DAF41_CAEEL
ID DAF41_CAEEL Reviewed; 175 AA.
AC Q23280;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Co-chaperone protein daf-41 {ECO:0000305};
DE AltName: Full=Abnormal dauer formation protein daf-41 {ECO:0000305};
DE AltName: Full=p23/cytosolic prostaglandin E synthase 3 homolog {ECO:0000303|PubMed:25830239};
GN Name=daf-41 {ECO:0000312|WormBase:ZC395.10};
GN Synonyms=p23 {ECO:0000303|PubMed:25830239};
GN ORFNames=ZC395.10 {ECO:0000312|WormBase:ZC395.10};
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.
RX PubMed=20880838; DOI=10.1074/jbc.m110.131086;
RA Gaiser A.M., Kretzschmar A., Richter K.;
RT "Cdc37-Hsp90 complexes are responsive to nucleotide-induced conformational
RT changes and binding of further cofactors.";
RL J. Biol. Chem. 285:40921-40932(2010).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25830239; DOI=10.1371/journal.pgen.1005023;
RA Horikawa M., Sural S., Hsu A.L., Antebi A.;
RT "Co-chaperone p23 regulates C. elegans lifespan in response to
RT temperature.";
RL PLoS Genet. 11:E1005023-E1005023(2015).
CC -!- FUNCTION: Co-chaperone for hsp90/daf-21 (PubMed:20880838). Involved in
CC regulation of longevity, larval entry and exit from the dauer stage of
CC development and response to environmental cues, such as oxidative
CC stress, in a temperature-dependent manner. Role in daf-16 and hsf-1
CC inhibition at elevated temperatures (PubMed:25830239).
CC {ECO:0000269|PubMed:20880838, ECO:0000269|PubMed:25830239}.
CC -!- TISSUE SPECIFICITY: Expressed in anterior and posterior neurons
CC including ASE, AWC, ASI and ADL amphids and phasmid sensory neurons,
CC peripheral neurons and ventral cord motorneurons. Additionally
CC expressed in body wall muscle, pharynx, vulva, germ cells and
CC intestine. {ECO:0000269|PubMed:25830239}.
CC -!- DEVELOPMENTAL STAGE: Expressed from embryo to adulthood.
CC {ECO:0000269|PubMed:25830239}.
CC -!- DISRUPTION PHENOTYPE: Resistant to oxidative and heat stress. At
CC increased temperatures, there is increased longevity and an increased
CC propensity of larvae to form dauer. At decreased temperatures, lifespan
CC is shorter. Defective chemotaxis in response to toxins.
CC {ECO:0000269|PubMed:25830239}.
CC -!- SIMILARITY: Belongs to the p23/wos2 family. {ECO:0000305}.
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DR EMBL; FO080775; CCD66668.1; -; Genomic_DNA.
DR PIR; T27543; T27543.
DR RefSeq; NP_498126.1; NM_065725.3.
DR AlphaFoldDB; Q23280; -.
DR SMR; Q23280; -.
DR BioGRID; 40958; 6.
DR ComplexPortal; CPX-4004; Hsp90-daf-41 chaperone complex.
DR STRING; 6239.ZC395.10.1; -.
DR EPD; Q23280; -.
DR PaxDb; Q23280; -.
DR PeptideAtlas; Q23280; -.
DR EnsemblMetazoa; ZC395.10.1; ZC395.10.1; WBGene00022599.
DR GeneID; 175727; -.
DR KEGG; cel:CELE_ZC395.10; -.
DR UCSC; ZC395.10.1; c. elegans.
DR CTD; 175727; -.
DR WormBase; ZC395.10; CE01436; WBGene00022599; daf-41.
DR eggNOG; KOG3158; Eukaryota.
DR GeneTree; ENSGT00880000138731; -.
DR HOGENOM; CLU_078883_0_1_1; -.
DR InParanoid; Q23280; -.
DR OMA; KEEGPYW; -.
DR OrthoDB; 1461729at2759; -.
DR PhylomeDB; Q23280; -.
DR Reactome; R-CEL-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR Reactome; R-CEL-3371511; HSF1 activation.
DR Reactome; R-CEL-8937144; Aryl hydrocarbon receptor signalling.
DR Reactome; R-CEL-8939211; ESR-mediated signaling.
DR PRO; PR:Q23280; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00022599; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0101031; C:chaperone complex; IPI:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030016; C:myofibril; HDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0051879; F:Hsp90 protein binding; IBA:GO_Central.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0022417; P:protein maturation by protein folding; IC:ComplexPortal.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR045250; p23-like.
DR PANTHER; PTHR22932; PTHR22932; 1.
DR Pfam; PF04969; CS; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51203; CS; 1.
PE 2: Evidence at transcript level;
KW Reference proteome.
FT CHAIN 1..175
FT /note="Co-chaperone protein daf-41"
FT /evidence="ECO:0000305"
FT /id="PRO_0000218955"
FT DOMAIN 2..89
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT REGION 109..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..166
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 175 AA; 19431 MW; D5C136F30446E37A CRC64;
MAKQPTVLWA QRESLVYLTI EVDEAKIEEL KGEGNKLHFQ GSSKTDKYEA TLEFFDEIDP
ASVKHTGSST RVVEITVQKK TPAWWPRLLQ NKGKVHWLKV DFGKWKDEDE DDEAEDAGAG
IGGGMANGFD LNQYMSQMGG AGGADFGGLE DDEEDDDMPD LEDNEEEEGK NGTRA
