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Protein

WAS protein family homolog 1

Gene

wash

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

Functioni

Acts as a nucleation-promoting factor by activating the Arp2/3 complex to induce actin polymerization (PubMed:19633175). Participates in both linear- and branched-actin networks (PubMed:19633175). Functions in linear-filament (bundled F-actin) by acting downstream of Rho1 and regulating actin and microtubule organization during oogenesis (PubMed:19633175). Nucleates actin in an Arp2/3-dependent manner and exhibits F-actin and microtubule bundling and cross-linking activity in the egg chamber (PubMed:19633175). During embryogenesis, acts downstream of Rho1 to activate the Arp2/3 complex which is necessary for the developmental migration of tail hemocytes anteriorly along the ventral midline (PubMed:25739458). Its function in hemocyte transmigration is independent of the WASH complex (PubMed:25739458). May play a role in endosomal sorting; its assembly in the WASH complex may regulate its nucleation-promoting factor (NPF) activity.Curated2 Publications

GO - Molecular functioni

  • GTPase binding Source: FlyBase

GO - Biological processi

  • actin crosslink formation Source: FlyBase
  • actin filament bundle assembly Source: FlyBase
  • Arp2/3 complex-mediated actin nucleation Source: FlyBase
  • microtubule bundle formation Source: FlyBase
  • oogenesis Source: FlyBase
  • prepupal development Source: FlyBase
  • protein transport Source: UniProtKB-KW
  • retrograde transport, endosome to Golgi Source: FlyBase
  • spiracle morphogenesis, open tracheal system Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Differentiation, Oogenesis, Protein transport, Transport

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
WAS protein family homolog 1
Alternative name(s):
Protein washout
Gene namesi
Name:washImported
ORF Names:CG13176Imported
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0033692. wash.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • early endosome Source: InterPro
  • endosome Source: FlyBase
  • nucleus Source: FlyBase
  • perinuclear region of cytoplasm Source: FlyBase
  • transcription factor complex Source: FlyBase
  • WASH complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Lethal. Larvae die at the transition from third larval instar to prepupal stage.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499WAS protein family homolog 1PRO_0000390969Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei491 – 4911Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ7JW27.
PRIDEiQ7JW27.

PTM databases

iPTMnetiQ7JW27.

Expressioni

Gene expression databases

BgeeiQ7JW27.
ExpressionAtlasiQ7JW27. differential.
GenevisibleiQ7JW27. DM.

Interactioni

Subunit structurei

Component of the WASH complex (PubMed:20498093). Interacts with spir and capu (PubMed:19633175). Interacts (via N-terminus) with Rho1 (via N-terminus) (PubMed:25739458).3 Publications

GO - Molecular functioni

  • GTPase binding Source: FlyBase

Protein-protein interaction databases

BioGridi62092. 3 interactions.
STRINGi7227.FBpp0087097.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini391 – 41323WH2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi328 – 39164Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the WASH1 family.Curated
Contains 1 WH2 domain.Curated

Phylogenomic databases

eggNOGiENOG410IFZ4. Eukaryota.
ENOG410YN2V. LUCA.
GeneTreeiENSGT00390000016717.
InParanoidiQ7JW27.
KOiK18461.
OMAiTHTTLET.
OrthoDBiEOG79PJPR.
PhylomeDBiQ7JW27.

Family and domain databases

InterProiIPR028290. WASH1.
IPR021854. WASH1_WAHD.
[Graphical view]
PANTHERiPTHR23331. PTHR23331. 1 hit.
PfamiPF11945. WASH_WAHD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7JW27-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEESPYLHSP YQVAIIATDL HHEDTIIQAA QSLDCLHKTI NSIFERIDAR
60 70 80 90 100
LARNGSKVED INNRVKRAQA KIDALVGSKR AIQIFAPARF PASDVLAPLP
110 120 130 140 150
ATFPQVAANP LMEQQVDQLP QGTYSSHSAA DQKPDDADIF FHVRGDREQE
160 170 180 190 200
SPLVAERKIT NRTAGLGILP AGGVRSVPSL MRFNTNEFAY GEDLNAWKRS
210 220 230 240 250
LPPQNARRVA SQSTQLTGEK QLAPAPHSLA HGTTKLATPA GDLRYNPAAL
260 270 280 290 300
AAPAIDVPLD LPDLPGIAND LQYEPVEEQT PIAPSQQFGD LPELPDLGLE
310 320 330 340 350
EQDIIVQAIA AQTHIPGPVR RKSVGQCPSP VTAAPPPPPP PPPPPPPPPP
360 370 380 390 400
AQTSAIPSPP PFPTKGAVKP LSPSLATPLN MPQPPPATED PRSELMAAIR
410 420 430 440 450
NAGGVHGGRL RSPAAAPLDV VDNSRSKAGG AVTGDLMADL HNKLMLRRKG
460 470 480 490
ISGSQNPVEA TAGNPLMQQL SRVIPPPVQP RKGSKSSDEH SEDDEDGWN
Length:499
Mass (Da):53,210
Last modified:October 3, 2006 - v1
Checksum:i62B903E956FB169B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF58562.1.
AE013599 Genomic DNA. Translation: AHN56132.1.
AY118440 mRNA. Translation: AAM48469.1.
RefSeqiNP_001286334.1. NM_001299405.1.
NP_610739.1. NM_136895.4.
UniGeneiDm.37984.

Genome annotation databases

EnsemblMetazoaiFBtr0087989; FBpp0087097; FBgn0033692.
FBtr0339595; FBpp0308667; FBgn0033692.
GeneIDi36311.
KEGGidme:Dmel_CG13176.
UCSCiCG13176-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF58562.1.
AE013599 Genomic DNA. Translation: AHN56132.1.
AY118440 mRNA. Translation: AAM48469.1.
RefSeqiNP_001286334.1. NM_001299405.1.
NP_610739.1. NM_136895.4.
UniGeneiDm.37984.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62092. 3 interactions.
STRINGi7227.FBpp0087097.

PTM databases

iPTMnetiQ7JW27.

Proteomic databases

PaxDbiQ7JW27.
PRIDEiQ7JW27.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0087989; FBpp0087097; FBgn0033692.
FBtr0339595; FBpp0308667; FBgn0033692.
GeneIDi36311.
KEGGidme:Dmel_CG13176.
UCSCiCG13176-RA. d. melanogaster.

Organism-specific databases

CTDi36311.
FlyBaseiFBgn0033692. wash.

Phylogenomic databases

eggNOGiENOG410IFZ4. Eukaryota.
ENOG410YN2V. LUCA.
GeneTreeiENSGT00390000016717.
InParanoidiQ7JW27.
KOiK18461.
OMAiTHTTLET.
OrthoDBiEOG79PJPR.
PhylomeDBiQ7JW27.

Miscellaneous databases

ChiTaRSiwash. fly.
GenomeRNAii36311.
NextBioi797868.
PROiQ7JW27.

Gene expression databases

BgeeiQ7JW27.
ExpressionAtlasiQ7JW27. differential.
GenevisibleiQ7JW27. DM.

Family and domain databases

InterProiIPR028290. WASH1.
IPR021854. WASH1_WAHD.
[Graphical view]
PANTHERiPTHR23331. PTHR23331. 1 hit.
PfamiPF11945. WASH_WAHD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  4. "Human subtelomeric WASH genes encode a new subclass of the WASP family."
    Linardopoulou E.V., Parghi S.S., Friedman C., Osborn G.E., Parkhurst S.M., Trask B.J.
    PLoS Genet. 3:E237-E237(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  5. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  6. "Wash functions downstream of Rho and links linear and branched actin nucleation factors."
    Liu R., Abreu-Blanco M.T., Barry K.C., Linardopoulou E.V., Osborn G.E., Parkhurst S.M.
    Development 136:2849-2860(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SPIR AND CAPU.
  7. "WASH and WAVE actin regulators of the Wiskott-Aldrich syndrome protein (WASP) family are controlled by analogous structurally related complexes."
    Jia D., Gomez T.S., Metlagel Z., Umetani J., Otwinowski Z., Rosen M.K., Billadeau D.D.
    Proc. Natl. Acad. Sci. U.S.A. 107:10442-10447(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  8. "Wash functions downstream of Rho1 GTPase in a subset of Drosophila immune cell developmental migrations."
    Verboon J.M., Rahe T.K., Rodriguez-Mesa E., Parkhurst S.M.
    Mol. Biol. Cell 26:1665-1674(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RHO1.

Entry informationi

Entry nameiWASH1_DROME
AccessioniPrimary (citable) accession number: Q7JW27
Secondary accession number(s): A0A0B4LF66
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 19, 2010
Last sequence update: October 3, 2006
Last modified: May 11, 2016
This is version 83 of the entry and version 1 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

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 one 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.