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Protein

Protein vav

Gene

Vav

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri552 – 60150Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • Rac guanyl-nucleotide exchange factor activity Source: FlyBase

GO - Biological processi

  • actin cytoskeleton reorganization Source: FlyBase
  • actin filament organization Source: FlyBase
  • axon guidance Source: FlyBase
  • axonogenesis Source: FlyBase
  • cell adhesion Source: FlyBase
  • cell migration Source: FlyBase
  • central nervous system development Source: FlyBase
  • dorsal closure Source: FlyBase
  • intracellular signal transduction Source: InterPro
  • melanotic encapsulation of foreign target Source: FlyBase
  • myoblast fusion Source: FlyBase
  • open tracheal system development Source: FlyBase
  • photoreceptor cell axon guidance Source: FlyBase
  • positive regulation of GTPase activity Source: GOC
  • regulation of cell shape Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_273164. Rho GTPase cycle.
REACT_275007. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_277617. GPVI-mediated activation cascade.
REACT_309033. G alpha (12/13) signalling events.
REACT_316445. Regulation of signaling by CBL.
REACT_318317. Signal transduction by L1.
REACT_331500. EPH-ephrin mediated repulsion of cells.
REACT_334486. Signaling by SCF-KIT.
REACT_336401. Interleukin-3, 5 and GM-CSF signaling.
REACT_339689. PIP3 activates AKT signaling.
REACT_346571. VEGFA-VEGFR2 Pathway.
REACT_347326. NRAGE signals death through JNK.
SignaLinkiQ9NHV9.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein vav
Short name:
DroVav
Short name:
dVAV
Gene namesi
Name:Vav
ORF Names:CG7893
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0040068. Vav.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 793793Protein vavPRO_0000080983Add
BLAST

Post-translational modificationi

Phosphorylated on tyrosine residues.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9NHV9.
PRIDEiQ9NHV9.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Developmental stagei

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

Gene expression databases

BgeeiQ9NHV9.
GenevisibleiQ9NHV9. DM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi7227.FBpp0112228.

Structurei

3D structure databases

ProteinModelPortaliQ9NHV9.
SMRiQ9NHV9. Positions 12-601, 618-783.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 136119CHPROSITE-ProRule annotationAdd
BLAST
Domaini216 – 396181DHPROSITE-ProRule annotationAdd
BLAST
Domaini432 – 541110PHPROSITE-ProRule annotationAdd
BLAST
Domaini622 – 726105SH2PROSITE-ProRule annotationAdd
BLAST
Domaini726 – 78863SH3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CH (calponin-homology) domain.PROSITE-ProRule annotation
Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri552 – 60150Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, SH2 domain, SH3 domain, Zinc-finger

Phylogenomic databases

eggNOGiNOG326494.
GeneTreeiENSGT00800000124085.
InParanoidiQ9NHV9.
OrthoDBiEOG78SQH7.
PhylomeDBiQ9NHV9.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR000219. DH-domain.
IPR002219. PE/DAG-bd.
IPR011993. PH-like_dom.
IPR001849. PH_domain.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF00307. CH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00017. SH2. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00109. 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]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50021. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: Q9NHV9-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MASSSSSNSF GGVAGVNGDL WRECVAWLTR CKVIPPDHKA AQPDAEIRIL
60 70 80 90 100
AMTLRDGVLL CNLVIHLDPS SLDPREFNRK PQMAQFLCSK NIKLFLDVCH
110 120 130 140 150
NNFGIRDADL FEPTMLYDLT NFHRVLITLS KLSQCRKVQQ LHPDLIGFNL
160 170 180 190 200
QLSPTERSHS DEAIYKDLHS TTTDNIACNG TGYDHTNTKE EEVYQDLCAL
210 220 230 240 250
HRTSRSQTAS STSFEQRDYV IRELIDTESN YLDVLTALKT KFMGPLERHL
260 270 280 290 300
NQDELRLIFP RIRELVDIHT KFLDKLRESL TPNAKVKMAQ VFLDFREPFL
310 320 330 340 350
IYGEFCSLLL GAIDYLADVC KKNQIIDQLV QKCERDYNVG KLQLRDILSV
360 370 380 390 400
PMQRILKYHL LLDKLVKETS PLHDDYRSLE RAKEAMIDVS QYINEVKRDS
410 420 430 440 450
DHLVIIQKVK DSICDIHLLQ NGNGSDLLQY GRLLLDGELH IKAHEDQKTK
460 470 480 490 500
LRYAFVFDKI LIMVKALHIK TGDMQYTYRD SHNLADYRVE QSHSRRTIGR
510 520 530 540 550
DTRFKYQLLL ARKSGKTAFT LYLKSEHERD KWRKALTEAM ESLEPPGCQS
560 570 580 590 600
TDHKMEIYTF DAPTTCRHCS KFLKGRIHQG YRCKVCQISV HKGCISSTGR
610 620 630 640 650
CKQNPVSVPP PVCDRQLSEF NWFAGNMDRE TAAHRLENRR IGTYLLRVRP
660 670 680 690 700
QGPSTAHETM YALSLKTDDN VIKHMKINQE NSGDSMLYCL SSRRHFKTIV
710 720 730 740 750
ELVSYYERND LGENFAGLNQ SLQWPYKEVI ATALYDYEPK AGSNQLQLRT
760 770 780 790
DCQVLVIGKD GDSKGWWRGK IGDTVGYFPK EYVQEQKLAS EEL
Length:793
Mass (Da):91,355
Last modified:July 11, 2002 - v2
Checksum:i1031929FE4FB8BF3
GO
Isoform B (identifier: Q9NHV9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-171: MASSSSSNSF...EAIYKDLHST → MRRMRASRRP...LPSRRRPNPS

Note: No experimental confirmation available.
Show »
Length:766
Mass (Da):88,953
Checksum:iA53E704D4DEEF085
GO

Sequence cautioni

The sequence AAM12266.1 differs from that shown.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531T → M in AAF28765 (PubMed:10781813).Curated
Sequence conflicti148 – 1481F → L in AAF28765 (PubMed:10781813).Curated
Sequence conflicti372 – 3721L → M in AAF28765 (PubMed:10781813).Curated
Sequence conflicti503 – 5031R → E in AAF28765 (PubMed:10781813).Curated
Sequence conflicti645 – 66420LLRVR…MYALS → PVASSSAGPIHCPRDDVCAY in AAF28765 (PubMed:10781813).CuratedAdd
BLAST
Sequence conflicti739 – 7391P → Q in AAF28765 (PubMed:10781813).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 171171MASSS…DLHST → MRRMRASRRPCFPTARAAMC ASYPSISPWMWLAPRRMPHP MRSHPRRNRMPANRNHRWPP QRQAFLCPLHRGHLWAVWCP PPPHRRRFWSARASGCSERP PPSTTTAPRWRPPSTSMPTS TARTTRRSTRICATLPSRRR PNPS in isoform B. 1 PublicationVSP_027801Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_573372.1. NM_133144.4. [Q9NHV9-1]
NP_728235.1. NM_167642.3. [Q9NHV9-1]
UniGeneiDm.218.

Genome annotation databases

EnsemblMetazoaiFBtr0074677; FBpp0074448; FBgn0040068. [Q9NHV9-1]
FBtr0074678; FBpp0074449; FBgn0040068. [Q9NHV9-1]
GeneIDi32920.
UCSCiCG7893-RA. d. melanogaster. [Q9NHV9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_573372.1. NM_133144.4. [Q9NHV9-1]
NP_728235.1. NM_167642.3. [Q9NHV9-1]
UniGeneiDm.218.

3D structure databases

ProteinModelPortaliQ9NHV9.
SMRiQ9NHV9. Positions 12-601, 618-783.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0112228.

Proteomic databases

PaxDbiQ9NHV9.
PRIDEiQ9NHV9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0074677; FBpp0074448; FBgn0040068. [Q9NHV9-1]
FBtr0074678; FBpp0074449; FBgn0040068. [Q9NHV9-1]
GeneIDi32920.
UCSCiCG7893-RA. d. melanogaster. [Q9NHV9-1]

Organism-specific databases

CTDi32920.
FlyBaseiFBgn0040068. Vav.

Phylogenomic databases

eggNOGiNOG326494.
GeneTreeiENSGT00800000124085.
InParanoidiQ9NHV9.
OrthoDBiEOG78SQH7.
PhylomeDBiQ9NHV9.

Enzyme and pathway databases

ReactomeiREACT_273164. Rho GTPase cycle.
REACT_275007. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_277617. GPVI-mediated activation cascade.
REACT_309033. G alpha (12/13) signalling events.
REACT_316445. Regulation of signaling by CBL.
REACT_318317. Signal transduction by L1.
REACT_331500. EPH-ephrin mediated repulsion of cells.
REACT_334486. Signaling by SCF-KIT.
REACT_336401. Interleukin-3, 5 and GM-CSF signaling.
REACT_339689. PIP3 activates AKT signaling.
REACT_346571. VEGFA-VEGFR2 Pathway.
REACT_347326. NRAGE signals death through JNK.
SignaLinkiQ9NHV9.

Miscellaneous databases

GenomeRNAii32920.
NextBioi781038.
PROiQ9NHV9.

Gene expression databases

BgeeiQ9NHV9.
GenevisibleiQ9NHV9. DM.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR000219. DH-domain.
IPR002219. PE/DAG-bd.
IPR011993. PH-like_dom.
IPR001849. PH_domain.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF00307. CH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00017. SH2. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00109. 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]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50021. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. 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.

Entry informationi

Entry nameiVAV_DROME
AccessioniPrimary (citable) accession number: Q9NHV9
Secondary accession number(s): A2RVJ3
, A4V4R6, Q8SWT3, Q8T061, Q9VWJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: July 11, 2002
Last modified: July 22, 2015
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.