WASH1_XENTR
ID WASH1_XENTR Reviewed; 472 AA.
AC Q28DN4;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 68.
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;
GN ORFNames=TNeu121a17.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neurula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6; TISSUE=Oviduct;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) 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; CR855419; CAJ83032.1; -; mRNA.
DR EMBL; BC123023; AAI23024.1; -; mRNA.
DR RefSeq; NP_001016854.1; NM_001016854.2.
DR RefSeq; XP_012814500.1; XM_012959046.2.
DR RefSeq; XP_012814501.1; XM_012959047.1.
DR RefSeq; XP_012814502.1; XM_012959048.2.
DR AlphaFoldDB; Q28DN4; -.
DR SMR; Q28DN4; -.
DR STRING; 8364.ENSXETP00000040722; -.
DR DNASU; 549608; -.
DR Ensembl; ENSXETT00000007834; ENSXETP00000007834; ENSXETG00000003630.
DR Ensembl; ENSXETT00000080702; ENSXETP00000072329; ENSXETG00000003630.
DR GeneID; 549608; -.
DR KEGG; xtr:549608; -.
DR CTD; 100287171; -.
DR Xenbase; XB-GENE-5947821; washc1.
DR eggNOG; ENOG502QSX3; Eukaryota.
DR InParanoid; Q28DN4; -.
DR OrthoDB; 904881at2759; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000003630; Expressed in gastrula and 12 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: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 InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR23331; PTHR23331; 1.
DR Pfam; PF11945; WASH_WAHD; 1.
DR PROSITE; PS51082; WH2; 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_0000390968"
FT DOMAIN 364..386
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..51
FT /note="Required for WASH complex assembly"
FT /evidence="ECO:0000250|UniProtKB:C4AMC7"
FT REGION 289..365
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 377..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..337
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 472 AA; 51236 MW; 38C929C4780D1589 CRC64;
MPQNRSMESQ AYSLPLILPD LRREEAIHQI TDTLQHLQTV SNDIFSRILQ RVETNRGQLQ
RINGRLSLAQ AKIERLKGIK KAIKVFSSAK YPAPEHLQEY SSVFAGAEDG WLAKKLRHKI
QSKHRPLDEQ AVQEKLKYFP VCVNTRGQDE ESAEEGLGSL PRNISSVSSL LLFNTTENLY
KKYVFLDPLA GVVTRTNPAL EGEDEEKLFD APLSITKREQ LERQTAENYF YVPDLGQVPE
IDVPYSLPDL PGVADDLMYS ADLGPGIAPS APGVPIPELP TFITEDITEN SRTDSQDGRL
LPPPPPPPPP PPPPPPPEPS VLSPPTSLAP PLPIPAPARV GSSDVGDPGS LQGAPKEVVN
PSDGRASLLE SIRQAGGIGK AKLRNVKEKK LEKKKMKEQE QVRATGGGGD LMSDLFNKLA
MRRKGISGKG PAAGEASGDG PTGAFARISD TIPPLPPPDQ ASGDGDEEDW ES
