VAV_DROME
ID VAV_DROME Reviewed; 793 AA.
AC Q9NHV9; A2RVJ3; A4V4R6; Q8SWT3; Q8T061; Q9VWJ5;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Protein vav;
DE Short=DroVav;
DE Short=dVAV;
GN Name=Vav; ORFNames=CG7893;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROBABLE FUNCTION, INTERACTION WITH
RP EGFR, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
RC TISSUE=Embryo;
RX PubMed=10781813; DOI=10.1016/s0014-5793(00)01413-7;
RA Dekel I., Russek N., Jones T., Mortin M.A., Katzav S.;
RT "Identification of the Drosophila melanogaster homologue of the mammalian
RT signal transducer protein, Vav.";
RL FEBS Lett. 472:99-104(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Head, Larva, and Pupae;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Couples tyrosine kinase signals with the activation of the
CC Rho/Rac GTPases. Probably plays a pivotal role as a signal transducer
CC protein during fruit fly development.
CC -!- SUBUNIT: Interacts (via SH2 domain) with Egfr (when phosphorylated on
CC tyrosine residues). {ECO:0000269|PubMed:10781813}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q9NHV9-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9NHV9-2; Sequence=VSP_027801;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10781813}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically in all
CC stages of development. {ECO:0000269|PubMed:10781813}.
CC -!- PTM: Phosphorylated on tyrosine residues.
CC {ECO:0000269|PubMed:10781813}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM12266.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR EMBL; AF218780; AAF28765.1; -; mRNA.
DR EMBL; AE014298; AAF48943.3; -; Genomic_DNA.
DR EMBL; AE014298; AAN09485.1; -; Genomic_DNA.
DR EMBL; AY069536; AAL39681.1; -; mRNA.
DR EMBL; AY095173; AAM12266.1; ALT_SEQ; mRNA.
DR EMBL; BT029984; ABM92858.1; -; mRNA.
DR RefSeq; NP_573372.1; NM_133144.4. [Q9NHV9-1]
DR RefSeq; NP_728235.1; NM_167642.3. [Q9NHV9-1]
DR AlphaFoldDB; Q9NHV9; -.
DR SMR; Q9NHV9; -.
DR BioGRID; 59225; 11.
DR PaxDb; Q9NHV9; -.
DR PeptideAtlas; Q9NHV9; -.
DR PRIDE; Q9NHV9; -.
DR EnsemblMetazoa; FBtr0074677; FBpp0074448; FBgn0040068. [Q9NHV9-1]
DR EnsemblMetazoa; FBtr0074678; FBpp0074449; FBgn0040068. [Q9NHV9-1]
DR GeneID; 32920; -.
DR KEGG; dme:Dmel_CG7893; -.
DR UCSC; CG7893-RA; d. melanogaster. [Q9NHV9-1]
DR CTD; 32920; -.
DR FlyBase; FBgn0040068; Vav.
DR VEuPathDB; VectorBase:FBgn0040068; -.
DR eggNOG; KOG2996; Eukaryota.
DR GeneTree; ENSGT00940000168738; -.
DR InParanoid; Q9NHV9; -.
DR OMA; NEDPVGE; -.
DR PhylomeDB; Q9NHV9; -.
DR Reactome; R-DME-114604; GPVI-mediated activation cascade.
DR Reactome; R-DME-1257604; PIP3 activates AKT signaling.
DR Reactome; R-DME-1433557; Signaling by SCF-KIT.
DR Reactome; R-DME-193648; NRAGE signals death through JNK.
DR Reactome; R-DME-2424491; DAP12 signaling.
DR Reactome; R-DME-2871796; FCERI mediated MAPK activation.
DR Reactome; R-DME-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-DME-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-DME-416482; G alpha (12/13) signalling events.
DR Reactome; R-DME-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-DME-445144; Signal transduction by L1.
DR Reactome; R-DME-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR Reactome; R-DME-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-DME-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-DME-8980692; RHOA GTPase cycle.
DR Reactome; R-DME-9013026; RHOB GTPase cycle.
DR Reactome; R-DME-9013106; RHOC GTPase cycle.
DR Reactome; R-DME-9013148; CDC42 GTPase cycle.
DR Reactome; R-DME-9013149; RAC1 GTPase cycle.
DR Reactome; R-DME-9027284; Erythropoietin activates RAS.
DR Reactome; R-DME-912631; Regulation of signaling by CBL.
DR Reactome; R-DME-9748787; Azathioprine ADME.
DR Reactome; R-DME-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR SignaLink; Q9NHV9; -.
DR BioGRID-ORCS; 32920; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 32920; -.
DR PRO; PR:Q9NHV9; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0040068; Expressed in brain and 48 other tissues.
DR ExpressionAtlas; Q9NHV9; baseline and differential.
DR Genevisible; Q9NHV9; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:FlyBase.
DR GO; GO:0090630; P:activation of GTPase activity; IDA:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IDA:FlyBase.
DR GO; GO:0016477; P:cell migration; IMP:FlyBase.
DR GO; GO:0007417; P:central nervous system development; IGI:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0051179; P:localization; IEA:UniProt.
DR GO; GO:0035011; P:melanotic encapsulation of foreign target; IMP:FlyBase.
DR GO; GO:0007520; P:myoblast fusion; IMP:FlyBase.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR GO; GO:0072499; P:photoreceptor cell axon guidance; IMP:FlyBase.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:FlyBase.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:FlyBase.
DR GO; GO:1903391; P:regulation of adherens junction organization; IMP:FlyBase.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IDA:FlyBase.
DR CDD; cd00029; C1; 1.
DR CDD; cd01223; PH_Vav; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd09940; SH2_Vav_family; 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; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
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; IPR035031; Vav_SH2_invertebrate.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
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; 1.
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; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Guanine-nucleotide releasing factor; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; SH2 domain; SH3 domain; Zinc;
KW Zinc-finger.
FT CHAIN 1..793
FT /note="Protein vav"
FT /id="PRO_0000080983"
FT DOMAIN 18..137
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 216..396
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 432..541
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 622..726
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 726..788
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 552..601
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT VAR_SEQ 1..171
FT /note="MASSSSSNSFGGVAGVNGDLWRECVAWLTRCKVIPPDHKAAQPDAEIRILAM
FT TLRDGVLLCNLVIHLDPSSLDPREFNRKPQMAQFLCSKNIKLFLDVCHNNFGIRDADLF
FT EPTMLYDLTNFHRVLITLSKLSQCRKVQQLHPDLIGFNLQLSPTERSHSDEAIYKDLHS
FT T -> MRRMRASRRPCFPTARAAMCASYPSISPWMWLAPRRMPHPMRSHPRRNRMPANR
FT NHRWPPQRQAFLCPLHRGHLWAVWCPPPPHRRRFWSARASGCSERPPPSTTTAPRWRPP
FT STSMPTSTARTTRRSTRICATLPSRRRPNPS (in isoform B)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_027801"
FT CONFLICT 53
FT /note="T -> M (in Ref. 1; AAF28765)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="F -> L (in Ref. 1; AAF28765)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="L -> M (in Ref. 1; AAF28765)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="R -> E (in Ref. 1; AAF28765)"
FT /evidence="ECO:0000305"
FT CONFLICT 645..664
FT /note="LLRVRPQGPSTAHETMYALS -> PVASSSAGPIHCPRDDVCAY (in
FT Ref. 1; AAF28765)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="P -> Q (in Ref. 1; AAF28765)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 793 AA; 91355 MW; 1031929FE4FB8BF3 CRC64;
MASSSSSNSF GGVAGVNGDL WRECVAWLTR CKVIPPDHKA AQPDAEIRIL AMTLRDGVLL
CNLVIHLDPS SLDPREFNRK PQMAQFLCSK NIKLFLDVCH NNFGIRDADL FEPTMLYDLT
NFHRVLITLS KLSQCRKVQQ LHPDLIGFNL QLSPTERSHS DEAIYKDLHS TTTDNIACNG
TGYDHTNTKE EEVYQDLCAL HRTSRSQTAS STSFEQRDYV IRELIDTESN YLDVLTALKT
KFMGPLERHL NQDELRLIFP RIRELVDIHT KFLDKLRESL TPNAKVKMAQ VFLDFREPFL
IYGEFCSLLL GAIDYLADVC KKNQIIDQLV QKCERDYNVG KLQLRDILSV PMQRILKYHL
LLDKLVKETS PLHDDYRSLE RAKEAMIDVS QYINEVKRDS DHLVIIQKVK DSICDIHLLQ
NGNGSDLLQY GRLLLDGELH IKAHEDQKTK LRYAFVFDKI LIMVKALHIK TGDMQYTYRD
SHNLADYRVE QSHSRRTIGR DTRFKYQLLL ARKSGKTAFT LYLKSEHERD KWRKALTEAM
ESLEPPGCQS TDHKMEIYTF DAPTTCRHCS KFLKGRIHQG YRCKVCQISV HKGCISSTGR
CKQNPVSVPP PVCDRQLSEF NWFAGNMDRE TAAHRLENRR IGTYLLRVRP QGPSTAHETM
YALSLKTDDN VIKHMKINQE NSGDSMLYCL SSRRHFKTIV ELVSYYERND LGENFAGLNQ
SLQWPYKEVI ATALYDYEPK AGSNQLQLRT DCQVLVIGKD GDSKGWWRGK IGDTVGYFPK
EYVQEQKLAS EEL
