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 05-FEB-2025, entry version 127. 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; 17. DR ComplexPortal; CPX-2562; WASH complex. DR IntAct; Q7JW27; 2. DR STRING; 7227.FBpp0308667; -. DR iPTMnet; Q7JW27; -. DR PaxDb; 7227-FBpp0087097; -. 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 AGR; FB:FBgn0033692; -. 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; SMDSPYE; -. DR OrthoDB; 307871at2759; -. DR PhylomeDB; Q7JW27; -. DR Reactome; R-DME-2029482; Regulation of actin dynamics for phagocytic cup formation. DR Reactome; R-DME-5663213; RHO GTPases Activate WASPs and WAVEs. 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 early-mid elongation-stage spermatid (Drosophila) in testis and 59 other cell types or tissues. DR ExpressionAtlas; Q7JW27; baseline and differential. 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 formation; 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; CXYORF1; 1. DR PANTHER; PTHR23331:SF1; WASH COMPLEX SUBUNIT 1; 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 333..363 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 490..499 FT /note="Acidic 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 //