VAV_RAT
ID VAV_RAT Reviewed; 843 AA.
AC P54100;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Proto-oncogene vav;
DE AltName: Full=p95;
GN Name=Vav1; Synonyms=Vav;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10395673;
RA Song J.S., Haleem-Smith H., Arudchandran R., Gomez J., Scott P.M.,
RA Mill J.F., Tan T.-H., Rivera J.;
RT "Tyrosine phosphorylation of Vav stimulates IL-6 production in mast cells
RT by a Rac/c-Jun N-terminal kinase-dependent pathway.";
RL J. Immunol. 163:802-810(1999).
CC -!- FUNCTION: Couples tyrosine kinase signals with the activation of the
CC Rho/Rac GTPases, thus leading to cell differentiation and/or
CC proliferation.
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}.
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DR EMBL; U39476; AAA98606.1; -; mRNA.
DR AlphaFoldDB; P54100; -.
DR SMR; P54100; -.
DR IntAct; P54100; 3.
DR STRING; 10116.ENSRNOP00000064264; -.
DR PhosphoSitePlus; P54100; -.
DR PaxDb; P54100; -.
DR RGD; 3951; Vav1.
DR eggNOG; KOG2996; Eukaryota.
DR InParanoid; P54100; -.
DR PhylomeDB; P54100; -.
DR Reactome; R-RNO-114604; GPVI-mediated activation cascade.
DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-RNO-1433557; Signaling by SCF-KIT.
DR Reactome; R-RNO-193648; NRAGE signals death through JNK.
DR Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-RNO-2871796; FCERI mediated MAPK activation.
DR Reactome; R-RNO-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-RNO-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-RNO-416482; G alpha (12/13) signalling events.
DR Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-RNO-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR Reactome; R-RNO-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR Reactome; R-RNO-9027284; Erythropoietin activates RAS.
DR Reactome; R-RNO-912631; Regulation of signaling by CBL.
DR Reactome; R-RNO-9748787; Azathioprine ADME.
DR Reactome; R-RNO-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR PRO; PR:P54100; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140031; F:phosphorylation-dependent protein binding; ISO:RGD.
DR GO; GO:0001784; F:phosphotyrosine residue binding; ISO:RGD.
DR GO; GO:0048468; P:cell development; TAS:RGD.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0006955; P:immune response; ISO:RGD.
DR GO; GO:0002768; P:immune response-regulating cell surface receptor signaling pathway; IEP:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISO:RGD.
DR GO; GO:0006909; P:phagocytosis; ISO:RGD.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISO:RGD.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0008361; P:regulation of cell size; ISO:RGD.
DR GO; GO:0043087; P:regulation of GTPase activity; ISO:RGD.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0042110; P:T cell activation; ISO:RGD.
DR GO; GO:0030217; P:T cell differentiation; ISO:RGD.
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..843
FT /note="Proto-oncogene vav"
FT /id="PRO_0000080982"
FT DOMAIN 1..119
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 194..373
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 402..504
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 590..658
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 669..763
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 780..840
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 515..564
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT MOD_RES 824
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P15498"
FT MOD_RES 842
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P27870"
SQ SEQUENCE 843 AA; 97954 MW; C4A5CACD45FCB80E CRC64;
MELWRQCTHW LIQCRVLPPS HRVTWEGAQV CELAQALRDG VLLCQLLNNL LPHAINLREV
NLRPQMSQFL CLKNIRTFLS TCCEKFGLKR SELFEAFDLF DVQDFGKVIY TLSALSWTPI
AQNKGIMPFP TEDSALGDED IYSGLSDQID DTAEEDEDLY DCVENEEAEG DEIYEDLMRS
ESVPTPPKMT EYDKRCCCLR EIQQTEEKYT DTLGSIQQHF MKPLQRFLKP QDMETIFVNI
EELLSVHTHF LKELKDALSG PGATMLYQVF IKYKERFLVY GRYCSQVESA IKHLDQVATA
REDVQMKLEE CSQRANNGRF TLRDLLMVPM QRVLKYHLLL QELVKHTQDT TEKENLRLAL
DAMRDLAQCV NEVKRDNETL RQITNFQLSI ENLDQSLANY GRPKIDGELK ITSVERRSKT
DRYAFLLDKA LLICKRRGDS YDLKASVNLH SFQVRDDSSG ERDNKKWSHM FLLIEDQGAQ
GYELFFKTRE LKKKWMEQFE MAISNIYPEN ATANGHDFQM FSFEETTSCK ACQMLLRGTF
YQGYRCYRCR APAHKECLGR VPPCGRQDFS GTMKKDKLHR RAQDKKRNEL GLPKMEVCQE
YYGIPPPPGA FGPFLRLNPG DIVELTKAEA EHTWWEGRNT ATNEVGWFPC NRVRPYVHGP
PQDLSVHLWY AGPMERAGAE GILTNRSDGT YLVRQRVKDT AEFAISIKYN VEVKHIKIMT
SEGLYRITEK KAFRGLPELV EFYQQNSLKD CFKSLDTTLQ FPYKEPERRA INKPPVGSTK
YFGTAKARYD FCARDRSELS LKEGDIIKIL NKKGQQGWWR GEIYGRIGWF PSNYVEEDYS
EYC
