VAV3_HUMAN
ID VAV3_HUMAN Reviewed; 847 AA.
AC Q9UKW4; B1AMM0; B1APV5; B4E232; B7ZLR1; E9PQ97; O60498; O95230; Q9Y5X8;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Guanine nucleotide exchange factor VAV3;
DE Short=VAV-3;
GN Name=VAV3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 1-692
RP (ISOFORM 3), ALTERNATIVE PROMOTER USAGE, TISSUE SPECIFICITY, INDUCTION, AND
RP VARIANT SER-298.
RC TISSUE=Keratinocyte;
RX PubMed=9705494; DOI=10.1093/nar/26.17.3883;
RA Trenkle T., Welsh J., Jung B., Mathieu-Daude F., McClelland M.;
RT "Non-stoichiometric reduced complexity probes for cDNA arrays.";
RL Nucleic Acids Res. 26:3883-3891(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND ALTERNATIVE SPLICING.
RX PubMed=10523675; DOI=10.1128/mcb.19.11.7870;
RA Movilla N., Bustelo X.R.;
RT "Biological and regulatory properties of Vav-3, a new member of the Vav
RT family of oncoproteins.";
RL Mol. Cell. Biol. 19:7870-7885(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT SER-298.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH ROS1, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RX PubMed=11094073; DOI=10.1128/mcb.20.24.9212-9224.2000;
RA Zeng L., Sachdev P., Yan L., Chan J.L., Trenkle T., McClelland M.,
RA Welsh J., Wang L.H.;
RT "Vav3 mediates receptor protein tyrosine kinase signaling, regulates GTPase
RT activity, modulates cell morphology, and induces cell transformation.";
RL Mol. Cell. Biol. 20:9212-9224(2000).
RN [8]
RP INTERACTION WITH SH2B2.
RX PubMed=12400014; DOI=10.1038/sj.onc.1205927;
RA Yabana N., Shibuya M.;
RT "Adaptor protein APS binds the NH2-terminal autoinhibitory domain of
RT guanine nucleotide exchange factor Vav3 and augments its activity.";
RL Oncogene 21:7720-7729(2002).
RN [9]
RP INTERACTION WITH EPHA2.
RX PubMed=16782872; DOI=10.1128/mcb.02215-05;
RA Hunter S.G., Zhuang G., Brantley-Sieders D.M., Swat W., Cowan C.W.,
RA Chen J.;
RT "Essential role of Vav family guanine nucleotide exchange factors in EphA
RT receptor-mediated angiogenesis.";
RL Mol. Cell. Biol. 26:4830-4842(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-141, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP STRUCTURE BY NMR OF 1-134.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CH domain from human VAV-3 protein.";
RL Submitted (DEC-2006) to the PDB data bank.
CC -!- FUNCTION: Exchange factor for GTP-binding proteins RhoA, RhoG and, to a
CC lesser extent, Rac1. Binds physically to the nucleotide-free states of
CC those GTPases. Plays an important role in angiogenesis. Its recruitment
CC by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase
CC activation and vascular endothelial cell migration and assembly (By
CC similarity). May be important for integrin-mediated signaling, at least
CC in some cell types. In osteoclasts, along with SYK tyrosine kinase,
CC required for signaling through integrin alpha-v/beta-1 (ITAGV-ITGB1), a
CC crucial event for osteoclast proper cytoskeleton organization and
CC function. This signaling pathway involves RAC1, but not RHO,
CC activation. Necessary for proper wound healing. In the course of wound
CC healing, required for the phagocytotic cup formation preceding
CC macrophage phagocytosis of apoptotic neutrophils. Responsible for
CC integrin beta-2 (ITGB2)-mediated macrophage adhesion and, to a lesser
CC extent, contributes to beta-3 (ITGB3)-mediated adhesion. Does not
CC affect integrin beta-1 (ITGB1)-mediated adhesion (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the PH domain of SH2B2. Interacts (via SH2
CC domains) with the phosphorylated form of EPHA2. Interacts with ROS1;
CC constitutive interaction that mediates VAV3 phosphorylation.
CC {ECO:0000269|PubMed:11094073, ECO:0000269|PubMed:12400014,
CC ECO:0000269|PubMed:16782872}.
CC -!- INTERACTION:
CC Q9UKW4; Q13191: CBLB; NbExp=3; IntAct=EBI-297568, EBI-744027;
CC Q9UKW4; Q13480: GAB1; NbExp=6; IntAct=EBI-297568, EBI-517684;
CC Q9UKW4; P62993: GRB2; NbExp=8; IntAct=EBI-297568, EBI-401755;
CC Q9UKW4; P08581: MET; NbExp=2; IntAct=EBI-297568, EBI-1039152;
CC Q9UKW4; P27986: PIK3R1; NbExp=2; IntAct=EBI-297568, EBI-79464;
CC Q9UKW4; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-297568, EBI-726876;
CC Q9UKW4; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-297568, EBI-527853;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q9UKW4-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=Q9UKW4-2; Sequence=VSP_001820;
CC Name=3; Synonyms=VAV3.1;
CC IsoId=Q9UKW4-3; Sequence=VSP_041360, VSP_041361;
CC Name=4;
CC IsoId=Q9UKW4-4; Sequence=VSP_042359;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 3 are widely expressed; both
CC are expressed at very low levels in skeletal muscle. In keratinocytes,
CC isoform 1 is less abundant than isoform 3. Isoform 3 is detected at
CC very low levels, if any, in adrenal gland, bone marrow, spleen, fetal
CC brain and spinal chord; in these tissues, isoform 1 is readily
CC detectable. {ECO:0000269|PubMed:11094073, ECO:0000269|PubMed:9705494}.
CC -!- INDUCTION: Down-regulated by EGF and TGF-beta.
CC {ECO:0000269|PubMed:9705494}.
CC -!- PTM: Phosphorylated. Phosphorylation can be mediated by ROS1. In
CC osteoclasts, undergoes tyrosine phosphorylation in response to CSF1 (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced by alternative promoter
CC usage. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD03799.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/VAV3ID42782ch1p13.html";
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DR EMBL; AF035442; AAD03799.1; ALT_INIT; mRNA.
DR EMBL; AF067817; AAC79695.1; -; mRNA.
DR EMBL; AF118887; AAD20349.1; -; mRNA.
DR EMBL; AF118886; AAD20348.1; -; mRNA.
DR EMBL; AK304088; BAG64994.1; -; mRNA.
DR EMBL; AK316295; BAH14666.1; -; mRNA.
DR EMBL; AC114491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL513206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471156; EAW51252.1; -; Genomic_DNA.
DR EMBL; BC143969; AAI43970.1; -; mRNA.
DR CCDS; CCDS44181.1; -. [Q9UKW4-3]
DR CCDS; CCDS785.1; -. [Q9UKW4-1]
DR RefSeq; NP_001073343.1; NM_001079874.1. [Q9UKW4-3]
DR RefSeq; NP_006104.4; NM_006113.4. [Q9UKW4-1]
DR RefSeq; XP_005270417.1; XM_005270360.2. [Q9UKW4-2]
DR PDB; 2D86; NMR; -; A=1-130.
DR PDBsum; 2D86; -.
DR AlphaFoldDB; Q9UKW4; -.
DR BMRB; Q9UKW4; -.
DR SMR; Q9UKW4; -.
DR BioGRID; 115715; 45.
DR IntAct; Q9UKW4; 23.
DR MINT; Q9UKW4; -.
DR STRING; 9606.ENSP00000359073; -.
DR iPTMnet; Q9UKW4; -.
DR PhosphoSitePlus; Q9UKW4; -.
DR BioMuta; VAV3; -.
DR DMDM; 12643372; -.
DR EPD; Q9UKW4; -.
DR jPOST; Q9UKW4; -.
DR MassIVE; Q9UKW4; -.
DR MaxQB; Q9UKW4; -.
DR PaxDb; Q9UKW4; -.
DR PeptideAtlas; Q9UKW4; -.
DR PRIDE; Q9UKW4; -.
DR ProteomicsDB; 84896; -. [Q9UKW4-1]
DR ProteomicsDB; 84897; -. [Q9UKW4-2]
DR ProteomicsDB; 84898; -. [Q9UKW4-3]
DR ProteomicsDB; 84899; -. [Q9UKW4-4]
DR ABCD; Q9UKW4; 2 sequenced antibodies.
DR Antibodypedia; 4549; 358 antibodies from 37 providers.
DR DNASU; 10451; -.
DR Ensembl; ENST00000370056.9; ENSP00000359073.4; ENSG00000134215.16. [Q9UKW4-1]
DR Ensembl; ENST00000415432.6; ENSP00000394897.2; ENSG00000134215.16. [Q9UKW4-3]
DR Ensembl; ENST00000527011.5; ENSP00000432540.1; ENSG00000134215.16. [Q9UKW4-4]
DR GeneID; 10451; -.
DR KEGG; hsa:10451; -.
DR MANE-Select; ENST00000370056.9; ENSP00000359073.4; NM_006113.5; NP_006104.4.
DR UCSC; uc001dvj.2; human. [Q9UKW4-1]
DR CTD; 10451; -.
DR DisGeNET; 10451; -.
DR GeneCards; VAV3; -.
DR HGNC; HGNC:12659; VAV3.
DR HPA; ENSG00000134215; Tissue enhanced (kidney).
DR MIM; 605541; gene.
DR neXtProt; NX_Q9UKW4; -.
DR OpenTargets; ENSG00000134215; -.
DR PharmGKB; PA37282; -.
DR VEuPathDB; HostDB:ENSG00000134215; -.
DR eggNOG; KOG2996; Eukaryota.
DR GeneTree; ENSGT00940000155252; -.
DR HOGENOM; CLU_013787_0_0_1; -.
DR InParanoid; Q9UKW4; -.
DR OMA; NEDPVGE; -.
DR OrthoDB; 710582at2759; -.
DR PhylomeDB; Q9UKW4; -.
DR TreeFam; TF316171; -.
DR PathwayCommons; Q9UKW4; -.
DR Reactome; R-HSA-114604; GPVI-mediated activation cascade.
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-2424491; DAP12 signaling.
DR Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
DR Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR Reactome; R-HSA-9748787; Azathioprine ADME.
DR SignaLink; Q9UKW4; -.
DR SIGNOR; Q9UKW4; -.
DR BioGRID-ORCS; 10451; 12 hits in 1071 CRISPR screens.
DR ChiTaRS; VAV3; human.
DR EvolutionaryTrace; Q9UKW4; -.
DR GeneWiki; VAV3; -.
DR GenomeRNAi; 10451; -.
DR Pharos; Q9UKW4; Tbio.
DR PRO; PR:Q9UKW4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UKW4; protein.
DR Bgee; ENSG00000134215; Expressed in tongue squamous epithelium and 170 other tissues.
DR ExpressionAtlas; Q9UKW4; baseline and differential.
DR Genevisible; Q9UKW4; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0001772; C:immunological synapse; IDA:CACAO.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; TAS:ProtInc.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; EXP:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0030593; P:neutrophil chemotaxis; IEA:Ensembl.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IEA:Ensembl.
DR GO; GO:0008361; P:regulation of cell size; IGI:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IGI:UniProtKB.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:ProtInc.
DR GO; GO:0006906; P:vesicle fusion; IEA:Ensembl.
DR CDD; cd00029; C1; 1.
DR CDD; cd00014; CH; 1.
DR CDD; cd01223; PH_Vav; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd10407; SH2_Vav3; 1.
DR CDD; cd11978; SH3_VAV3_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; IPR035881; VAV3_SH2.
DR InterPro; IPR035734; VAV3_SH3_2.
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; PF07653; SH3_2; 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; 2.
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 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Alternative splicing;
KW Angiogenesis; Guanine-nucleotide releasing factor; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; SH2 domain; SH3 domain; Zinc;
KW Zinc-finger.
FT CHAIN 1..847
FT /note="Guanine nucleotide exchange factor VAV3"
FT /id="PRO_0000080986"
FT DOMAIN 1..119
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 192..371
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 400..502
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 672..766
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 788..847
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 513..562
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 560..847
FT /note="Sufficient for interaction with ROS1"
FT /evidence="ECO:0000269|PubMed:11094073"
FT MOD_RES 141
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..560
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9705494"
FT /id="VSP_041360"
FT VAR_SEQ 1..107
FT /note="MEPWKQCAQWLIHCKVLPTNHRVTWDSAQVFDLAQTLRDGVLLCQLLNNLRA
FT HSINLKEINLRPQMSQFLCLKNIRTFLTACCETFGMRKSELFEAFDLFDVRDFGK ->
FT MQLPDCPCRAHLP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10523675"
FT /id="VSP_001820"
FT VAR_SEQ 561..568
FT /note="NCGRVNSG -> MPIFTFLS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9705494"
FT /id="VSP_041361"
FT VAR_SEQ 783..784
FT /note="SL -> SSPSLFCGFSFVTPPDYSFVPPSSTPFWSV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042359"
FT VARIANT 139
FT /note="D -> N (in dbSNP:rs34318889)"
FT /id="VAR_061800"
FT VARIANT 298
FT /note="T -> S (in dbSNP:rs7528153)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9705494"
FT /id="VAR_033522"
FT VARIANT 616
FT /note="P -> S (in dbSNP:rs12410676)"
FT /id="VAR_051998"
FT VARIANT 618
FT /note="Q -> H (in dbSNP:rs12403266)"
FT /id="VAR_033523"
FT CONFLICT 107
FT /note="K -> E (in Ref. 1; AAC79695)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="Y -> H (in Ref. 2; AAD20348)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="V -> A (in Ref. 2; AAD20348)"
FT /evidence="ECO:0000305"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:2D86"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:2D86"
FT HELIX 41..50
FT /evidence="ECO:0007829|PDB:2D86"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:2D86"
FT HELIX 68..84
FT /evidence="ECO:0007829|PDB:2D86"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:2D86"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:2D86"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:2D86"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:2D86"
SQ SEQUENCE 847 AA; 97776 MW; C1E29F0B094CB721 CRC64;
MEPWKQCAQW LIHCKVLPTN HRVTWDSAQV FDLAQTLRDG VLLCQLLNNL RAHSINLKEI
NLRPQMSQFL CLKNIRTFLT ACCETFGMRK SELFEAFDLF DVRDFGKVIE TLSRLSRTPI
ALATGIRPFP TEESINDEDI YKGLPDLIDE TLVEDEEDLY DCVYGEDEGG EVYEDLMKAE
EAHQPKCPEN DIRSCCLAEI KQTEEKYTET LESIEKYFMA PLKRFLTAAE FDSVFINIPE
LVKLHRNLMQ EIHDSIVNKN DQNLYQVFIN YKERLVIYGQ YCSGVESAIS SLDYISKTKE
DVKLKLEECS KRANNGKFTL RDLLVVPMQR VLKYHLLLQE LVKHTTDPTE KANLKLALDA
MKDLAQYVNE VKRDNETLRE IKQFQLSIEN LNQPVLLFGR PQGDGEIRIT TLDKHTKQER
HIFLFDLAVI VCKRKGDNYE MKEIIDLQQY KIANNPTTDK ENKKWSYGFY LIHTQGQNGL
EFYCKTKDLK KKWLEQFEMA LSNIRPDYAD SNFHDFKMHT FTRVTSCKVC QMLLRGTFYQ
GYLCFKCGAR AHKECLGRVD NCGRVNSGEQ GTLKLPEKRT NGLRRTPKQV DPGLPKMQVI
RNYSGTPPPA LHEGPPLQLQ AGDTVELLKG DAHSLFWQGR NLASGEVGFF PSDAVKPCPC
VPKPVDYSCQ PWYAGAMERL QAETELINRV NSTYLVRHRT KESGEYAISI KYNNEAKHIK
ILTRDGFFHI AENRKFKSLM ELVEYYKHHS LKEGFRTLDT TLQFPYKEPE HSAGQRGNRA
GNSLLSPKVL GIAIARYDFC ARDMRELSLL KGDVVKIYTK MSANGWWRGE VNGRVGWFPS
TYVEEDE
