HSP90_CAEBR
ID HSP90_CAEBR Reviewed; 706 AA.
AC Q61W58; A8WXX6;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Heat shock protein 90;
DE AltName: Full=Abnormal dauer formation protein 21;
GN Name=daf-21 {ECO:0000250|UniProtKB:Q18688}; ORFNames=CBG04560;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Molecular chaperone that promotes the maturation, structural
CC maintenance and proper regulation of specific target proteins involved
CC for instance in cell cycle control and signal transduction. Undergoes a
CC functional cycle that is linked to its ATPase activity. This cycle
CC probably induces conformational changes in the client proteins, thereby
CC causing their activation. Interacts dynamically with various co-
CC chaperones that modulate its substrate recognition, ATPase cycle and
CC chaperone function. By stabilizing the receptor-type guanylate cyclase
CC daf-11 or another signal transduction component that regulates cGMP
CC levels, plays a role in dauer formation and chemotaxis to non-volatile
CC and volatile attractants detected by AWC sensory neurons. Participates
CC in the control of cell cycle progression at the prophase/metaphase
CC transition in oocyte development by ensuring the activity of wee-1.3
CC kinase, which negatively regulates cdk-1 through its phosphorylation.
CC Regulates yap-1 nuclear export after heat shock treatment.
CC {ECO:0000250|UniProtKB:Q18688}.
CC -!- SUBUNIT: Homodimer. Interacts (via TPR repeat-binding and central
CC region) with pph-5 (via phosphatase domain); the interaction promotes
CC pph-5 phosphatase activity. Interacts (via central region) with co-
CC chaperone cdc-37 (via N-terminus); the interaction inhibits daf-21
CC ATPase activity. {ECO:0000250|UniProtKB:P08238}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Note=Perinuclear
CC region of somatic cells. {ECO:0000250}.
CC -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC repeat-containing proteins. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE601135; CAP25236.1; -; Genomic_DNA.
DR RefSeq; XP_002637777.1; XM_002637731.1.
DR AlphaFoldDB; Q61W58; -.
DR SMR; Q61W58; -.
DR STRING; 6238.CBG04560; -.
DR PRIDE; Q61W58; -.
DR EnsemblMetazoa; CBG04560.1; CBG04560.1; WBGene00027205.
DR GeneID; 8579774; -.
DR KEGG; cbr:CBG_04560; -.
DR CTD; 8579774; -.
DR WormBase; CBG04560; CBP01204; WBGene00027205; Cbr-daf-21.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; Q61W58; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 924636at2759; -.
DR Proteomes; UP000008549; Chromosome V.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:1990565; C:HSP90-CDC37 chaperone complex; IEA:EnsemblMetazoa.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblMetazoa.
DR GO; GO:0097718; F:disordered domain specific binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblMetazoa.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; IEA:EnsemblMetazoa.
DR GO; GO:1990634; F:protein phosphatase 5 binding; IEA:EnsemblMetazoa.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:EnsemblMetazoa.
DR GO; GO:0006935; P:chemotaxis; IEA:EnsemblMetazoa.
DR GO; GO:0040024; P:dauer larval development; IEA:EnsemblMetazoa.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:EnsemblMetazoa.
DR GO; GO:0008340; P:determination of adult lifespan; IEA:EnsemblMetazoa.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IEA:EnsemblMetazoa.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:EnsemblMetazoa.
DR GO; GO:0006611; P:protein export from nucleus; IEA:EnsemblMetazoa.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:0050920; P:regulation of chemotaxis; IEA:EnsemblMetazoa.
DR GO; GO:0045859; P:regulation of protein kinase activity; IEA:EnsemblMetazoa.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Chaperone; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Stress response.
FT CHAIN 1..706
FT /note="Heat shock protein 90"
FT /id="PRO_0000233900"
FT REGION 217..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 702..706
FT /note="TPR repeat-binding"
FT COMPBIAS 691..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 706 AA; 80849 MW; 30653E9FE8A6AE16 CRC64;
MSENAETFAF QAEIAQLMSL IINTFYSNKE IYLRELISNA SDALDKIRYQ ALTEPSELDT
GKELFIKITP NKEEKTLTIM DTGIGMTKAD LVNNLGTIAK SGTKAFMEAL QAGADISMIG
QFGVGFYSAF LVADKVVVTS KNNDDDSYQW ESSAGGSFVV RPYNDPELTR GTKITMYIKE
DQVDFLEERK IKEIVKKHSQ FIGYPIKLVV EKEREKEVED EEAVESKDEE KKEGDVENVG
EDADAEKDKK KTKKIKEKYF EDEELNKTKP IWTRNPDDIS NEEYAEFYKS LSNDWEDHLA
VKHFSVEGQL EFRALLFAPQ RAPFDLFENK KSKNSIKLYV RRVFIMENCE ELMPEYLNFI
KGVVDSEDLP LNISREMLQQ SKILKVIRKN LVKKCMELFD EIAEDKDNFK KFYEQFGKNL
KLGIHEDSTN RKKLSEFLRY ATSAGEEPTS LKEYVSRMKE NQTQIYYITG ESKEVVAASA
FVERVKSRGF EVLYMCDPID EYCVQQLKEY DGKKLVSVTK EGLELPETEE EKKKFEEDKV
AYENLCKVIK DILEKKIEKV AVSNRLVSSP CCIVTSEYGW SANMERIMKA QALRDSSTMG
YMAAKKHLEI NPDHAIMKTL RERVEADKND KTVKDLVVLL FETALLSSGF SLEEPQSHAS
RIYRMIKLGL DIGDEDIEES AVPSSCTAEA KIEGADEDAS RMEEVD
