WASH1_DANRE
ID WASH1_DANRE Reviewed; 481 AA.
AC A4IG59; A8DZA2;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=WASH complex subunit 1 {ECO:0000250|UniProtKB:A8K0Z3};
DE AltName: Full=WAS protein family homolog 1;
GN Name=washc1 {ECO:0000250|UniProtKB:A8K0Z3}; Synonyms=wash, Wash1;
GN ORFNames=si:ch211-11f8.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a nucleation-promoting factor at the surface of
CC endosomes, where it recruits and activates the Arp2/3 complex to induce
CC actin polymerization, playing a key role in the fission of tubules that
CC serve as transport intermediates during endosome sorting.
CC {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000250|UniProtKB:C4AMC7}.
CC -!- SUBUNIT: Component of the WASH complex. {ECO:0000250|UniProtKB:A8K0Z3,
CC ECO:0000250|UniProtKB:C4AMC7}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000250|UniProtKB:A8K0Z3}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q8VDD8}.
CC -!- DOMAIN: The VCA (verprolin, cofilin, acidic) domain promotes actin
CC polymerization by the Arp2/3 complex in vitro.
CC {ECO:0000250|UniProtKB:C4AMC7}.
CC -!- SIMILARITY: Belongs to the WASH1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAP09504.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL928990; CAP09504.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC134941; AAI34942.1; -; mRNA.
DR RefSeq; NP_001103920.1; NM_001110450.1.
DR AlphaFoldDB; A4IG59; -.
DR SMR; A4IG59; -.
DR STRING; 7955.ENSDARP00000087184; -.
DR PaxDb; A4IG59; -.
DR PeptideAtlas; A4IG59; -.
DR Ensembl; ENSDART00000092752; ENSDARP00000087184; ENSDARG00000063457.
DR GeneID; 555174; -.
DR KEGG; dre:555174; -.
DR CTD; 555174; -.
DR ZFIN; ZDB-GENE-050419-138; wash1.
DR eggNOG; ENOG502QSX3; Eukaryota.
DR GeneTree; ENSGT00390000016717; -.
DR InParanoid; A4IG59; -.
DR OMA; MYSAAKY; -.
DR OrthoDB; 904881at2759; -.
DR PhylomeDB; A4IG59; -.
DR TreeFam; TF318222; -.
DR PRO; PR:A4IG59; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 18.
DR Bgee; ENSDARG00000063457; Expressed in mature ovarian follicle and 20 other tissues.
DR ExpressionAtlas; A4IG59; baseline.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071203; C:WASH complex; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
DR GO; GO:0043015; F:gamma-tubulin binding; IBA:GO_Central.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR InterPro; IPR028290; WASH1.
DR InterPro; IPR021854; WASH1_WAHD.
DR PANTHER; PTHR23331; PTHR23331; 1.
DR Pfam; PF11945; WASH_WAHD; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Endosome; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..481
FT /note="WASH complex subunit 1"
FT /id="PRO_0000390966"
FT DOMAIN 371..393
FT /note="WH2"
FT REGION 1..54
FT /note="Required for WASH complex assembly"
FT /evidence="ECO:0000250|UniProtKB:C4AMC7"
FT REGION 273..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..481
FT /note="VCA"
FT /evidence="ECO:0000250|UniProtKB:C4AMC7"
FT REGION 429..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..344
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 341
FT /note="M -> I (in Ref. 2; AAI34942)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="G -> S (in Ref. 2; AAI34942)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 52112 MW; 6A4C2029A8DC82CE CRC64;
MVRMTQKRYL EGQVYSVPLI QPDLRREEAV HQITDALQYL EMISTDIFTR VSESVEKNRA
HLQSVTDRIK LAQARVQKIK GSKKATKVFS SAKYPAPEKL QDYSSIFTGA VDPASQKRPR
IKVQSKLRPL DDKAQQEKLM YLPVCVNTKK RSEDETEEGL GSLPRNVNSV SSLLLFNTTE
NLYKKYVFLD PLAGAVTKTH TTLETEKEDK PFDAPLSITK REQLERQTAE NYFYVPDLGQ
VPEIDVPSYL PDLPGIADDL MYSADLGPGF APSVPASNSI PELPSFGTDH DESSGSDSQF
KLEAPPPPPP PPPPPPEPTH VPVPPPGTSA APPPPPPPPP MTADNTDASS PAPPTGTVKG
APSEVVQPSN GRASLLESIR NAGGIGKANL RNVKERKMEK KKQKEQEQVG ATVSGGDLMS
DLFNKLAMRR KGISGKGPAG QGDSSEAPAS SGGAFARMSD VIPPLPAPQQ SAADDEDDWE
A
