HSP90_CAEEL
ID HSP90_CAEEL Reviewed; 702 AA.
AC Q18688;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Heat shock protein 90;
DE AltName: Full=Abnormal dauer formation protein 21;
GN Name=daf-21 {ECO:0000312|EMBL:CAA99793.1}; ORFNames=C47E8.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000312|EMBL:CAA99793.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA99793.1};
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 PROTEIN SEQUENCE OF 35-67; 76-100; 255-263; 286-298; 310-327; 358-371;
RP 418-427; 436-453; 470-480 AND 688-697, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V.;
RL Submitted (MAR-2006) to UniProtKB.
RN [3]
RP FUNCTION.
RX PubMed=7828815; DOI=10.1093/genetics/138.2.303;
RA Vowels J.J., Thomas J.H.;
RT "Multiple chemosensory defects in daf-11 and daf-21 mutants of
RT Caenorhabditis elegans.";
RL Genetics 138:303-316(1994).
RN [4]
RP FUNCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF GLU-292.
RX PubMed=10790386; DOI=10.1093/genetics/155.1.85;
RA Birnby D.A., Link E.M., Vowels J.J., Tian H., Colacurcio P.L., Thomas J.H.;
RT "A transmembrane guanylyl cyclase (DAF-11) and Hsp90 (DAF-21) regulate a
RT common set of chemosensory behaviors in Caenorhabditis elegans.";
RL Genetics 155:85-104(2000).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12950278; DOI=10.1046/j.1440-169x.2003.00706.x;
RA Inoue T., Takamura K., Yamae H., Ise N., Kawakami M., Tabuse Y., Miwa J.,
RA Yamaguchi Y.;
RT "Caenorhabditis elegans DAF-21 (HSP90) is characteristically and
RT predominantly expressed in germline cells: spatial and temporal analysis.";
RL Dev. Growth Differ. 45:369-376(2003).
RN [6]
RP FUNCTION.
RX PubMed=16466390; DOI=10.1111/j.1440-169x.2006.00841.x;
RA Inoue T., Hirata K., Kuwana Y., Fujita M., Miwa J., Roy R., Yamaguchi Y.;
RT "Cell cycle control by daf-21/Hsp90 at the first meiotic prophase/metaphase
RT boundary during oogenesis in Caenorhabditis elegans.";
RL Dev. Growth Differ. 48:25-32(2006).
RN [7]
RP FUNCTION.
RX PubMed=23396260; DOI=10.1016/j.yexcr.2013.01.020;
RA Iwasa H., Maimaiti S., Kuroyanagi H., Kawano S., Inami K., Timalsina S.,
RA Ikeda M., Nakagawa K., Hata Y.;
RT "Yes-associated protein homolog, YAP-1, is involved in the thermotolerance
RT and aging in the nematode Caenorhabditis elegans.";
RL Exp. Cell Res. 319:931-945(2013).
RN [8]
RP INTERACTION WITH CDC-37.
RX PubMed=23569206; DOI=10.1074/jbc.m112.439257;
RA Eckl J.M., Rutz D.A., Haslbeck V., Zierer B.K., Reinstein J., Richter K.;
RT "Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90)
RT motility by interaction with N-terminal and middle domain binding sites.";
RL J. Biol. Chem. 288:16032-16042(2013).
RN [9]
RP SUBUNIT, AND INTERACTION WITH PPH-5.
RX PubMed=26593036; DOI=10.1038/srep17058;
RA Haslbeck V., Eckl J.M., Drazic A., Rutz D.A., Lorenz O.R., Zimmermann K.,
RA Kriehuber T., Lindemann C., Madl T., Richter K.;
RT "The activity of protein phosphatase 5 towards native clients is modulated
RT by the middle- and C-terminal domains of Hsp90.";
RL Sci. Rep. 5:17058-17058(2015).
RN [10]
RP FUNCTION, AND INDUCTION.
RX PubMed=29949773; DOI=10.1016/j.celrep.2018.05.093;
RA O'Brien D., Jones L.M., Good S., Miles J., Vijayabaskar M.S., Aston R.,
RA Smith C.E., Westhead D.R., van Oosten-Hawle P.;
RT "A PQM-1-Mediated Response Triggers Transcellular Chaperone Signaling and
RT Regulates Organismal Proteostasis.";
RL Cell Rep. 23:3905-3919(2018).
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. In response to cellular stress, up-regulated in
CC distal tissues in a pqm-1-dependent manner, preventing protein
CC misfolding and maintaining proteostasis (PubMed:29949773). By
CC stabilizing the receptor-type guanylate cyclase daf-11 or another
CC signal transduction component that regulates cGMP levels, plays a role
CC in dauer formation and chemotaxis to non-volatile and volatile
CC attractants detected by AWC sensory neurons (PubMed:10790386,
CC PubMed:7828815). Participates in the control of cell cycle progression
CC at the prophase/metaphase transition in oocyte development by ensuring
CC the activity of wee-1.3 kinase, which negatively regulates cdk-1
CC through its phosphorylation (PubMed:16466390). Regulates yap-1 nuclear
CC export after heat shock treatment (PubMed:23396260).
CC {ECO:0000269|PubMed:10790386, ECO:0000269|PubMed:16466390,
CC ECO:0000269|PubMed:23396260, ECO:0000269|PubMed:29949773,
CC ECO:0000269|PubMed:7828815}.
CC -!- SUBUNIT: Homodimer (PubMed:26593036). Interacts (via TPR repeat-binding
CC and central region) with pph-5 (via phosphatase domain); the
CC interaction promotes pph-5 phosphatase activity (PubMed:26593036).
CC Interacts (via central region) with co-chaperone cdc-37 (via N-
CC terminus); the interaction inhibits daf-21 ATPase activity
CC (PubMed:23569206). {ECO:0000269|PubMed:23569206,
CC ECO:0000269|PubMed:26593036}.
CC -!- INTERACTION:
CC Q18688; P20792: daf-1; NbExp=2; IntAct=EBI-313329, EBI-360236;
CC Q18688; Q18688: daf-21; NbExp=3; IntAct=EBI-313329, EBI-313329;
CC Q18688; Q11184: let-756; NbExp=3; IntAct=EBI-313329, EBI-3843983;
CC Q18688; O16259: sti-1; NbExp=3; IntAct=EBI-313329, EBI-6514174;
CC Q18688; G5EG62: unc-45; NbExp=5; IntAct=EBI-313329, EBI-6675165;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:12950278}. Note=Perinuclear region of somatic
CC cells.
CC -!- TISSUE SPECIFICITY: In the embryo comma stage, expression is strongly
CC detected in cells of the head region and less so in other areas. In
CC early larvae, expressed in postembryonic germ cells derived from Z2 and
CC Z3 cells and the head region, in both hermaphrodites and males. Under
CC heat stress conditions, larval expression is not only detected in germ
CC cells, but also all over the body. In adult hermaphrodites, expression
CC is localized uniquely in the germ cells. {ECO:0000269|PubMed:12950278}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed throughout development.
CC {ECO:0000269|PubMed:10790386}.
CC -!- INDUCTION: Induced by heat-stress. {ECO:0000269|PubMed:29949773}.
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}.
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DR EMBL; BX284605; CAA99793.1; -; Genomic_DNA.
DR PIR; T20019; T20019.
DR RefSeq; NP_506626.1; NM_074225.3.
DR PDB; 4GQT; X-ray; 2.15 A; A/B=1-224.
DR PDB; 4I2Z; X-ray; 2.90 A; B=693-702.
DR PDBsum; 4GQT; -.
DR PDBsum; 4I2Z; -.
DR AlphaFoldDB; Q18688; -.
DR SMR; Q18688; -.
DR BioGRID; 44973; 111.
DR ComplexPortal; CPX-3983; Hsp90-cdc-37-pph-5 phosphatase complex.
DR ComplexPortal; CPX-3984; Hsp90-Cdc37 chaperone complex.
DR ComplexPortal; CPX-4002; Hsp90-cdc-37-aha-1 complex.
DR ComplexPortal; CPX-4003; Hsp90-sti-1 chaperone complex.
DR ComplexPortal; CPX-4004; Hsp90-daf-41 chaperone complex.
DR DIP; DIP-25037N; -.
DR IntAct; Q18688; 16.
DR MINT; Q18688; -.
DR STRING; 6239.C47E8.5.2; -.
DR iPTMnet; Q18688; -.
DR World-2DPAGE; 0011:Q18688; -.
DR World-2DPAGE; 0020:Q18688; -.
DR EPD; Q18688; -.
DR PaxDb; Q18688; -.
DR PeptideAtlas; Q18688; -.
DR PRIDE; Q18688; -.
DR EnsemblMetazoa; C47E8.5.1; C47E8.5.1; WBGene00000915.
DR EnsemblMetazoa; C47E8.5.2; C47E8.5.2; WBGene00000915.
DR GeneID; 179971; -.
DR KEGG; cel:CELE_C47E8.5; -.
DR UCSC; C47E8.5.1; c. elegans.
DR CTD; 179971; -.
DR WormBase; C47E8.5; CE05441; WBGene00000915; daf-21.
DR eggNOG; KOG0019; Eukaryota.
DR GeneTree; ENSGT01020000230401; -.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; Q18688; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 924636at2759; -.
DR PhylomeDB; Q18688; -.
DR Reactome; R-CEL-1227986; Signaling by ERBB2.
DR Reactome; R-CEL-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-CEL-203615; eNOS activation.
DR Reactome; R-CEL-3371511; HSF1 activation.
DR Reactome; R-CEL-3371571; HSF1-dependent transactivation.
DR Reactome; R-CEL-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-CEL-8937144; Aryl hydrocarbon receptor signalling.
DR Reactome; R-CEL-8939211; ESR-mediated signaling.
DR Reactome; R-CEL-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-CEL-9652282; Drug-mediated inhibition of ERBB2 signaling.
DR SignaLink; Q18688; -.
DR PRO; PR:Q18688; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000915; Expressed in germ line (C elegans) and 10 other tissues.
DR GO; GO:0101031; C:chaperone complex; IDA:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:1990565; C:HSP90-CDC37 chaperone complex; IDA:ComplexPortal.
DR GO; GO:0045121; C:membrane raft; HDA:WormBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008287; C:protein serine/threonine phosphatase complex; IC:ComplexPortal.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:WormBase.
DR GO; GO:0097718; F:disordered domain specific binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; IPI:UniProtKB.
DR GO; GO:1990634; F:protein phosphatase 5 binding; IPI:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:WormBase.
DR GO; GO:0006935; P:chemotaxis; IGI:UniProtKB.
DR GO; GO:0040024; P:dauer larval development; IMP:WormBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IGI:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IGI:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IDA:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0006611; P:protein export from nucleus; IMP:WormBase.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0022417; P:protein maturation by protein folding; IC:ComplexPortal.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:0050920; P:regulation of chemotaxis; IMP:UniProtKB.
DR GO; GO:0045859; P:regulation of protein kinase activity; IDA:ComplexPortal.
DR GO; GO:0009408; P:response to heat; IGI:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Chaperone; Cytoplasm;
KW Direct protein sequencing; Nucleotide-binding; Reference proteome;
KW Stress response.
FT CHAIN 1..702
FT /note="Heat shock protein 90"
FT /id="PRO_0000233901"
FT REGION 218..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 698..702
FT /note="TPR repeat-binding"
FT COMPBIAS 687..702
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 371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 292
FT /note="E->K: Specific sensory defects and reduced
FT fertility."
FT /evidence="ECO:0000269|PubMed:10790386"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:4GQT"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:4GQT"
FT HELIX 31..51
FT /evidence="ECO:0007829|PDB:4GQT"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:4GQT"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:4GQT"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:4GQT"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:4GQT"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:4GQT"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:4GQT"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:4GQT"
FT HELIX 116..122
FT /evidence="ECO:0007829|PDB:4GQT"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:4GQT"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:4GQT"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:4GQT"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:4GQT"
FT STRAND 169..178
FT /evidence="ECO:0007829|PDB:4GQT"
FT HELIX 180..186
FT /evidence="ECO:0007829|PDB:4GQT"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:4GQT"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:4GQT"
SQ SEQUENCE 702 AA; 80283 MW; 2B0E975A24074811 CRC64;
MSENAETFAF QAEIAQLMSL IINTFYSNKE IYLRELISNA SDALDKIRYQ ALTEPSELDT
GKELFIKITP NKEEKTLTIM DTGIGMTKAD LVNNLGTIAK SGTKAFMEAL QAGADISMIG
QFGVGFYSAF LVADKVVVTS KNNDDDSYQW ESSAGGSFVV RPFNDPEVTR GTKIVMHIKE
DQIDFLEERK IKEIVKKHSQ FIGYPIKLVV EKEREKEVED EEAVEAKDEE KKEGEVENVA
DDADKKKTKK IKEKYFEDEE LNKTKPIWTR NPDDISNEEY AEFYKSLSND WEDHLAVKHF
SVEGQLEFRA LLFVPQRAPF DLFENKKSKN SIKLYVRRVF IMENCEELMP EYLNFIKGVV
DSEDLPLNIS REMLQQSKIL KVIRKNLVKK CMELIDEVAE DKDNFKKFYE QFGKNLKLGI
HEDSTNRKKL SDFLRYSTSA GDEPTSLKEY VSRMKENQTQ IYYITGESKD VVAASAFVER
VKSRGFEVLY MCDPIDEYCV QQLKEYDGKK LVSVTKEGLE LPETEEEKKK FEEDKVAYEN
LCKVIKDILE KKVEKVGVSN RLVSSPCCIV TSEYGWSANM ERIMKAQALR DSSTMGYMAA
KKHLEINPDH AIMKTLRDRV EVDKNDKTVK DLVVLLFETA LLASGFSLEE PQSHASRIYR
MIKLGLDIGD DEIEDSAVPS SCTAEAKIEG AEEDASRMEE VD
