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   24-JAN-2024, entry version 188.
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   STRING; 7227.FBpp0112228; -.
DR   PeptideAtlas; 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   AGR; FB:FBgn0040068; -.
DR   CTD; 32920; -.
DR   FlyBase; FBgn0040068; Vav.
DR   VEuPathDB; VectorBase:FBgn0040068; -.
DR   eggNOG; KOG2996; Eukaryota.
DR   GeneTree; ENSGT00940000168738; -.
DR   InParanoid; Q9NHV9; -.
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-9013148; CDC42 GTPase cycle.
DR   Reactome; R-DME-9013149; RAC1 GTPase cycle.
DR   Reactome; R-DME-9013423; RAC3 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 cell types or 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:0030036; P:actin cytoskeleton organization; 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: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:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:FlyBase.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:FlyBase.
DR   GO; GO:1903391; P:regulation of adherens junction organization; IMP:FlyBase.
DR   GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IDA:FlyBase.
DR   CDD; cd20810; C1_VAV; 1.
DR   CDD; cd21201; CH_VAV; 1.
DR   CDD; cd01223; PH_Vav; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   CDD; cd09940; SH2_Vav_family; 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; 1.
DR   InterPro; IPR001715; CH_dom.
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   PANTHER; PTHR45818; PROTEIN VAV; 1.
DR   PANTHER; PTHR45818:SF3; PROTEIN VAV; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF15411; PH_10; 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; 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; 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
//

ID   A8JUQ9_DROME            Unreviewed;      1001 AA.
AC   A8JUQ9;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   24-JAN-2024, entry version 135.
DE   SubName: Full=Vav guanine nucleotide exchange factor, isoform C {ECO:0000313|EMBL:ABW09454.1};
GN   Name=Vav {ECO:0000313|EMBL:ABW09454.1,
GN   ECO:0000313|FlyBase:FBgn0040068};
GN   Synonyms=BcDNA:GH01128 {ECO:0000313|EMBL:ABW09454.1}, Dmel\CG7893
GN   {ECO:0000313|EMBL:ABW09454.1}, DmVav {ECO:0000313|EMBL:ABW09454.1},
GN   DroVav {ECO:0000313|EMBL:ABW09454.1}, vav
GN   {ECO:0000313|EMBL:ABW09454.1};
GN   ORFNames=CG7893 {ECO:0000313|EMBL:ABW09454.1,
GN   ECO:0000313|FlyBase:FBgn0040068}, Dmel_CG7893
GN   {ECO:0000313|EMBL:ABW09454.1};
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 {ECO:0000313|EMBL:ABW09454.1, ECO:0000313|Proteomes:UP000000803};
RN   [1] {ECO:0000313|EMBL:ABW09454.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J., 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., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA   Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA   Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA   Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA   Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA   Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA   Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000313|EMBL:ABW09454.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537568;
RA   Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA   Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA   George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA   Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA   Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA   Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT   "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT   euchromatic genome sequence.";
RL   Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN   [3] {ECO:0000313|EMBL:ABW09454.1, ECO:0000313|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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] {ECO:0000313|EMBL:ABW09454.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537573;
RA   Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA   Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA   Celniker S.E.;
RT   "The transposable elements of the Drosophila melanogaster euchromatin: a
RT   genomics perspective.";
RL   Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN   [5] {ECO:0000313|EMBL:ABW09454.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537574;
RA   Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA   Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA   Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA   Karpen G.H.;
RT   "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL   Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN   [6] {ECO:0000313|EMBL:ABW09454.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA   Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA   Ashburner M., Anxolabehere D.;
RT   "Combined evidence annotation of transposable elements in genome
RT   sequences.";
RL   PLoS Comput. Biol. 1:166-175(2005).
RN   [7] {ECO:0000313|EMBL:ABW09454.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569856; DOI=10.1126/science.1139815;
RA   Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT   "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL   Science 316:1586-1591(2007).
RN   [8] {ECO:0000313|EMBL:ABW09454.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569867; DOI=10.1126/science.1139816;
RA   Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA   Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA   Dimitri P., Karpen G.H., Celniker S.E.;
RT   "Sequence finishing and mapping of Drosophila melanogaster
RT   heterochromatin.";
RL   Science 316:1625-1628(2007).
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DR   EMBL; AE014298; ABW09454.1; -; Genomic_DNA.
DR   RefSeq; NP_001097030.1; NM_001103560.3.
DR   AlphaFoldDB; A8JUQ9; -.
DR   SMR; A8JUQ9; -.
DR   PaxDb; 7227-FBpp0112228; -.
DR   EnsemblMetazoa; FBtr0113316; FBpp0112228; FBgn0040068.
DR   GeneID; 32920; -.
DR   UCSC; CG7893-RC; d. melanogaster.
DR   AGR; FB:FBgn0040068; -.
DR   CTD; 32920; -.
DR   FlyBase; FBgn0040068; Vav.
DR   VEuPathDB; VectorBase:FBgn0040068; -.
DR   GeneTree; ENSGT00940000168738; -.
DR   OMA; LELACIH; -.
DR   OrthoDB; 2911406at2759; -.
DR   PhylomeDB; A8JUQ9; -.
DR   BioGRID-ORCS; 32920; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 32920; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0040068; Expressed in brain and 48 other cell types or tissues.
DR   ExpressionAtlas; A8JUQ9; baseline and differential.
DR   Genevisible; A8JUQ9; DM.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR   GO; GO:0048468; P:cell development; IEA:UniProt.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0060429; P:epithelium development; IEA:UniProt.
DR   CDD; cd20810; C1_VAV; 1.
DR   CDD; cd21201; CH_VAV; 1.
DR   CDD; cd01223; PH_Vav; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   CDD; cd09940; SH2_Vav_family; 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; 1.
DR   InterPro; IPR001715; CH_dom.
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   PANTHER; PTHR45818; PROTEIN VAV; 1.
DR   PANTHER; PTHR45818:SF3; PROTEIN VAV; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF15411; PH_10; 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; 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; 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   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:A8JUQ9};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          18..137
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          424..604
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          640..749
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          760..809
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          830..934
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          934..996
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          186..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..295
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1001 AA;  113585 MW;  24AD55A2BAEEE999 CRC64;
     MASSSSSNSF GGVAGVNGDL WRECVAWLTR CKVIPPDHKA AQPDAEIRIL AMTLRDGVLL
     CNLVIHLDPS SLDPREFNRK PQMAQFLCSK NIKLFLDVCH NNFGIRDADL FEPTMLYDLT
     NFHRVLITLS KLSQCRKVQQ LHPDLIGFNL QLSPTERSHS DEAIYKDLHS TDLNMRKTSS
     IDASASSSAE YYDRTSQSGS LDENSDITIE NGTEDIDDYI EDSLSNMCDS TIDNDAEDAG
     VETPLLSDCQ GSHVRELSFD LALDVVSSTT DGASNAVTPT PESYARQSQS PLAAAAPSVP
     VSAAPGPPMG RLVSTSSSSS SLLVSESQRL QRAAAAVYNY RSSMASTEHE YAYIYSEDDE
     KVYEDLCYVT FQAKAKPEVT TDNIACNGTG YDHTNTKEEE VYQDLCALHR TSRSQTASST
     SFEQRDYVIR ELIDTESNYL DVLTALKTKF MGPLERHLNQ DELRLIFPRI RELVDIHTKF
     LDKLRESLTP NAKVKMAQVF LDFREPFLIY GEFCSLLLGA IDYLADVCKK NQIIDQLVQK
     CERDYNVGKL QLRDILSVPM QRILKYHLLL DKLVKETSPL HDDYRSLERA KEAMIDVSQY
     INEVKRDSDH LVIIQKVKDS ICDIHLLQNG NGSDLLQYGR LLLDGELHIK AHEDQKTKLR
     YAFVFDKILI MVKALHIKTG DMQYTYRDSH NLADYRVEQS HSRRTIGRDT RFKYQLLLAR
     KSGKTAFTLY LKSEHERDKW RKALTEAMES LEPPGCQSTD HKMEIYTFDA PTTCRHCSKF
     LKGRIHQGYR CKVCQISVHK GCISSTGRCK QNPVSVPPPV CDRQLSEFNW FAGNMDRETA
     AHRLENRRIG TYLLRVRPQG PSTAHETMYA LSLKTDDNVI KHMKINQENS GDSMLYCLSS
     RRHFKTIVEL VSYYERNDLG ENFAGLNQSL QWPYKEVIAT ALYDYEPKAG SNQLQLRTDC
     QVLVIGKDGD SKGWWRGKIG DTVGYFPKEY VQEQKLASEE L
//

ID   M9PHJ6_DROME            Unreviewed;       964 AA.
AC   M9PHJ6;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   SubName: Full=Vav guanine nucleotide exchange factor, isoform D {ECO:0000313|EMBL:AGB95543.1};
GN   Name=Vav {ECO:0000313|EMBL:AGB95543.1,
GN   ECO:0000313|FlyBase:FBgn0040068};
GN   Synonyms=BcDNA:GH01128 {ECO:0000313|EMBL:AGB95543.1}, Dmel\CG7893
GN   {ECO:0000313|EMBL:AGB95543.1}, DmVav {ECO:0000313|EMBL:AGB95543.1},
GN   DroVav {ECO:0000313|EMBL:AGB95543.1}, vav
GN   {ECO:0000313|EMBL:AGB95543.1};
GN   ORFNames=CG7893 {ECO:0000313|EMBL:AGB95543.1,
GN   ECO:0000313|FlyBase:FBgn0040068}, Dmel_CG7893
GN   {ECO:0000313|EMBL:AGB95543.1};
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 {ECO:0000313|EMBL:AGB95543.1, ECO:0000313|Proteomes:UP000000803};
RN   [1] {ECO:0000313|EMBL:AGB95543.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J., 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., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA   Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA   Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA   Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA   Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA   Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA   Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000313|EMBL:AGB95543.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537568;
RA   Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA   Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA   George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA   Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA   Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA   Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT   "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT   euchromatic genome sequence.";
RL   Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN   [3] {ECO:0000313|EMBL:AGB95543.1, ECO:0000313|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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] {ECO:0000313|EMBL:AGB95543.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537573;
RA   Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA   Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA   Celniker S.E.;
RT   "The transposable elements of the Drosophila melanogaster euchromatin: a
RT   genomics perspective.";
RL   Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN   [5] {ECO:0000313|EMBL:AGB95543.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537574;
RA   Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA   Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA   Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA   Karpen G.H.;
RT   "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL   Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN   [6] {ECO:0000313|EMBL:AGB95543.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA   Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA   Ashburner M., Anxolabehere D.;
RT   "Combined evidence annotation of transposable elements in genome
RT   sequences.";
RL   PLoS Comput. Biol. 1:166-175(2005).
RN   [7] {ECO:0000313|EMBL:AGB95543.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569856; DOI=10.1126/science.1139815;
RA   Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT   "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL   Science 316:1586-1591(2007).
RN   [8] {ECO:0000313|EMBL:AGB95543.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569867; DOI=10.1126/science.1139816;
RA   Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA   Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA   Dimitri P., Karpen G.H., Celniker S.E.;
RT   "Sequence finishing and mapping of Drosophila melanogaster
RT   heterochromatin.";
RL   Science 316:1625-1628(2007).
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DR   EMBL; AE014298; AGB95543.1; -; Genomic_DNA.
DR   RefSeq; NP_001259703.1; NM_001272774.1.
DR   AlphaFoldDB; M9PHJ6; -.
DR   SMR; M9PHJ6; -.
DR   EnsemblMetazoa; FBtr0333759; FBpp0305901; FBgn0040068.
DR   GeneID; 32920; -.
DR   AGR; FB:FBgn0040068; -.
DR   CTD; 32920; -.
DR   FlyBase; FBgn0040068; Vav.
DR   VEuPathDB; VectorBase:FBgn0040068; -.
DR   GeneTree; ENSGT00940000168738; -.
DR   HOGENOM; CLU_013787_0_0_1; -.
DR   OrthoDB; 2911406at2759; -.
DR   BioGRID-ORCS; 32920; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 32920; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0040068; Expressed in brain and 48 other cell types or tissues.
DR   ExpressionAtlas; M9PHJ6; baseline and differential.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR   GO; GO:0048468; P:cell development; IEA:UniProt.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0060429; P:epithelium development; IEA:UniProt.
DR   CDD; cd20810; C1_VAV; 1.
DR   CDD; cd21201; CH_VAV; 1.
DR   CDD; cd01223; PH_Vav; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   CDD; cd09940; SH2_Vav_family; 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; 1.
DR   InterPro; IPR001715; CH_dom.
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   PANTHER; PTHR45818; PROTEIN VAV; 1.
DR   PANTHER; PTHR45818:SF3; PROTEIN VAV; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF15411; PH_10; 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; 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; 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   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:M9PHJ6};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          18..137
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          387..567
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          603..712
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          723..772
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          793..897
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          897..959
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          186..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..295
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   964 AA;  109432 MW;  6975B6E42EEE124E CRC64;
     MASSSSSNSF GGVAGVNGDL WRECVAWLTR CKVIPPDHKA AQPDAEIRIL AMTLRDGVLL
     CNLVIHLDPS SLDPREFNRK PQMAQFLCSK NIKLFLDVCH NNFGIRDADL FEPTMLYDLT
     NFHRVLITLS KLSQCRKVQQ LHPDLIGFNL QLSPTERSHS DEAIYKDLHS TDLNMRKTSS
     IDASASSSAE YYDRTSQSGS LDENSDITIE NGTEDIDDYI EDSLSNMCDS TIDNDAEDAG
     VETPLLSDCQ GSHVRELSFD LALDVVSSTT DGASNAVTPT PESYARQSQS PLAAAAPSVP
     VSAAPGPPMG RLVSTSSSSS SLLVSESQRL QRAAAAVYNY RSSMASTEHE YAYIYSEDDE
     KVYEDLCYVT FQAKAKPETA SSTSFEQRDY VIRELIDTES NYLDVLTALK TKFMGPLERH
     LNQDELRLIF PRIRELVDIH TKFLDKLRES LTPNAKVKMA QVFLDFREPF LIYGEFCSLL
     LGAIDYLADV CKKNQIIDQL VQKCERDYNV GKLQLRDILS VPMQRILKYH LLLDKLVKET
     SPLHDDYRSL ERAKEAMIDV SQYINEVKRD SDHLVIIQKV KDSICDIHLL QNGNGSDLLQ
     YGRLLLDGEL HIKAHEDQKT KLRYAFVFDK ILIMVKALHI KTGDMQYTYR DSHNLADYRV
     EQSHSRRTIG RDTRFKYQLL LARKSGKTAF TLYLKSEHER DKWRKALTEA MESLEPPGCQ
     STDHKMEIYT FDAPTTCRHC SKFLKGRIHQ GYRCKVCQIS VHKGCISSTG RCKQNPVSVP
     PPVCDRQLSE FNWFAGNMDR ETAAHRLENR RIGTYLLRVR PQGPSTAHET MYALSLKTDD
     NVIKHMKINQ ENSGDSMLYC LSSRRHFKTI VELVSYYERN DLGENFAGLN QSLQWPYKEV
     IATALYDYEP KAGSNQLQLR TDCQVLVIGK DGDSKGWWRG KIGDTVGYFP KEYVQEQKLA
     SEEL
//