HCH1_YEAST
ID HCH1_YEAST Reviewed; 153 AA.
AC P53834; D6W0R3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Hsp90 co-chaperone HCH1;
DE AltName: Full=High-copy Hsp90 suppressor protein 1;
GN Name=HCH1; OrderedLocusNames=YNL281W; ORFNames=N0589;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION IN HSP82 REGULATION.
RX PubMed=9990037; DOI=10.1073/pnas.96.4.1409;
RA Nathan D.F., Vos M.H., Lindquist S.;
RT "Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a
RT Saccharomyces cerevisiae Hsp90 loss-of-function mutation.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1409-1414(1999).
RN [4]
RP FUNCTION, AND INTERACTION WITH HSP82.
RX PubMed=12504007; DOI=10.1016/s1097-2765(02)00785-2;
RA Panaretou B., Siligardi G., Meyer P., Maloney A., Sullivan J.K., Singh S.,
RA Millson S.H., Clarke P.A., Naaby-Hansen S., Stein R., Cramer R.,
RA Mollapour M., Workman P., Piper P.W., Pearl L.H., Prodromou C.;
RT "Activation of the ATPase activity of hsp90 by the stress-regulated
RT cochaperone aha1.";
RL Mol. Cell 10:1307-1318(2002).
RN [5]
RP FUNCTION, AND INTERACTION WITH HSP82.
RX PubMed=12604615; DOI=10.1074/jbc.m212761200;
RA Lotz G.P., Lin H., Harst A., Obermann W.M.J.;
RT "Aha1 binds to the middle domain of Hsp90, contributes to client protein
RT activation, and stimulates the ATPase activity of the molecular
RT chaperone.";
RL J. Biol. Chem. 278:17228-17235(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Co-chaperone that binds to the molecular chaperone HSP82 and
CC stimulates its ATPase activity. Although not essential, it confers
CC thermotolerance when intracellular levels of HSP82 are limiting.
CC {ECO:0000269|PubMed:12504007, ECO:0000269|PubMed:12604615,
CC ECO:0000269|PubMed:9990037}.
CC -!- SUBUNIT: Monomer. Interacts with HSP82. {ECO:0000269|PubMed:12504007,
CC ECO:0000269|PubMed:12604615}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 8528 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AHA1 family. {ECO:0000305}.
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DR EMBL; Z71557; CAA96193.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10279.1; -; Genomic_DNA.
DR PIR; S63255; S63255.
DR RefSeq; NP_014118.1; NM_001183119.1.
DR AlphaFoldDB; P53834; -.
DR SMR; P53834; -.
DR BioGRID; 35560; 100.
DR DIP; DIP-4395N; -.
DR IntAct; P53834; 33.
DR MINT; P53834; -.
DR STRING; 4932.YNL281W; -.
DR iPTMnet; P53834; -.
DR MaxQB; P53834; -.
DR PaxDb; P53834; -.
DR PRIDE; P53834; -.
DR EnsemblFungi; YNL281W_mRNA; YNL281W; YNL281W.
DR GeneID; 855440; -.
DR KEGG; sce:YNL281W; -.
DR SGD; S000005225; HCH1.
DR VEuPathDB; FungiDB:YNL281W; -.
DR eggNOG; KOG2936; Eukaryota.
DR HOGENOM; CLU_132818_0_0_1; -.
DR InParanoid; P53834; -.
DR OMA; EFMHDED; -.
DR BioCyc; YEAST:G3O-33272-MON; -.
DR PRO; PR:P53834; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53834; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0001671; F:ATPase activator activity; IDA:SGD.
DR GO; GO:0051087; F:chaperone binding; IDA:SGD.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:InterPro.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IMP:SGD.
DR Gene3D; 3.15.10.20; -; 1.
DR InterPro; IPR036338; Aha1.
DR InterPro; IPR039981; AHSA-like.
DR InterPro; IPR015310; AHSA1_N.
DR PANTHER; PTHR13009; PTHR13009; 1.
DR Pfam; PF09229; Aha1_N; 1.
DR SMART; SM01000; Aha1_N; 1.
DR SUPFAM; SSF103111; SSF103111; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..153
FT /note="Hsp90 co-chaperone HCH1"
FT /id="PRO_0000215823"
SQ SEQUENCE 153 AA; 17246 MW; DAD84DBF9BF5DC9F CRC64;
MVVLNPNNWH WVDKNTLPWS KDYLNGKLTS LSTVSSDGKS KIELTQVSSI TGDSNVSQRK
GKPICYFDLQ LSMNVKVTNL DTNKDDEDDD GILADGKLEI PEFMHDESDI PILSQGFDAF
DGLVRSEFVP KVVETLLKYQ DDLIKEHSKD IQV
