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ATP-dependent molecular chaperone HSC82 (82 kDa heat shock cognate protein) (Heat shock protein Hsp90 constitutive isoform)

 HSC82_YEAST             Reviewed;         705 AA.
P15108; D6W010;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
25-OCT-2017, entry version 181.
RecName: Full=ATP-dependent molecular chaperone HSC82;
AltName: Full=82 kDa heat shock cognate protein;
AltName: Full=Heat shock protein Hsp90 constitutive isoform;
Name=HSC82; OrderedLocusNames=YMR186W; ORFNames=YM8010.16;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE, AND INDUCTION.
PubMed=2674684; DOI=10.1128/MCB.9.9.3919;
Borkovich K.A., Farrelly F.W., Finkelstein D.B., Taulien J.,
Lindquist S.;
"hsp82 is an essential protein that is required in higher
concentrations for growth of cells at higher temperatures.";
Mol. Cell. Biol. 9:3919-3930(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169872;
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S.,
Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome
XIII.";
Nature 387:90-93(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
PROTEIN SEQUENCE OF 2-8.
STRAIN=ATCC 204508 / S288c;
PubMed=7483834; DOI=10.1002/yea.320110702;
Boucherie H., Dujardin G., Kermorgant M., Monribot C., Slonimski P.P.,
Perrot M.;
"Two-dimensional protein map of Saccharomyces cerevisiae: construction
of a gene-protein index.";
Yeast 11:601-613(1995).
[5]
INDUCTION.
PubMed=9296388;
Zarzov P., Boucherie H., Mann C.;
"A yeast heat shock transcription factor (Hsf1) mutant is defective in
both Hsc82/Hsp82 synthesis and spindle pole body duplication.";
J. Cell Sci. 110:1879-1891(1997).
[6]
FUNCTION, AND INTERACTION WITH CNA2.
PubMed=11094077; DOI=10.1128/MCB.20.24.9262-9270.2000;
Imai J., Yahara I.;
"Role of HSP90 in salt stress tolerance via stabilization and
regulation of calcineurin.";
Mol. Cell. Biol. 20:9262-9270(2000).
[7]
MUTAGENESIS OF LEU-453 AND GLU-493.
PubMed=12121981; DOI=10.1074/jbc.M203038200;
Matsumoto S., Tanaka E., Nemoto T.K., Ono T., Takagi T., Imai J.,
Kimura Y., Yahara I., Kobayakawa T., Ayuse T., Oi K., Mizuno A.;
"Interaction between the N-terminal and middle regions is essential
for the in vivo function of HSP90 molecular chaperone.";
J. Biol. Chem. 277:34959-34966(2002).
[8]
INTERACTION WITH SGT1.
PubMed=15340069; DOI=10.1128/MCB.24.18.8069-8079.2004;
Bansal P.K., Abdulle R., Kitagawa K.;
"Sgt1 associates with Hsp90: an initial step of assembly of the core
kinetochore complex.";
Mol. Cell. Biol. 24:8069-8079(2004).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
STRAIN=ATCC 76625 / YPH499;
PubMed=14576278; DOI=10.1073/pnas.2135385100;
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P.,
Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B.,
Rehling P., Pfanner N., Meisinger C.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
[12]
INTERACTION WITH NAP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18086883; DOI=10.1128/MCB.01035-07;
Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F.,
Pemberton L.F.;
"Phosphorylation by casein kinase 2 regulates Nap1 localization and
function.";
Mol. Cell. Biol. 28:1313-1325(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-653, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
-!- FUNCTION: Molecular chaperone that promotes the maturation,
structural maintenance and proper regulation of specific target
proteins involved in cell cycle control and signal transduction
such as CNA2. Undergoes a functional cycle that is linked to its
ATPase activity (By similarity). Interacts dynamically with
various co-chaperones that modulate its substrate recognition,
ATPase cycle and chaperone function. Required for growth at high
temperatures. {ECO:0000250, ECO:0000269|PubMed:11094077}.
-!- SUBUNIT: Interacts with the co-chaperone SGT1. Interacts directly
with the substrate CNA2. Interacts with NAP1.
{ECO:0000269|PubMed:11094077, ECO:0000269|PubMed:15340069,
ECO:0000269|PubMed:18086883}.
-!- INTERACTION:
Q12449:AHA1; NbExp=3; IntAct=EBI-8666, EBI-37072;
P08566:ARO1; NbExp=3; IntAct=EBI-8666, EBI-2883;
P33313:CNS1; NbExp=2; IntAct=EBI-8666, EBI-4806;
P47103:CPR7; NbExp=2; IntAct=EBI-8666, EBI-5436;
P53043:PPT1; NbExp=2; IntAct=EBI-8666, EBI-13796;
P38164:SEA4; NbExp=2; IntAct=EBI-8666, EBI-21365;
Q02821:SRP1; NbExp=2; IntAct=EBI-8666, EBI-1797;
P10591:SSA1; NbExp=2; IntAct=EBI-8666, EBI-8591;
P15705:STI1; NbExp=3; IntAct=EBI-8666, EBI-18418;
-!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion.
-!- INDUCTION: Expressed constitutively at a high level and is
moderately induced by high temperatures dependent on transcription
factor HSF1. {ECO:0000269|PubMed:2674684,
ECO:0000269|PubMed:9296388}.
-!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
repeat-containing proteins. {ECO:0000250}.
-!- MISCELLANEOUS: Present with 132053 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the heat shock protein 90 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M26044; AAA02813.1; -; Unassigned_DNA.
EMBL; Z49808; CAA89919.1; -; Genomic_DNA.
EMBL; BK006946; DAA10084.1; -; Genomic_DNA.
PIR; S55133; S55133.
RefSeq; NP_013911.1; NM_001182692.1.
ProteinModelPortal; P15108; -.
SMR; P15108; -.
BioGrid; 35364; 1166.
DIP; DIP-1524N; -.
IntAct; P15108; 177.
MINT; MINT-393096; -.
STRING; 4932.YMR186W; -.
ChEMBL; CHEMBL4199; -.
iPTMnet; P15108; -.
SWISS-2DPAGE; P15108; -.
MaxQB; P15108; -.
PRIDE; P15108; -.
TopDownProteomics; P15108; -.
EnsemblFungi; YMR186W; YMR186W; YMR186W.
GeneID; 855224; -.
KEGG; sce:YMR186W; -.
EuPathDB; FungiDB:YMR186W; -.
SGD; S000004798; HSC82.
GeneTree; ENSGT00900000140978; -.
HOGENOM; HOG000031988; -.
InParanoid; P15108; -.
KO; K04079; -.
OMA; YESFGKN; -.
OrthoDB; EOG092C1GW3; -.
BioCyc; YEAST:G3O-32874-MONOMER; -.
Reactome; R-SCE-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
Reactome; R-SCE-203615; eNOS activation.
Reactome; R-SCE-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-SCE-3371511; HSF1 activation.
Reactome; R-SCE-3371568; Attenuation phase.
Reactome; R-SCE-3371571; HSF1-dependent transactivation.
Reactome; R-SCE-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-SCE-6798695; Neutrophil degranulation.
Reactome; R-SCE-844456; The NLRP3 inflammasome.
PRO; PR:P15108; -.
Proteomes; UP000002311; Chromosome XIII.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IDA:SGD.
GO; GO:0042623; F:ATPase activity, coupled; ISS:SGD.
GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
GO; GO:0006458; P:'de novo' protein folding; ISS:SGD.
GO; GO:0000492; P:box C/D snoRNP assembly; IMP:SGD.
GO; GO:0034605; P:cellular response to heat; IMP:SGD.
GO; GO:0043248; P:proteasome assembly; IMP:SGD.
GO; GO:0006457; P:protein folding; IMP:SGD.
GO; GO:0042026; P:protein refolding; ISS:SGD.
GO; GO:0000723; P:telomere maintenance; IMP:SGD.
CDD; cd00075; HATPase_c; 1.
Gene3D; 3.30.565.10; -; 1.
HAMAP; MF_00505; HSP90; 1.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR019805; Heat_shock_protein_90_CS.
InterPro; IPR037196; HSP90_C.
InterPro; IPR001404; Hsp90_fam.
InterPro; IPR020575; Hsp90_N.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
PANTHER; PTHR11528; PTHR11528; 1.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF00183; HSP90; 1.
PIRSF; PIRSF002583; Hsp90; 1.
PRINTS; PR00775; HEATSHOCK90.
SMART; SM00387; HATPase_c; 1.
SUPFAM; SSF110942; SSF110942; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF55874; SSF55874; 1.
PROSITE; PS00298; HSP90; 1.
1: Evidence at protein level;
ATP-binding; Chaperone; Coiled coil; Complete proteome; Cytoplasm;
Direct protein sequencing; Mitochondrion; Nucleotide-binding;
Phosphoprotein; Reference proteome; Repeat; Stress response.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7483834}.
CHAIN 2 705 ATP-dependent molecular chaperone HSC82.
/FTId=PRO_0000062958.
REPEAT 221 225 1.
REPEAT 226 230 2.
REPEAT 232 236 3.
REPEAT 246 250 4.
REGION 221 259 4 X 5 AA repeats of [DE]-[DE]-[DE]-K-K;
highly charged region.
MOTIF 701 705 TPR repeat-binding.
BINDING 37 37 ATP. {ECO:0000250}.
BINDING 79 79 ATP. {ECO:0000250}.
BINDING 98 98 ATP. {ECO:0000250}.
BINDING 124 124 ATP; via amide nitrogen. {ECO:0000250}.
BINDING 376 376 ATP. {ECO:0000250}.
MOD_RES 653 653 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MUTAGEN 453 453 L->A: Leads to growth defect at 37
degrees Celsius, probably by disrupting
the intramolecular interaction of the N-
termini with the middle domains; when
associated with A-493.
{ECO:0000269|PubMed:12121981}.
MUTAGEN 493 493 E->A: Leads to growth defect at 37
degrees Celsius, probably by disrupting
the intramolecular interaction of the N-
termini with the middle domains; when
associated with A-453.
{ECO:0000269|PubMed:12121981}.
CONFLICT 619 619 K -> I (in Ref. 1). {ECO:0000305}.
CONFLICT 621 621 L -> T (in Ref. 1). {ECO:0000305}.
SEQUENCE 705 AA; 80900 MW; DBD41524091B1F9B CRC64;
MAGETFEFQA EITQLMSLII NTVYSNKEIF LRELISNASD ALDKIRYQAL SDPKQLETEP
DLFIRITPKP EEKVLEIRDS GIGMTKAELI NNLGTIAKSG TKAFMEALSA GADVSMIGQF
GVGFYSLFLV ADRVQVISKN NEDEQYIWES NAGGSFTVTL DEVNERIGRG TVLRLFLKDD
QLEYLEEKRI KEVIKRHSEF VAYPIQLLVT KEVEKEVPIP EEEKKDEEKK DEDDKKPKLE
EVDEEEEEKK PKTKKVKEEV QELEELNKTK PLWTRNPSDI TQEEYNAFYK SISNDWEDPL
YVKHFSVEGQ LEFRAILFIP KRAPFDLFES KKKKNNIKLY VRRVFITDEA EDLIPEWLSF
VKGVVDSEDL PLNLSREMLQ QNKIMKVIRK NIVKKLIEAF NEIAEDSEQF DKFYSAFAKN
IKLGVHEDTQ NRAALAKLLR YNSTKSVDEL TSLTDYVTRM PEHQKNIYYI TGESLKAVEK
SPFLDALKAK NFEVLFLTDP IDEYAFTQLK EFEGKTLVDI TKDFELEETD EEKAEREKEI
KEYEPLTKAL KDILGDQVEK VVVSYKLLDA PAAIRTGQFG WSANMERIMK AQALRDSSMS
SYMSSKKTFE ISPKSPIIKE LKKRVDEGGA QDKTVKDLTN LLFETALLTS GFSLEEPTSF
ASRINRLISL GLNIDEDEET ETAPEASTEA PVEEVPADTE MEEVD


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