WASH1_DROME
ID WASH1_DROME Reviewed; 499 AA.
AC Q7JW27; A0A0B4LF66;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=WASH complex subunit 1 {ECO:0000250|UniProtKB:A8K0Z3};
DE AltName: Full=Protein washout;
DE AltName: Full=WAS protein family homolog 1;
GN Name=wash {ECO:0000312|FlyBase:FBgn0033692};
GN ORFNames=CG13176 {ECO:0000312|FlyBase:FBgn0033692};
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 [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 [2]
RP GENOME REANNOTATION.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
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 [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=18159949; DOI=10.1371/journal.pgen.0030237;
RA Linardopoulou E.V., Parghi S.S., Friedman C., Osborn G.E., Parkhurst S.M.,
RA Trask B.J.;
RT "Human subtelomeric WASH genes encode a new subclass of the WASP family.";
RL PLoS Genet. 3:E237-E237(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [6]
RP FUNCTION, AND INTERACTION WITH SPIR AND CAPU.
RX PubMed=19633175; DOI=10.1242/dev.035246;
RA Liu R., Abreu-Blanco M.T., Barry K.C., Linardopoulou E.V., Osborn G.E.,
RA Parkhurst S.M.;
RT "Wash functions downstream of Rho and links linear and branched actin
RT nucleation factors.";
RL Development 136:2849-2860(2009).
RN [7]
RP SUBUNIT.
RX PubMed=20498093; DOI=10.1073/pnas.0913293107;
RA Jia D., Gomez T.S., Metlagel Z., Umetani J., Otwinowski Z., Rosen M.K.,
RA Billadeau D.D.;
RT "WASH and WAVE actin regulators of the Wiskott-Aldrich syndrome protein
RT (WASP) family are controlled by analogous structurally related complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10442-10447(2010).
RN [8]
RP FUNCTION, AND INTERACTION WITH RHO1.
RX PubMed=25739458; DOI=10.1091/mbc.e14-08-1266;
RA Verboon J.M., Rahe T.K., Rodriguez-Mesa E., Parkhurst S.M.;
RT "Wash functions downstream of Rho1 GTPase in a subset of Drosophila immune
RT cell developmental migrations.";
RL Mol. Biol. Cell 26:1665-1674(2015).
CC -!- FUNCTION: Acts as a nucleation-promoting factor by activating the
CC Arp2/3 complex to induce actin polymerization (PubMed:19633175).
CC Participates in both linear- and branched-actin networks
CC (PubMed:19633175). Functions in linear-filament (bundled F-actin) by
CC acting downstream of Rho1 and regulating actin and microtubule
CC organization during oogenesis (PubMed:19633175). Nucleates actin in an
CC Arp2/3-dependent manner and exhibits F-actin and microtubule bundling
CC and cross-linking activity in the egg chamber (PubMed:19633175). During
CC embryogenesis, acts downstream of Rho1 to activate the Arp2/3 complex
CC which is necessary for the developmental migration of tail hemocytes
CC anteriorly along the ventral midline (PubMed:25739458). Its function in
CC hemocyte transmigration is independent of the WASH complex
CC (PubMed:25739458). May play a role in endosomal sorting; its assembly
CC in the WASH complex may regulate its nucleation-promoting factor (NPF)
CC activity. {ECO:0000269|PubMed:19633175, ECO:0000269|PubMed:25739458,
CC ECO:0000305}.
CC -!- SUBUNIT: Component of the WASH complex (PubMed:20498093). Interacts
CC with spir and capu (PubMed:19633175). Interacts (via N-terminus) with
CC Rho1 (via N-terminus) (PubMed:25739458). {ECO:0000269|PubMed:19633175,
CC ECO:0000269|PubMed:20498093, ECO:0000269|PubMed:25739458}.
CC -!- DISRUPTION PHENOTYPE: Lethal. Larvae die at the transition from third
CC larval instar to prepupal stage. {ECO:0000269|PubMed:18159949}.
CC -!- SIMILARITY: Belongs to the WASH1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE013599; AAF58562.1; -; Genomic_DNA.
DR EMBL; AE013599; AHN56132.1; -; Genomic_DNA.
DR EMBL; AY118440; AAM48469.1; -; mRNA.
DR RefSeq; NP_001286334.1; NM_001299405.1.
DR RefSeq; NP_610739.1; NM_136895.4.
DR AlphaFoldDB; Q7JW27; -.
DR SMR; Q7JW27; -.
DR BioGRID; 62092; 15.
DR IntAct; Q7JW27; 1.
DR STRING; 7227.FBpp0087097; -.
DR iPTMnet; Q7JW27; -.
DR PaxDb; Q7JW27; -.
DR DNASU; 36311; -.
DR EnsemblMetazoa; FBtr0087989; FBpp0087097; FBgn0033692.
DR EnsemblMetazoa; FBtr0339595; FBpp0308667; FBgn0033692.
DR GeneID; 36311; -.
DR KEGG; dme:Dmel_CG13176; -.
DR UCSC; CG13176-RA; d. melanogaster.
DR CTD; 36311; -.
DR FlyBase; FBgn0033692; wash.
DR VEuPathDB; VectorBase:FBgn0033692; -.
DR eggNOG; ENOG502QSX3; Eukaryota.
DR GeneTree; ENSGT00390000016717; -.
DR HOGENOM; CLU_029156_1_0_1; -.
DR InParanoid; Q7JW27; -.
DR OMA; MYSAAKY; -.
DR OrthoDB; 904881at2759; -.
DR PhylomeDB; Q7JW27; -.
DR SignaLink; Q7JW27; -.
DR BioGRID-ORCS; 36311; 0 hits in 3 CRISPR screens.
DR ChiTaRS; wash; fly.
DR GenomeRNAi; 36311; -.
DR PRO; PR:Q7JW27; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033692; Expressed in testis and 21 other tissues.
DR ExpressionAtlas; Q7JW27; baseline and differential.
DR Genevisible; Q7JW27; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IDA:FlyBase.
DR GO; GO:0005635; C:nuclear envelope; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0071203; C:WASH complex; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0043014; F:alpha-tubulin binding; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0043015; F:gamma-tubulin binding; IBA:GO_Central.
DR GO; GO:0051020; F:GTPase binding; IPI:FlyBase.
DR GO; GO:0005521; F:lamin binding; IDA:FlyBase.
DR GO; GO:0051764; P:actin crosslink formation; IDA:FlyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:FlyBase.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IDA:FlyBase.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0001578; P:microtubule bundle formation; IDA:FlyBase.
DR GO; GO:0140591; P:nuclear envelope budding; IMP:FlyBase.
DR GO; GO:0006998; P:nuclear envelope organization; IMP:FlyBase.
DR GO; GO:0071765; P:nuclear inner membrane organization; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IMP:FlyBase.
DR GO; GO:0035210; P:prepupal development; IMP:FlyBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0033044; P:regulation of chromosome organization; IMP:FlyBase.
DR GO; GO:2001135; P:regulation of endocytic recycling; IMP:FlyBase.
DR GO; GO:0035751; P:regulation of lysosomal lumen pH; IMP:FlyBase.
DR GO; GO:1903353; P:regulation of nucleus organization; IMP:FlyBase.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:FlyBase.
DR GO; GO:0035277; P:spiracle morphogenesis, open tracheal system; IMP:FlyBase.
DR InterPro; IPR028290; WASH1.
DR InterPro; IPR021854; WASH1_WAHD.
DR PANTHER; PTHR23331; PTHR23331; 1.
DR Pfam; PF11945; WASH_WAHD; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Differentiation; Oogenesis; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..499
FT /note="WASH complex subunit 1"
FT /id="PRO_0000390969"
FT DOMAIN 391..413
FT /note="WH2"
FT REGION 317..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..367
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 499 AA; 53210 MW; 62B903E956FB169B CRC64;
MEESPYLHSP YQVAIIATDL HHEDTIIQAA QSLDCLHKTI NSIFERIDAR LARNGSKVED
INNRVKRAQA KIDALVGSKR AIQIFAPARF PASDVLAPLP ATFPQVAANP LMEQQVDQLP
QGTYSSHSAA DQKPDDADIF FHVRGDREQE SPLVAERKIT NRTAGLGILP AGGVRSVPSL
MRFNTNEFAY GEDLNAWKRS LPPQNARRVA SQSTQLTGEK QLAPAPHSLA HGTTKLATPA
GDLRYNPAAL AAPAIDVPLD LPDLPGIAND LQYEPVEEQT PIAPSQQFGD LPELPDLGLE
EQDIIVQAIA AQTHIPGPVR RKSVGQCPSP VTAAPPPPPP PPPPPPPPPP AQTSAIPSPP
PFPTKGAVKP LSPSLATPLN MPQPPPATED PRSELMAAIR NAGGVHGGRL RSPAAAPLDV
VDNSRSKAGG AVTGDLMADL HNKLMLRRKG ISGSQNPVEA TAGNPLMQQL SRVIPPPVQP
RKGSKSSDEH SEDDEDGWN
