ID   VAV_MOUSE               Reviewed;         845 AA.
AC   P27870; Q8BTV7;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   24-JAN-2024, entry version 227.
DE   RecName: Full=Proto-oncogene vav;
DE   AltName: Full=p95vav;
GN   Name=Vav1; Synonyms=Vav;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND MUTAGENESIS OF CYS-529;
RP   CYS-532 AND HIS-554.
RX   PubMed=2069873;
RA   Coppola J., Bryant S., Koda T., Conway D., Barbacid M.;
RT   "Mechanism of activation of the vav protooncogene.";
RL   Cell Growth Differ. 2:95-105(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1565462;
RA   Adams J.M., Houston H., Allen J., Lints T., Harvey R.;
RT   "The hematopoietically expressed vav proto-oncogene shares homology with
RT   the dbl GDP-GTP exchange factor, the bcr gene and a yeast gene (CDC24)
RT   involved in cytoskeletal organization.";
RL   Oncogene 7:611-618(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-93.
RX   PubMed=2005887; DOI=10.1128/mcb.11.4.1912-1920.1991;
RA   Katzav S., Cleveland J.L., Heslop H.E., Pulido D.;
RT   "Loss of the amino-terminal helix-loop-helix domain of the vav proto-
RT   oncogene activates its transforming potential.";
RL   Mol. Cell. Biol. 11:1912-1920(1991).
RN   [5]
RP   INTERACTION WITH TEC.
RX   PubMed=8877094;
RA   Miyazato A., Yamashita Y., Hatake K., Miura Y., Ozawa K., Mano H.;
RT   "Tec protein tyrosine kinase is involved in the signaling mechanism of
RT   granulocyte colony-stimulating factor receptor.";
RL   Cell Growth Differ. 7:1135-1139(1996).
RN   [6]
RP   INTERACTION WITH HCK, AND PHOSPHORYLATION.
RX   PubMed=9400828; DOI=10.1002/jlb.62.6.859;
RA   English B.K., Orlicek S.L., Mei Z., Meals E.A.;
RT   "Bacterial LPS and IFN-gamma trigger the tyrosine phosphorylation of vav in
RT   macrophages: evidence for involvement of the hck tyrosine kinase.";
RL   J. Leukoc. Biol. 62:859-864(1997).
RN   [7]
RP   INTERACTION WITH SLA.
RX   PubMed=10662792; DOI=10.1084/jem.191.3.463;
RA   Sosinowski T., Pandey A., Dixit V.M., Weiss A.;
RT   "Src-like adaptor protein (SLAP) is a negative regulator of T cell receptor
RT   signaling.";
RL   J. Exp. Med. 191:463-474(2000).
RN   [8]
RP   PHOSPHORYLATION, AND INTERACTION WITH CBLB.
RX   PubMed=10646609; DOI=10.1038/35003235;
RA   Chiang Y.J., Kole H.K., Brown K., Naramura M., Fukuhara S., Hu R.-J.,
RA   Jang I.K., Gutkind J.S., Shevach E., Gu H.;
RT   "Cbl-b regulates the CD28 dependence of T-cell activation.";
RL   Nature 403:216-220(2000).
RN   [9]
RP   PHOSPHORYLATION, AND INTERACTION WITH CBLB.
RX   PubMed=10646608; DOI=10.1038/35003228;
RA   Bachmaier K., Krawczyk C., Kozieradzki I., Kong Y.-Y., Sasaki T.,
RA   Oliveira-dos-Santos A., Mariathasan S., Bouchard D., Wakeham A., Itie A.,
RA   Le J., Ohashi P.S., Sarosi I., Nishina H., Lipkowitz S., Penninger J.M.;
RT   "Negative regulation of lymphocyte activation and autoimmunity by the
RT   molecular adaptor Cbl-b.";
RL   Nature 403:211-216(2000).
RN   [10]
RP   INTERACTION WITH CLNK.
RX   PubMed=11463797; DOI=10.1074/jbc.m106390200;
RA   Goitsuka R., Tatsuno A., Ishiai M., Kurosaki T., Kitamura D.;
RT   "MIST functions through distinct domains in immunoreceptor signaling in the
RT   presence and absence of LAT.";
RL   J. Biol. Chem. 276:36043-36050(2001).
RN   [11]
RP   POSSIBLE INTERACTION WITH CCPG1.
RX   PubMed=17000758; DOI=10.1128/mcb.00670-06;
RA   Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.;
RT   "Ccpg1, a novel scaffold protein that regulates the activity of the Rho
RT   guanine nucleotide exchange factor Dbs.";
RL   Mol. Cell. Biol. 26:8964-8975(2006).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-844, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Mast cell;
RX   PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [13]
RP   INTERACTION WITH ANKRD54.
RX   PubMed=19064729; DOI=10.1182/blood-2008-04-153452;
RA   Samuels A.L., Klinken S.P., Ingley E.;
RT   "Liar, a novel Lyn-binding nuclear/cytoplasmic shuttling protein that
RT   influences erythropoietin-induced differentiation.";
RL   Blood 113:3845-3856(2009).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [15]
RP   INTERACTION WITH THEMIS2.
RX   PubMed=20644716; DOI=10.1371/journal.pone.0011465;
RA   Peirce M.J., Brook M., Morrice N., Snelgrove R., Begum S., Lanfrancotti A.,
RA   Notley C., Hussell T., Cope A.P., Wait R.;
RT   "Themis2/ICB1 is a signaling scaffold that selectively regulates macrophage
RT   Toll-like receptor signaling and cytokine production.";
RL   PLoS ONE 5:E11465-E11465(2010).
RN   [16]
RP   INTERACTION WITH CD6.
RX   PubMed=24584089; DOI=10.1038/ni.2843;
RA   Roncagalli R., Hauri S., Fiore F., Liang Y., Chen Z., Sansoni A.,
RA   Kanduri K., Joly R., Malzac A., Laehdesmaeki H., Lahesmaa R., Yamasaki S.,
RA   Saito T., Malissen M., Aebersold R., Gstaiger M., Malissen B.;
RT   "Quantitative proteomics analysis of signalosome dynamics in primary T
RT   cells identifies the surface receptor CD6 as a Lat adaptor-independent TCR
RT   signaling hub.";
RL   Nat. Immunol. 15:384-392(2014).
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 (PubMed:10646609, PubMed:10646608). May interact with CCPG1
CC       (PubMed:17000758). Interacts with CLNK (PubMed:11463797). Interacts
CC       with THEMIS2 (PubMed:20644716). Interacts with NEK3 and this
CC       interaction is prolactin-dependent. Interacts with ITK. Interacts with
CC       PTK2B/PYK2 (By similarity). Interacts with HCK. Interacts with
CC       PTK2B/PYK2. Interacts (via SH2 domain) with SYK (By similarity).
CC       Interacts with ANKRD54 (PubMed:19064729). Interacts with CD6
CC       (PubMed:24584089). Interacts with isoform 2 of CRACR2A (By similarity).
CC       {ECO:0000250|UniProtKB:P15498, ECO:0000269|PubMed:10646608,
CC       ECO:0000269|PubMed:10646609, ECO:0000269|PubMed:10662792,
CC       ECO:0000269|PubMed:11463797, ECO:0000269|PubMed:19064729,
CC       ECO:0000269|PubMed:20644716, ECO:0000269|PubMed:24584089,
CC       ECO:0000269|PubMed:8877094, ECO:0000269|PubMed:9400828}.
CC   -!- INTERACTION:
CC       P27870; P19878: NCF2; Xeno; NbExp=4; IntAct=EBI-1697, EBI-489611;
CC   -!- TISSUE SPECIFICITY: Widely expressed in hematopoietic cells but not in
CC       other cell types. Found in the spleen and lung.
CC       {ECO:0000269|PubMed:2069873}.
CC   -!- DOMAIN: The DH domain is involved in interaction with CCPG1.
CC   -!- PTM: Phosphorylated by FYN (By similarity). Phosphorylated on tyrosine
CC       residues by HCK in response to IFNG and bacterial lipopolysaccharide
CC       (LPS). {ECO:0000250, ECO:0000269|PubMed:10646608,
CC       ECO:0000269|PubMed:10646609, ECO:0000269|PubMed:9400828}.
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DR   EMBL; X64361; CAA45713.1; -; mRNA.
DR   EMBL; AK088586; BAC40436.1; -; mRNA.
DR   EMBL; M59833; AAA63402.1; -; mRNA.
DR   CCDS; CCDS28931.1; -.
DR   PIR; A61187; TVMSVV.
DR   RefSeq; NP_035821.3; NM_011691.4.
DR   PDB; 1F5X; NMR; -; A=170-375.
DR   PDB; 1GCP; X-ray; 2.10 A; A/B/C/D=595-660.
DR   PDB; 1GCQ; X-ray; 1.68 A; C=595-660.
DR   PDB; 1K1Z; NMR; -; A=583-660.
DR   PDB; 2KBT; NMR; -; A=784-844.
DR   PDB; 2VRW; X-ray; 1.85 A; B=170-575.
DR   PDBsum; 1F5X; -.
DR   PDBsum; 1GCP; -.
DR   PDBsum; 1GCQ; -.
DR   PDBsum; 1K1Z; -.
DR   PDBsum; 2KBT; -.
DR   PDBsum; 2VRW; -.
DR   AlphaFoldDB; P27870; -.
DR   SMR; P27870; -.
DR   BioGRID; 204500; 28.
DR   DIP; DIP-31010N; -.
DR   IntAct; P27870; 14.
DR   MINT; P27870; -.
DR   STRING; 10090.ENSMUSP00000005889; -.
DR   iPTMnet; P27870; -.
DR   PhosphoSitePlus; P27870; -.
DR   EPD; P27870; -.
DR   jPOST; P27870; -.
DR   PaxDb; 10090-ENSMUSP00000005889; -.
DR   PeptideAtlas; P27870; -.
DR   ProteomicsDB; 298277; -.
DR   Antibodypedia; 665; 829 antibodies from 42 providers.
DR   DNASU; 22324; -.
DR   Ensembl; ENSMUST00000005889.16; ENSMUSP00000005889.10; ENSMUSG00000034116.18.
DR   GeneID; 22324; -.
DR   KEGG; mmu:22324; -.
DR   UCSC; uc008dep.2; mouse.
DR   AGR; MGI:98923; -.
DR   CTD; 7409; -.
DR   MGI; MGI:98923; Vav1.
DR   VEuPathDB; HostDB:ENSMUSG00000034116; -.
DR   eggNOG; KOG2996; Eukaryota.
DR   GeneTree; ENSGT00940000159125; -.
DR   HOGENOM; CLU_013787_0_0_1; -.
DR   InParanoid; P27870; -.
DR   OMA; PYISRPT; -.
DR   OrthoDB; 2911406at2759; -.
DR   PhylomeDB; P27870; -.
DR   TreeFam; TF316171; -.
DR   Reactome; R-MMU-114604; GPVI-mediated activation cascade.
DR   Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-MMU-1433557; Signaling by SCF-KIT.
DR   Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR   Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
DR   Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
DR   Reactome; R-MMU-389359; CD28 dependent Vav1 pathway.
DR   Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR   Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-MMU-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR   Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability.
DR   Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR   Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR   Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR   Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR   Reactome; R-MMU-9027284; Erythropoietin activates RAS.
DR   Reactome; R-MMU-912631; Regulation of signaling by CBL.
DR   Reactome; R-MMU-9748787; Azathioprine ADME.
DR   Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR   BioGRID-ORCS; 22324; 5 hits in 79 CRISPR screens.
DR   ChiTaRS; Vav1; mouse.
DR   EvolutionaryTrace; P27870; -.
DR   PRO; PR:P27870; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; P27870; Protein.
DR   Bgee; ENSMUSG00000034116; Expressed in skin of snout and 160 other cell types or tissues.
DR   ExpressionAtlas; P27870; baseline and differential.
DR   GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IGI:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140031; F:phosphorylation-dependent protein binding; IPI:UniProtKB.
DR   GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IGI:MGI.
DR   GO; GO:0006955; P:immune response; IMP:MGI.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IGI:MGI.
DR   GO; GO:0035556; P:intracellular signal transduction; IMP:MGI.
DR   GO; GO:0030593; P:neutrophil chemotaxis; IGI:MGI.
DR   GO; GO:0006909; P:phagocytosis; IGI:MGI.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; IGI:MGI.
DR   GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IGI:MGI.
DR   GO; GO:0072593; P:reactive oxygen species metabolic process; IGI:MGI.
DR   GO; GO:0008361; P:regulation of cell size; IEA:Ensembl.
DR   GO; GO:0042110; P:T cell activation; IMP:MGI.
DR   GO; GO:0030217; P:T cell differentiation; IGI:MGI.
DR   CDD; cd20867; C1_VAV1; 1.
DR   CDD; cd21262; CH_VAV1; 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; 3.30.60.20; -; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 2.
DR   InterPro; IPR022613; CAMSAP-like_CH_dom.
DR   InterPro; IPR001715; CH_dom.
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; IPR035879; VAV1_SH2.
DR   InterPro; IPR035730; VAV1_SH3_1.
DR   InterPro; IPR035729; VAV1_SH3_2.
DR   PANTHER; PTHR45818; PROTEIN VAV; 1.
DR   PANTHER; PTHR45818:SF2; PROTO-ONCOGENE VAV; 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; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 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.
DR   Genevisible; P27870; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Guanine-nucleotide releasing factor; Metal-binding;
KW   Phosphoprotein; Proto-oncogene; Reference proteome; Repeat; SH2 domain;
KW   SH3 domain; Zinc; Zinc-finger.
FT   CHAIN           1..845
FT                   /note="Proto-oncogene vav"
FT                   /id="PRO_0000080981"
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          592..660
FT                   /note="SH3 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          671..765
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          782..842
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         826
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P15498"
FT   MOD_RES         844
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17947660"
FT   MUTAGEN         529
FT                   /note="C->S: Abolishes transforming activity."
FT                   /evidence="ECO:0000269|PubMed:2069873"
FT   MUTAGEN         532
FT                   /note="C->S: Abolishes transforming activity."
FT                   /evidence="ECO:0000269|PubMed:2069873"
FT   MUTAGEN         554
FT                   /note="H->D: Abolishes transforming activity."
FT                   /evidence="ECO:0000269|PubMed:2069873"
FT   CONFLICT        29
FT                   /note="Q -> E (in Ref. 4; AAA63402)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        226
FT                   /note="R -> L (in Ref. 3; BAC40436)"
FT                   /evidence="ECO:0000305"
FT   HELIX           170..177
FT                   /evidence="ECO:0007829|PDB:1F5X"
FT   TURN            178..180
FT                   /evidence="ECO:0007829|PDB:1F5X"
FT   HELIX           191..219
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   HELIX           221..224
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   TURN            225..227
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   HELIX           230..237
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   HELIX           240..259
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   HELIX           261..263
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   HELIX           266..273
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   HELIX           276..278
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   HELIX           279..300
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   HELIX           302..316
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   HELIX           322..325
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   HELIX           328..333
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   HELIX           336..346
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   HELIX           350..389
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   STRAND          390..392
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   HELIX           397..400
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   STRAND          402..412
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   STRAND          420..437
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   STRAND          440..448
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   TURN            449..451
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   STRAND          452..455
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   STRAND          469..475
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   STRAND          481..488
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   HELIX           489..506
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   TURN            509..512
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   HELIX           513..515
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   STRAND          518..521
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   TURN            530..532
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   STRAND          538..541
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   STRAND          543..546
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   TURN            547..549
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   HELIX           555..560
FT                   /evidence="ECO:0007829|PDB:2VRW"
FT   TURN            585..587
FT                   /evidence="ECO:0007829|PDB:1K1Z"
FT   STRAND          596..599
FT                   /evidence="ECO:0007829|PDB:1GCQ"
FT   STRAND          603..607
FT                   /evidence="ECO:0007829|PDB:1GCQ"
FT   HELIX           610..612
FT                   /evidence="ECO:0007829|PDB:1GCQ"
FT   STRAND          624..629
FT                   /evidence="ECO:0007829|PDB:1GCQ"
FT   STRAND          635..641
FT                   /evidence="ECO:0007829|PDB:1GCQ"
FT   TURN            642..644
FT                   /evidence="ECO:0007829|PDB:1GCQ"
FT   STRAND          647..651
FT                   /evidence="ECO:0007829|PDB:1GCQ"
FT   HELIX           652..654
FT                   /evidence="ECO:0007829|PDB:1GCQ"
FT   STRAND          655..657
FT                   /evidence="ECO:0007829|PDB:1GCQ"
FT   STRAND          786..791
FT                   /evidence="ECO:0007829|PDB:2KBT"
FT   STRAND          796..800
FT                   /evidence="ECO:0007829|PDB:2KBT"
FT   STRAND          808..813
FT                   /evidence="ECO:0007829|PDB:2KBT"
FT   STRAND          817..825
FT                   /evidence="ECO:0007829|PDB:2KBT"
FT   STRAND          828..833
FT                   /evidence="ECO:0007829|PDB:2KBT"
FT   STRAND          836..841
FT                   /evidence="ECO:0007829|PDB:2KBT"
SQ   SEQUENCE   845 AA;  98137 MW;  3666DCCD1C5229DA CRC64;
     MELWRQCTHW LIQCRVLPPS HRVTWEGAQV CELAQALRDG VLLCQLLNNL LPQAINLREV
     NLRPQMSQFL CLKNIRTFLS TCCEKFGLKR SELFEAFDLF DVQDFGKVIY TLSALSWTPI
     AQNKGIMPFP TEDSALNDED IYSGLSDQID DTAEEDEDLY DCVENEEAEG DEIYEDLMRL
     ESVPTPPKMT EYDKRCCCLR EIQQTEEKYT DTLGSIQQHF MKPLQRFLKP QDMETIFVNI
     EELFSVHTHF LKELKDALAG PGATTLYQVF IKYKERFLVY GRYCSQVESA SKHLDQVATA
     REDVQMKLEE CSQRANNGRF TLRDLLMVPM QRVLKYHLLL QELVKHTQDA TEKENLRLAL
     DAMRDLAQCV NEVKRDNETL RQITNFQLSI ENLDQSLANY GRPKIDGELK ITSVERRSKT
     DRYAFLLDKA LLICKRRGDS YDLKASVNLH SFQVRDDSSG ERDNKKWSHM FLLIEDQGAQ
     GYELFFKTRE LKKKWMEQFE MAISNIYPEN ATANGHDFQM FSFEETTSCK ACQMLLRGTF
     YQGYRCYRCR APAHKECLGR VPPCGRHGQD FAGTMKKDKL HRRAQDKKRN ELGLPKMEVF
     QEYYGIPPPP GAFGPFLRLN PGDIVELTKA EAEHNWWEGR NTATNEVGWF PCNRVHPYVH
     GPPQDLSVHL WYAGPMERAG AEGILTNRSD GTYLVRQRVK DTAEFAISIK YNVEVKHIKI
     MTSEGLYRIT EKKAFRGLLE LVEFYQQNSL KDCFKSLDTT LQFPYKEPER RAISKPPAGS
     TKYFGTAKAR YDFCARDRSE LSLKEGDIIK ILNKKGQQGW WRGEIYGRIG WFPSNYVEED
     YSEYC
//