVEVKHIKIM
TAEGLYRITE KKAFRGLTEL VEFYQQNSLK DCFKSLDTTL QFPFKEPERR AINKPSAGSI
KIFGTAKARY DFCARDRSEL SLKEGDIVKI LNKKGQQGWW RGEIYGRIGW FPSNYVEEDY
SEYC
