HSP90_CANAL
ID HSP90_CANAL Reviewed; 707 AA.
AC P46598; A0A1D8PR20; Q3MPE0; Q5AH23;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Heat shock protein 90 homolog;
GN Name=HSP90; OrderedLocusNames=CAALFM_C702030WA;
GN ORFNames=CaJ7.0234, CaO19.13868, CaO19.6515;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10261 / CBS 2718 / NBRC 1061;
RX PubMed=7591093; DOI=10.1128/iai.63.11.4506-4514.1995;
RA Swoboda R.K., Bertram G., Budge S., Gooday G.W., Gow N.A.R., Brown A.J.P.;
RT "Structure and regulation of the HSP90 gene from the pathogenic fungus
RT Candida albicans.";
RL Infect. Immun. 63:4506-4514(1995).
RN [2]
RP ERRATUM OF PUBMED:7591093.
RX PubMed=8550228; DOI=10.1128/iai.64.2.680-680.1996;
RA Swoboda R.K., Bertram G., Budge S., Gooday G.W., Gow N.A.R., Brown A.J.P.;
RL Infect. Immun. 64:680-680(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15937140; DOI=10.1534/genetics.104.034652;
RA Chibana H., Oka N., Nakayama H., Aoyama T., Magee B.B., Magee P.T.,
RA Mikami Y.;
RT "Sequence finishing and gene mapping for Candida albicans chromosome 7 and
RT syntenic analysis against the Saccharomyces cerevisiae genome.";
RL Genetics 170:1525-1537(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
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 similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {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:0000305}.
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DR EMBL; X81025; CAA56931.1; -; Genomic_DNA.
DR EMBL; AP006852; BAE44720.1; -; Genomic_DNA.
DR EMBL; CP017629; AOW30566.1; -; Genomic_DNA.
DR RefSeq; XP_721353.1; XM_716260.1.
DR PDB; 6CJI; X-ray; 1.64 A; A=7-218.
DR PDB; 6CJJ; X-ray; 1.74 A; A=7-218.
DR PDB; 6CJL; X-ray; 1.70 A; A/B=7-218.
DR PDB; 6CJP; X-ray; 2.60 A; A/B=7-218.
DR PDB; 6CJR; X-ray; 1.80 A; A/B=7-218.
DR PDB; 6CJS; X-ray; 1.90 A; A=7-218.
DR PDBsum; 6CJI; -.
DR PDBsum; 6CJJ; -.
DR PDBsum; 6CJL; -.
DR PDBsum; 6CJP; -.
DR PDBsum; 6CJR; -.
DR PDBsum; 6CJS; -.
DR AlphaFoldDB; P46598; -.
DR SMR; P46598; -.
DR BioGRID; 1220045; 428.
DR STRING; 237561.P46598; -.
DR ChEMBL; CHEMBL3580503; -.
DR COMPLUYEAST-2DPAGE; P46598; -.
DR PRIDE; P46598; -.
DR ABCD; P46598; 8 sequenced antibodies.
DR GeneID; 3636951; -.
DR KEGG; cal:CAALFM_C702030WA; -.
DR CGD; CAL0000201062; HSP90.
DR VEuPathDB; FungiDB:C7_02030W_A; -.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; P46598; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 924636at2759; -.
DR PRO; PR:P46598; -.
DR Proteomes; UP000000559; Chromosome 7.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005737; C:cytoplasm; IDA:CGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
DR GO; GO:0016020; C:membrane; IDA:CGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0140453; C:protein aggregate center; IEA:EnsemblFungi.
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; IGI:CGD.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0010619; P:adenylate cyclase-activating glucose-activated G protein-coupled receptor signaling pathway; IEA:EnsemblFungi.
DR GO; GO:0034605; P:cellular response to heat; IMP:CGD.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:EnsemblFungi.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; IEA:EnsemblFungi.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IGI:CGD.
DR GO; GO:1900429; P:negative regulation of filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0006457; P:protein folding; IGI:CGD.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:CGD.
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; IPR019805; Heat_shock_protein_90_CS.
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.
DR PROSITE; PS00298; HSP90; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..707
FT /note="Heat shock protein 90 homolog"
FT /id="PRO_0000062961"
FT REGION 216..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 703..707
FT /note="TPR repeat-binding"
FT COMPBIAS 230..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:6CJI"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:6CJI"
FT HELIX 32..54
FT /evidence="ECO:0007829|PDB:6CJI"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:6CJI"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:6CJP"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:6CJI"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:6CJI"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:6CJI"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:6CJI"
FT HELIX 101..113
FT /evidence="ECO:0007829|PDB:6CJI"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:6CJI"
FT HELIX 126..132
FT /evidence="ECO:0007829|PDB:6CJI"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:6CJI"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:6CJI"
FT STRAND 155..163
FT /evidence="ECO:0007829|PDB:6CJI"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:6CJI"
FT STRAND 171..180
FT /evidence="ECO:0007829|PDB:6CJI"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:6CJI"
FT HELIX 190..200
FT /evidence="ECO:0007829|PDB:6CJI"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:6CJI"
SQ SEQUENCE 707 AA; 80823 MW; 3BF614C70F2E5446 CRC64;
MADAKVETHE FTAEISQLMS LIINTVYSNK EIFLRELISN ASDALDKIRY QALSDPSQLE
SEPELFIRII PQKDQKVLEI RDSGIGMTKA DLVNNLGTIA KSGTKSFMEA LSAGADVSMI
GQFGVGFYSL FLVADHVQVI SKHNDDEQYV WESNAGGKFT VTLDETNERL GRGTMLRLFL
KEDQLEYLEE KRIKEVVKKH SEFVAYPIQL VVTKEVEKEV PETEEEDKAA EEDDKKPKLE
EVKDEEDEKK EKKTKTVKEE VTETEELNKT KPLWTRNPSD ITQDEYNAFY KSISNDWEDP
LAVKHFSVEG QLEFRAILFV PKRAPFDAFE SKKKKNNIKL YVRRVFITDD AEELIPEWLS
FIKGVVDSED LPLNLSREML QQNKILKVIR KNIVKKMIET FNEISEDQEQ FNQFYTAFSK
NIKLGIHEDA QNRQSLAKLL RFYSTKSSEE MTSLSDYVTR MPEHQKNIYY ITGESIKAVE
KSPFLDALKA KNFEVLFMVD PIDEYAMTQL KEFEDKKLVD ITKDFELEES DEEKAAREKE
IKEYEPLTKA LKDILGDQVE KVVVSYKLVD APAAIRTGQF GWSANMERIM KAQALRDTTM
SSYMSSKKTF EISPSSPIIK ELKKKVETDG AEDKTVKDLT TLLFDTALLT SGFTLDEPSN
FAHRINRLIA LGLNIDDDSE ETAVEPEATT TASTDEPAGE SAMEEVD
