WASC3_CAEEL
ID WASC3_CAEEL Reviewed; 189 AA.
AC O01901;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=WASH complex subunit homolog 3 {ECO:0000250|UniProtKB:Q9Y3C0};
DE AltName: Full=Daf-16-dependent longevity protein 1 {ECO:0000312|WormBase:F59E12.10};
GN Name=ddl-1; ORFNames=F59E12.10;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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]
RP FUNCTION, IDENTIFICATION IN THE DHIC COMPLEX, INTERACTION WITH DDL-2; HSF-1
RP AND HSB-1, TISSUE SPECIFICITY, PHOSPHORYLATION AT THR-182, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF THR-182.
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:Q9Y3C0, ECO:0000269|PubMed:22265419}.
CC -!- SUBUNIT: Probable component of the WASH complex (By similarity).
CC Component of the DHIC (ddl-1-containing hsf-1 inhibitory complex),
CC which contains at least ddl-1, ddl-2, hsb-1 and hsf-1
CC (PubMed:22265419). Within the complex, interacts with ddl-2
CC (PubMed:22265419). Within the complex, interacts with hsb-1
CC (PubMed:22265419). Within the complex, interacts with hsf-1
CC (PubMed:22265419). Formation of the DHIC may be dependent upon the
CC Insulin/IGF-1-like signaling (IIS) mediated pathway (PubMed:22265419).
CC {ECO:0000250|UniProtKB:Q9Y3C0, ECO:0000269|PubMed:22265419}.
CC -!- INTERACTION:
CC O01901; O18195: ddl-2; NbExp=6; IntAct=EBI-323542, EBI-313368;
CC O01901; Q9U3B7: hsb-1; NbExp=5; IntAct=EBI-323542, EBI-311898;
CC O01901; G5EFT5: hsf-1; NbExp=3; IntAct=EBI-323542, EBI-2916699;
CC O01901; G5ECG0: tac-1; NbExp=3; IntAct=EBI-323542, EBI-320612;
CC O01901; Q9XVK6: wve-1; NbExp=3; IntAct=EBI-323542, EBI-312105;
CC -!- TISSUE SPECIFICITY: Expressed in pharynx, intestine, body wall muscles,
CC vulva muscles, spermatheca, and several head and tail neurons.
CC {ECO:0000269|PubMed:22265419}.
CC -!- PTM: Phosphorylated (PubMed:22265419). Phosphorylation on Thr-182 may
CC promote DHIC complex dissociation and consequently the activation of
CC heat-shock transcription factor hsf-1 (PubMed:22265419).
CC Phosphorylation is modulated by the Insulin/IGF-1-like signaling (IIS)
CC mediated pathway (PubMed:22265419). {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 both
CC before and after heat shock (PubMed:22265419). Increases in transcript
CC levels of heat-shock protein genes sim-1, hsp-70, hsp-16.2 and F44E5.5
CC after heat shock, but not in unstressed conditions (PubMed:22265419).
CC May also increase levels of post-translationally modified hsf-1 under
CC heat stressed and unstressed conditions (PubMed:22265419).
CC {ECO:0000269|PubMed:22265419}.
CC -!- SIMILARITY: Belongs to the CCDC53 family. {ECO:0000305}.
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DR EMBL; FO080594; CCD64976.1; -; Genomic_DNA.
DR PIR; T15265; T15265.
DR RefSeq; NP_495101.1; NM_062700.2.
DR AlphaFoldDB; O01901; -.
DR SMR; O01901; -.
DR BioGRID; 39296; 9.
DR ComplexPortal; CPX-4305; DHIC complex.
DR DIP; DIP-24590N; -.
DR IntAct; O01901; 8.
DR STRING; 6239.F59E12.10; -.
DR EPD; O01901; -.
DR PaxDb; O01901; -.
DR PeptideAtlas; O01901; -.
DR EnsemblMetazoa; F59E12.10.1; F59E12.10.1; WBGene00019125.
DR EnsemblMetazoa; F59E12.10.2; F59E12.10.2; WBGene00019125.
DR UCSC; F59E12.10; c. elegans.
DR WormBase; F59E12.10; CE11536; WBGene00019125; ddl-1.
DR eggNOG; KOG4496; Eukaryota.
DR GeneTree; ENSGT00390000014084; -.
DR HOGENOM; CLU_117940_1_0_1; -.
DR InParanoid; O01901; -.
DR OMA; RDLKMVQ; -.
DR OrthoDB; 1425330at2759; -.
DR PhylomeDB; O01901; -.
DR PRO; PR:O01901; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00019125; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0071203; C:WASH complex; IBA:GO_Central.
DR GO; GO:0030041; P:actin filament polymerization; 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: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 InterPro; IPR019309; WASHC3.
DR PANTHER; PTHR13015; PTHR13015; 1.
DR Pfam; PF10152; CCDC53; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Phosphoprotein; Reference proteome.
FT CHAIN 1..189
FT /note="WASH complex subunit homolog 3"
FT /id="PRO_0000065388"
FT REGION 76..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 35..74
FT /evidence="ECO:0000255"
FT COMPBIAS 165..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22265419"
FT MUTAGEN 182
FT /note="T->A: Abolishes threonine phosphorylation."
FT /evidence="ECO:0000269|PubMed:22265419"
SQ SEQUENCE 189 AA; 20952 MW; D83A072806B01543 CRC64;
MNASSRTKPA IDLNKVPPID HHRTAVTFNC LIMKMTEMLN NFGNKMEDIL EKAEQSLDTA
DRKLRLMESK LAGMSLEDKS TTATPSSAPE IDEIHESNPS SSQIVEETVE EKPEEHTTTV
LIKDDPAYSK YFKMLKLGVL EAGVIQKMKS EGVDPSILKR GDEPSRPQAQ TSRNYESSGE
STASFSDSD
