WASH1_CAEEL
ID WASH1_CAEEL Reviewed; 497 AA.
AC O18195;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=WASH complex subunit homolog 1 {ECO:0000250|UniProtKB:A8K0Z3};
GN Name=ddl-2 {ECO:0000312|WormBase:Y48E1B.1};
GN ORFNames=Y48E1B.1 {ECO:0000312|WormBase:Y48E1B.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE DHIC COMPLEX, INTERACTION WITH DDL-1,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22265419; DOI=10.1016/j.cell.2011.12.019;
RA Chiang W.C., Ching T.T., Lee H.C., Mousigian C., Hsu A.L.;
RT "HSF-1 regulators DDL-1/2 link insulin-like signaling to heat-shock
RT responses and modulation of longevity.";
RL Cell 148:322-334(2012).
CC -!- FUNCTION: Acts as a component of the WASH core complex that functions
CC as a nucleation-promoting factor (NPF) at the surface of endosomes,
CC where it recruits and activates the Arp2/3 complex to induce actin
CC polymerization, playing a key role in the fission of tubules that serve
CC as transport intermediates during endosome sorting (By similarity).
CC Acts as a component of the DHIC (ddl-1-containing hsf-1 inhibitory
CC complex) which modulates lifespan by sequestering the heat shock
CC transcription factor hsf-1 to negatively regulate its binding to DNA
CC and its transcriptional activity (PubMed:22265419).
CC {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000269|PubMed:22265419}.
CC -!- SUBUNIT: Component of the WASH core complex (By similarity). Component
CC of the DHIC (ddl-1-containing hsf-1 inhibitory) complex, which contains
CC at least ddl-1, ddl-2, hsb-1 and hsf-1 (PubMed:22265419). Within the
CC complex, interacts with ddl-1 (PubMed:22265419). Formation of the DHIC
CC may be dependent upon the Insulin/IGF-1-like signaling (IIS) mediated
CC pathway (PubMed:22265419). {ECO:0000250|UniProtKB:A8K0Z3,
CC ECO:0000269|PubMed:22265419}.
CC -!- INTERACTION:
CC O18195; O01901: ddl-1; NbExp=6; IntAct=EBI-313368, EBI-323542;
CC O18195; G5EC32: sorb-1; NbExp=6; IntAct=EBI-313368, EBI-325337;
CC -!- TISSUE SPECIFICITY: Expressed in several neurons located throughout the
CC body. {ECO:0000269|PubMed:22265419}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown positively modulates
CC lifespan; effect abolished in hsf-1 mutant background
CC (PubMed:22265419). Increases resistance to both heat and oxidative
CC stresses (PubMed:22265419). Increases localization to the nucleus and
CC also DNA binding activity of heat-shock transcription factor hsf-1
CC after heat shock (PubMed:22265419). Increases in transcript levels of
CC heat shock protein genes sim-1, hsp-70, hsp-16.2 and F44E5.5 after heat
CC shock, but not in unstressed conditions (PubMed:22265419). May also
CC moderately decrease levels of post-translationally modified hsf-1 under
CC heat stressed conditions (PubMed:22265419).
CC {ECO:0000269|PubMed:22265419}.
CC -!- SIMILARITY: Belongs to the WASH1 family. {ECO:0000305}.
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DR EMBL; BX284602; CAB07688.1; -; Genomic_DNA.
DR PIR; T27012; T27012.
DR RefSeq; NP_496847.1; NM_064446.1.
DR AlphaFoldDB; O18195; -.
DR SMR; O18195; -.
DR ComplexPortal; CPX-4305; DHIC complex.
DR DIP; DIP-26697N; -.
DR IntAct; O18195; 4.
DR STRING; 6239.Y48E1B.1; -.
DR EPD; O18195; -.
DR PaxDb; O18195; -.
DR PeptideAtlas; O18195; -.
DR EnsemblMetazoa; Y48E1B.1.1; Y48E1B.1.1; WBGene00013000.
DR GeneID; 190025; -.
DR KEGG; cel:CELE_Y48E1B.1; -.
DR UCSC; Y48E1B.1; c. elegans.
DR CTD; 190025; -.
DR WormBase; Y48E1B.1; CE14854; WBGene00013000; ddl-2.
DR eggNOG; ENOG502QSX3; Eukaryota.
DR GeneTree; ENSGT00390000016717; -.
DR HOGENOM; CLU_551222_0_0_1; -.
DR InParanoid; O18195; -.
DR OMA; MYSAAKY; -.
DR OrthoDB; 1217217at2759; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00013000; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0071203; C:WASH complex; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0043014; F:alpha-tubulin binding; IBA:GO_Central.
DR GO; GO:0043015; F:gamma-tubulin binding; IBA:GO_Central.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR GO; GO:0051220; P:cytoplasmic sequestering of protein; IMP:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IC:ComplexPortal.
DR GO; GO:2000677; P:regulation of transcription regulatory region DNA binding; IMP:WormBase.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..497
FT /note="WASH complex subunit homolog 1"
FT /id="PRO_0000453734"
FT DOMAIN 390..412
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 306..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..336
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..374
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 497 AA; 54580 MW; 785BCB7AC0341AD0 CRC64;
MYHVPLIPRD AGREETIFRI NQSLQKLLRV SDEIFDRVEH RITRIHGKAE AIDRRTEVLE
KKLESLQESD KVITFTLPRQ LPKLPEEPPT STSLFRINID TEHFPGSEEL PAFRRADDHV
LRPCEPIDFT YELNKPDKFF LTSQVLKEYE QKGWERYKKR LLGGLRELSR SPEHIAELFY
AGTSIPAFEG VSGDFSKKAL DADDDGGTSR SGRTTDELAQ LRLHEQLLED TALSSTLMQE
DSLDDNHPLA FRINFNEKKK KTAKMVEMPD SLPNLKGHAH DFTLRDPEID EDRLLDILPA
DDQIPEASEP TEAEADAPTT FILPPPPPPM KLDPSPQPAA TPVEITEIPP IISPPAPPPP
PPPPPPPPPP QTPSASSSVT FSPTKSVDGG RSDLMAAIRA AGGAGNAKLS RIAEKPKRKG
KFDGILESSA LLGASETPRN SAPAPDGGGG GGDLMSALSK ALDARRKAIN GKVEAQPPAK
VSSTIPAPPN FDDEEWD
