Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9NHV9 (VAV_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein vav

Short name=DroVav
Short name=dVAV
Gene names
Name:Vav
ORF Names:CG7893
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length793 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Couples tyrosine kinase signals with the activation of the Rho/Rac GTPases. Probably plays a pivotal role as a signal transducer protein during fruit fly development. Ref.1

Subunit structure

Interacts (via SH2 domain) with Egfr (when phosphorylated on tyrosine residues). Ref.1

Tissue specificity

Ubiquitous. Ref.1

Developmental stage

Expressed both maternally and zygotically in all stages of development. Ref.1

Post-translational modification

Phosphorylated on tyrosine residues. Ref.1

Sequence similarities

Contains 1 CH (calponin-homology) domain.

Contains 1 DH (DBL-homology) domain.

Contains 1 PH domain.

Contains 1 phorbol-ester/DAG-type zinc finger.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Sequence caution

The sequence AAM12266.1 differs from that shown. Reason:

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   DomainRepeat
SH2 domain
SH3 domain
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionGuanine-nucleotide releasing factor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton reorganization

Inferred from direct assay PubMed 15950967. Source: FlyBase

actin filament organization

Inferred from mutant phenotype PubMed 14527345. Source: FlyBase

activation of Rac GTPase activity

Inferred from direct assay PubMed 15950967. Source: FlyBase

axon guidance

Inferred from mutant phenotype PubMed 15950967PubMed 20147552. Source: FlyBase

axonogenesis

Inferred from mutant phenotype PubMed 20147552. Source: FlyBase

cell adhesion

Inferred from mutant phenotype PubMed 14527345. Source: FlyBase

cell migration

Inferred from mutant phenotype PubMed 15950967. Source: FlyBase

central nervous system development

Inferred from genetic interaction PubMed 20147552. Source: FlyBase

dorsal closure

Inferred from mutant phenotype PubMed 15950967. Source: FlyBase

melanotic encapsulation of foreign target

Inferred from mutant phenotype PubMed 21947570. Source: FlyBase

myoblast fusion

Inferred from mutant phenotype PubMed 15950967. Source: FlyBase

open tracheal system development

Inferred from mutant phenotype PubMed 15950967. Source: FlyBase

photoreceptor cell axon guidance

Inferred from mutant phenotype PubMed 20147552. Source: FlyBase

regulation of Rac GTPase activity

Inferred from direct assay PubMed 15950967. Source: GOC

regulation of cell shape

Inferred from mutant phenotype PubMed 14527345. Source: FlyBase

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

   Molecular_functionRac guanyl-nucleotide exchange factor activity

Inferred from direct assay PubMed 15950967. Source: FlyBase

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q9NHV9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: Q9NHV9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-171: MASSSSSNSF...EAIYKDLHST → MRRMRASRRP...LPSRRRPNPS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 793793Protein vav
PRO_0000080983

Regions

Domain18 – 136119CH
Domain216 – 396181DH
Domain432 – 541110PH
Domain622 – 726105SH2
Domain726 – 78863SH3
Zinc finger552 – 60150Phorbol-ester/DAG-type

Natural variations

Alternative sequence1 – 171171MASSS…DLHST → MRRMRASRRPCFPTARAAMC ASYPSISPWMWLAPRRMPHP MRSHPRRNRMPANRNHRWPP QRQAFLCPLHRGHLWAVWCP PPPHRRRFWSARASGCSERP PPSTTTAPRWRPPSTSMPTS TARTTRRSTRICATLPSRRR PNPS in isoform B.
VSP_027801

Experimental info

Sequence conflict531T → M in AAF28765. Ref.1
Sequence conflict1481F → L in AAF28765. Ref.1
Sequence conflict3721L → M in AAF28765. Ref.1
Sequence conflict5031R → E in AAF28765. Ref.1
Sequence conflict645 – 66420LLRVR…MYALS → PVASSSAGPIHCPRDDVCAY in AAF28765. Ref.1
Sequence conflict7391P → Q in AAF28765. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified July 11, 2002. Version 2.
Checksum: 1031929FE4FB8BF3

FASTA79391,355
        10         20         30         40         50         60 
MASSSSSNSF GGVAGVNGDL WRECVAWLTR CKVIPPDHKA AQPDAEIRIL AMTLRDGVLL 

        70         80         90        100        110        120 
CNLVIHLDPS SLDPREFNRK PQMAQFLCSK NIKLFLDVCH NNFGIRDADL FEPTMLYDLT 

       130        140        150        160        170        180 
NFHRVLITLS KLSQCRKVQQ LHPDLIGFNL QLSPTERSHS DEAIYKDLHS TTTDNIACNG 

       190        200        210        220        230        240 
TGYDHTNTKE EEVYQDLCAL HRTSRSQTAS STSFEQRDYV IRELIDTESN YLDVLTALKT 

       250        260        270        280        290        300 
KFMGPLERHL NQDELRLIFP RIRELVDIHT KFLDKLRESL TPNAKVKMAQ VFLDFREPFL 

       310        320        330        340        350        360 
IYGEFCSLLL GAIDYLADVC KKNQIIDQLV QKCERDYNVG KLQLRDILSV PMQRILKYHL 

       370        380        390        400        410        420 
LLDKLVKETS PLHDDYRSLE RAKEAMIDVS QYINEVKRDS DHLVIIQKVK DSICDIHLLQ 

       430        440        450        460        470        480 
NGNGSDLLQY GRLLLDGELH IKAHEDQKTK LRYAFVFDKI LIMVKALHIK TGDMQYTYRD 

       490        500        510        520        530        540 
SHNLADYRVE QSHSRRTIGR DTRFKYQLLL ARKSGKTAFT LYLKSEHERD KWRKALTEAM 

       550        560        570        580        590        600 
ESLEPPGCQS TDHKMEIYTF DAPTTCRHCS KFLKGRIHQG YRCKVCQISV HKGCISSTGR 

       610        620        630        640        650        660 
CKQNPVSVPP PVCDRQLSEF NWFAGNMDRE TAAHRLENRR IGTYLLRVRP QGPSTAHETM 

       670        680        690        700        710        720 
YALSLKTDDN VIKHMKINQE NSGDSMLYCL SSRRHFKTIV ELVSYYERND LGENFAGLNQ 

       730        740        750        760        770        780 
SLQWPYKEVI ATALYDYEPK AGSNQLQLRT DCQVLVIGKD GDSKGWWRGK IGDTVGYFPK 

       790 
EYVQEQKLAS EEL 

« Hide

Isoform B [UniParc].

Checksum: A53E704D4DEEF085
Show »

FASTA76688,953

References

« Hide 'large scale' references
[1]"Identification of the Drosophila melanogaster homologue of the mammalian signal transducer protein, Vav."
Dekel I., Russek N., Jones T., Mortin M.A., Katzav S.
FEBS Lett. 472:99-104(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROBABLE FUNCTION, INTERACTION WITH EGFR, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION.
Tissue: Embryo.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Strain: Berkeley.
Tissue: Embryo.
[5]Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
Strain: Berkeley.
Tissue: Head, Larva and Pupae.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF218780 mRNA. Translation: AAF28765.1.
AE014298 Genomic DNA. Translation: AAF48943.3.
AE014298 Genomic DNA. Translation: AAN09485.1.
AY069536 mRNA. Translation: AAL39681.1.
AY095173 mRNA. Translation: AAM12266.1. Sequence problems.
BT029984 mRNA. Translation: ABM92858.1.
RefSeqNP_573372.1. NM_133144.4.
NP_728235.1. NM_167642.3.
UniGeneDm.218.

3D structure databases

ProteinModelPortalQ9NHV9.
SMRQ9NHV9. Positions 12-601, 615-785.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ9NHV9.
PRIDEQ9NHV9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0074677; FBpp0074448; FBgn0040068. [Q9NHV9-1]
FBtr0074678; FBpp0074449; FBgn0040068. [Q9NHV9-1]
GeneID32920.
KEGGdme:Dmel_CG7893.
UCSCCG7893-RA. d. melanogaster. [Q9NHV9-1]

Organism-specific databases

CTD32920.
FlyBaseFBgn0040068. Vav.

Phylogenomic databases

eggNOGNOG326494.
GeneTreeENSGT00740000115307.
InParanoidQ9NHV9.
KOK05730.
OrthoDBEOG78SQH7.
PhylomeDBQ9NHV9.

Enzyme and pathway databases

SignaLinkQ9NHV9.

Gene expression databases

BgeeQ9NHV9.

Family and domain databases

Gene3D1.10.418.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProIPR001715. CH-domain.
IPR000219. DH-domain.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR028530. Vav.
[Graphical view]
PANTHERPTHR22826:SF53. PTHR22826:SF53. 1 hit.
PfamPF00130. C1_1. 1 hit.
PF00307. CH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
SMARTSM00109. C1. 1 hit.
SM00033. CH. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF47576. SSF47576. 1 hit.
SSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEPS50021. CH. 1 hit.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi32920.
NextBio781038.

Entry information

Entry nameVAV_DROME
AccessionPrimary (citable) accession number: Q9NHV9
Secondary accession number(s): A2RVJ3 expand/collapse secondary AC list , A4V4R6, Q8SWT3, Q8T061, Q9VWJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: July 11, 2002
Last modified: April 16, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase