ID   WASH1_XENLA             Reviewed;         472 AA.
AC   Q5U4A3;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 61.
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=wash1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) 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}.
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DR   EMBL; BC085201; AAH85201.1; -; mRNA.
DR   RefSeq; NP_001088612.1; NM_001095143.1.
DR   AlphaFoldDB; Q5U4A3; -.
DR   SMR; Q5U4A3; -.
DR   BioGRID; 105587; 1.
DR   IntAct; Q5U4A3; 1.
DR   MaxQB; Q5U4A3; -.
DR   DNASU; 495507; -.
DR   GeneID; 495507; -.
DR   KEGG; xla:495507; -.
DR   CTD; 495507; -.
DR   Xenbase; XB-GENE-5947866; washc1.L.
DR   OrthoDB; 904881at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 495507; Expressed in internal ear and 19 other tissues.
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:0034314; P:Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
DR   GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
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..472
FT                   /note="WASH complex subunit 1"
FT                   /id="PRO_0000390967"
FT   DOMAIN          364..386
FT                   /note="WH2"
FT   REGION          1..51
FT                   /note="Required for WASH complex assembly"
FT                   /evidence="ECO:0000250|UniProtKB:C4AMC7"
FT   REGION          294..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..472
FT                   /note="VCA"
FT                   /evidence="ECO:0000250|UniProtKB:C4AMC7"
FT   REGION          429..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..336
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..400
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   472 AA;  51124 MW;  A1152EC1F7803170 CRC64;
     MPQNRSVESQ AYSLPLILPD LRREEAIHQI TDTLQHLQTV SNDIFSRILQ RVETNRDQLQ
     RINGRLSLAQ AKIERLKGSK KAIKVFSSAK YPAPDRLQEY SSIFAGAKDG WSAKKQRHKI
     QSKHRPLDEQ AVQEKLKYFP VCVNTRGQDE ESAEEGLGSL PRNINSVSSL LLFNTTENLY
     KKYVLLDPLA GVVTRTNPAL EGEDEEKLFD APLSITKREQ LERQTAENYF YVPDLGQVPE
     IDVPYSLPDL LGVADDLMYS ADLGPGIAPS APGVPIPELP TFTTEDITEN SITDRQDGRL
     LPPPPPPPPP PPPPPPPEPS ALSPPAPPPP PLSIPAPAKK GGSDPGDQGA VQGAPKEVVN
     PSNGRASLLE SIRQAGGIGK ANLRNVKEKK LEKKKMKEQE QVGATGGGGD LMSDLFNKLA
     MRRKGISGKV PAAGEASGDG PTGAFARISD TIPPLPPPHQ ASGDGDEDDW ES