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Protein

Heat shock protein 90

Gene

daf-21

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. By stabilizing the receptor-type guanylate cyclase daf-11 or another signal transduction component that regulates cGMP levels, plays a role in dauer formation and chemotaxis to non-volatile and volatile attractants detected by AWC sensory neurons (PubMed:10790386, PubMed:7828815). Participates in the control of cell cycle progression at the prophase/metaphase transition in oocyte development by ensuring the activity of wee-1.3 kinase, which negatively regulates cdk-1 through its phosphorylation (PubMed:16466390). Regulates yap-1 nuclear export after heat shock treatment (PubMed:23396260).4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391ATPBy similarity
Binding sitei81 – 811ATPBy similarity
Binding sitei100 – 1001ATPBy similarity
Binding sitei126 – 1261ATP; via amide nitrogenBy similarity
Binding sitei371 – 3711ATPBy similarity

GO - Molecular functioni

  • ATPase activity Source: WormBase
  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • chaperone-mediated protein folding Source: WormBase
  • chemotaxis Source: UniProtKB
  • chemotaxis to cAMP Source: UniProtKB
  • dauer larval development Source: WormBase
  • detection of chemical stimulus Source: UniProtKB
  • determination of adult lifespan Source: WormBase
  • nematode larval development Source: WormBase
  • protein export from nucleus Source: WormBase
  • regulation of chemotaxis Source: UniProtKB
  • response to biotin Source: UniProtKB
  • response to inorganic substance Source: UniProtKB
  • response to stress Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Cell cycle, Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-CEL-1474151. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
R-CEL-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-CEL-203615. eNOS activation.
R-CEL-399954. Sema3A PAK dependent Axon repulsion.
R-CEL-5218920. VEGFR2 mediated vascular permeability.
R-CEL-844456. The NLRP3 inflammasome.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein 90
Alternative name(s):
Abnormal dauer formation protein 21
Gene namesi
Name:daf-21Imported
ORF Names:C47E8.5
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome V

Organism-specific databases

WormBaseiC47E8.5; CE05441; WBGene00000915; daf-21.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: WormBase
  • membrane raft Source: WormBase
  • perinuclear region of cytoplasm Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi292 – 2921E → K: Specific sensory defects and reduced fertility. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 702702Heat shock protein 90PRO_0000233901Add
BLAST

Proteomic databases

EPDiQ18688.
PaxDbiQ18688.
PRIDEiQ18688.

2D gel databases

World-2DPAGE0011:Q18688.
0020:Q18688.

PTM databases

iPTMnetiQ18688.

Expressioni

Tissue specificityi

In the embryo comma stage, expression is strongly detected in cells of the head region and less so in other areas. In early larvae, expressed in postembryonic germ cells derived from Z2 and Z3 cells and the head region, in both hermaphrodites and males. Under heat stress conditions, larval expression is not only detected in germ cells, but also all over the body. In adult hermaphrodites, expression is localized uniquely in the germ cells.1 Publication

Developmental stagei

Highly expressed throughout development.1 Publication

Gene expression databases

BgeeiWBGene00000915.

Interactioni

Subunit structurei

Homodimer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-313329,EBI-313329
daf-1P207922EBI-313329,EBI-360236
let-756Q111843EBI-313329,EBI-3843983
sti-1O162593EBI-313329,EBI-6514174
unc-45G5EG625EBI-313329,EBI-6675165

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi44973. 19 interactions.
DIPiDIP-25037N.
IntActiQ18688. 15 interactions.
MINTiMINT-228446.
STRINGi6239.C47E8.5.4.

Structurei

Secondary structure

1
702
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 94Combined sources
Helixi12 – 2312Combined sources
Helixi31 – 5121Combined sources
Helixi55 – 606Combined sources
Beta strandi66 – 716Combined sources
Turni72 – 754Combined sources
Beta strandi76 – 816Combined sources
Helixi88 – 947Combined sources
Turni95 – 973Combined sources
Helixi103 – 1119Combined sources
Helixi116 – 1227Combined sources
Helixi125 – 1317Combined sources
Beta strandi133 – 1419Combined sources
Beta strandi148 – 1525Combined sources
Beta strandi157 – 1626Combined sources
Beta strandi169 – 17810Combined sources
Helixi180 – 1867Combined sources
Helixi188 – 19811Combined sources
Beta strandi206 – 2083Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GQTX-ray2.15A/B1-224[»]
4I2ZX-ray2.90B693-702[»]
ProteinModelPortaliQ18688.
SMRiQ18688. Positions 3-668.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi698 – 7025TPR repeat-binding

Domaini

The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.By similarity

Sequence similaritiesi

Belongs to the heat shock protein 90 family.Sequence analysis

Phylogenomic databases

eggNOGiKOG0019. Eukaryota.
KOG0020. Eukaryota.
COG0326. LUCA.
GeneTreeiENSGT00840000129758.
HOGENOMiHOG000031988.
InParanoidiQ18688.
KOiK04079.
OMAiMHIKEDQ.
OrthoDBiEOG091G0270.
PhylomeDBiQ18688.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90. 1 hit.
InterProiIPR003594. HATPase_C.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR11528. PTHR11528. 1 hit.
PfamiPF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view]
PIRSFiPIRSF002583. Hsp90. 1 hit.
PRINTSiPR00775. HEATSHOCK90.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.

Sequencei

Sequence statusi: Complete.

Q18688-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSENAETFAF QAEIAQLMSL IINTFYSNKE IYLRELISNA SDALDKIRYQ
60 70 80 90 100
ALTEPSELDT GKELFIKITP NKEEKTLTIM DTGIGMTKAD LVNNLGTIAK
110 120 130 140 150
SGTKAFMEAL QAGADISMIG QFGVGFYSAF LVADKVVVTS KNNDDDSYQW
160 170 180 190 200
ESSAGGSFVV RPFNDPEVTR GTKIVMHIKE DQIDFLEERK IKEIVKKHSQ
210 220 230 240 250
FIGYPIKLVV EKEREKEVED EEAVEAKDEE KKEGEVENVA DDADKKKTKK
260 270 280 290 300
IKEKYFEDEE LNKTKPIWTR NPDDISNEEY AEFYKSLSND WEDHLAVKHF
310 320 330 340 350
SVEGQLEFRA LLFVPQRAPF DLFENKKSKN SIKLYVRRVF IMENCEELMP
360 370 380 390 400
EYLNFIKGVV DSEDLPLNIS REMLQQSKIL KVIRKNLVKK CMELIDEVAE
410 420 430 440 450
DKDNFKKFYE QFGKNLKLGI HEDSTNRKKL SDFLRYSTSA GDEPTSLKEY
460 470 480 490 500
VSRMKENQTQ IYYITGESKD VVAASAFVER VKSRGFEVLY MCDPIDEYCV
510 520 530 540 550
QQLKEYDGKK LVSVTKEGLE LPETEEEKKK FEEDKVAYEN LCKVIKDILE
560 570 580 590 600
KKVEKVGVSN RLVSSPCCIV TSEYGWSANM ERIMKAQALR DSSTMGYMAA
610 620 630 640 650
KKHLEINPDH AIMKTLRDRV EVDKNDKTVK DLVVLLFETA LLASGFSLEE
660 670 680 690 700
PQSHASRIYR MIKLGLDIGD DEIEDSAVPS SCTAEAKIEG AEEDASRMEE

VD
Length:702
Mass (Da):80,283
Last modified:November 1, 1996 - v1
Checksum:i2B0E975A24074811
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75530 Genomic DNA. Translation: CAA99793.1.
PIRiT20019.
RefSeqiNP_506626.1. NM_074225.3.
UniGeneiCel.17789.

Genome annotation databases

EnsemblMetazoaiC47E8.5.1; C47E8.5.1; WBGene00000915.
C47E8.5.2; C47E8.5.2; WBGene00000915.
C47E8.5.3; C47E8.5.3; WBGene00000915.
C47E8.5.4; C47E8.5.4; WBGene00000915.
GeneIDi179971.
KEGGicel:CELE_C47E8.5.
UCSCiC47E8.5.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75530 Genomic DNA. Translation: CAA99793.1.
PIRiT20019.
RefSeqiNP_506626.1. NM_074225.3.
UniGeneiCel.17789.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GQTX-ray2.15A/B1-224[»]
4I2ZX-ray2.90B693-702[»]
ProteinModelPortaliQ18688.
SMRiQ18688. Positions 3-668.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi44973. 19 interactions.
DIPiDIP-25037N.
IntActiQ18688. 15 interactions.
MINTiMINT-228446.
STRINGi6239.C47E8.5.4.

PTM databases

iPTMnetiQ18688.

2D gel databases

World-2DPAGE0011:Q18688.
0020:Q18688.

Proteomic databases

EPDiQ18688.
PaxDbiQ18688.
PRIDEiQ18688.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiC47E8.5.1; C47E8.5.1; WBGene00000915.
C47E8.5.2; C47E8.5.2; WBGene00000915.
C47E8.5.3; C47E8.5.3; WBGene00000915.
C47E8.5.4; C47E8.5.4; WBGene00000915.
GeneIDi179971.
KEGGicel:CELE_C47E8.5.
UCSCiC47E8.5.1. c. elegans.

Organism-specific databases

CTDi179971.
WormBaseiC47E8.5; CE05441; WBGene00000915; daf-21.

Phylogenomic databases

eggNOGiKOG0019. Eukaryota.
KOG0020. Eukaryota.
COG0326. LUCA.
GeneTreeiENSGT00840000129758.
HOGENOMiHOG000031988.
InParanoidiQ18688.
KOiK04079.
OMAiMHIKEDQ.
OrthoDBiEOG091G0270.
PhylomeDBiQ18688.

Enzyme and pathway databases

ReactomeiR-CEL-1474151. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
R-CEL-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-CEL-203615. eNOS activation.
R-CEL-399954. Sema3A PAK dependent Axon repulsion.
R-CEL-5218920. VEGFR2 mediated vascular permeability.
R-CEL-844456. The NLRP3 inflammasome.

Miscellaneous databases

PROiQ18688.

Gene expression databases

BgeeiWBGene00000915.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90. 1 hit.
InterProiIPR003594. HATPase_C.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR11528. PTHR11528. 1 hit.
PfamiPF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view]
PIRSFiPIRSF002583. Hsp90. 1 hit.
PRINTSiPR00775. HEATSHOCK90.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHSP90_CAEEL
AccessioniPrimary (citable) accession number: Q18688
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: November 1, 1996
Last modified: September 7, 2016
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.