AHA1_YEAST
ID AHA1_YEAST Reviewed; 350 AA.
AC Q12449; D6VSJ8; Q02565; Q7LIE3;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Hsp90 co-chaperone AHA1;
DE AltName: Full=Activator of Hsp90 ATPase protein 1;
GN Name=AHA1; OrderedLocusNames=YDR214W; ORFNames=YD8142.16, YD8142B.06;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 129-350.
RX PubMed=3515197; DOI=10.1038/320283a0;
RA Hartshorne T.A., Blumberg H., Young E.T.;
RT "Sequence homology of the yeast regulatory protein ADR1 with Xenopus
RT transcription factor TFIIIA.";
RL Nature 320:283-287(1986).
RN [5]
RP FUNCTION, INDUCTION, 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 [6]
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 [7]
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 [8]
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).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-156 IN COMPLEX WITH HSP82, AND
RP MUTAGENESIS OF ASP-53; ARG-59; LYS-60 AND LYS-62.
RX PubMed=14739935; DOI=10.1038/sj.emboj.7600060;
RA Meyer P.;
RT "Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90
RT chaperone machinery.";
RL EMBO J. 23:511-519(2004).
RN [12]
RP ERRATUM OF PUBMED:14739935.
RX PubMed=15039704; DOI=10.1038/sj.emboj.7600141;
RA Meyer P., Prodromou C., Liao C., Hu B., Mark Roe S., Vaughan C.K.,
RA Vlasic I., Panaretou B., Piper P.W., Pearl L.H.;
RL EMBO J. 23:1402-1410(2004).
CC -!- FUNCTION: Co-chaperone that binds to the molecular chaperone HSP82 and
CC stimulates its ATPase activity. Binding to HSP82 promotes a
CC conformational switch in the catalytic loop of HSP82, facilitating the
CC interaction of the catalytic 'Arg-380' with ATP in the N-terminal
CC nucleotide-binding domain. Although not essential, it confers
CC thermotolerance when intracellular levels of HSP82 are limiting.
CC {ECO:0000269|PubMed:12504007, ECO:0000269|PubMed:12604615}.
CC -!- SUBUNIT: Monomer. Interacts with HSP82. {ECO:0000269|PubMed:12504007,
CC ECO:0000269|PubMed:12604615, ECO:0000269|PubMed:14739935}.
CC -!- INTERACTION:
CC Q12449; P39009: DUN1; NbExp=2; IntAct=EBI-37072, EBI-6194;
CC Q12449; P15108: HSC82; NbExp=3; IntAct=EBI-37072, EBI-8666;
CC Q12449; P02829: HSP82; NbExp=13; IntAct=EBI-37072, EBI-8659;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:12504007}.
CC -!- MISCELLANEOUS: Present with 13939 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AHA1 family. {ECO:0000305}.
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DR EMBL; Z68194; CAA92357.1; -; Genomic_DNA.
DR EMBL; Z68195; CAA92365.1; -; Genomic_DNA.
DR EMBL; AY557694; AAS56020.1; -; Genomic_DNA.
DR EMBL; U28414; AAA73862.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12058.1; -; Genomic_DNA.
DR PIR; S61581; S61581.
DR RefSeq; NP_010500.3; NM_001180522.3.
DR PDB; 1USU; X-ray; 2.15 A; B=1-156.
DR PDB; 1USV; X-ray; 2.70 A; B/D/F/H=1-156.
DR PDB; 6XLB; EM; 3.80 A; C1/D1=1-350.
DR PDB; 6XLD; EM; 3.66 A; C=1-350.
DR PDB; 6XLE; EM; 2.74 A; C/D=1-350.
DR PDB; 6XLF; EM; 3.15 A; C/D=1-350.
DR PDB; 6XLG; EM; 2.71 A; C/D=1-350.
DR PDB; 6XLH; EM; 2.83 A; C/D=1-350.
DR PDBsum; 1USU; -.
DR PDBsum; 1USV; -.
DR PDBsum; 6XLB; -.
DR PDBsum; 6XLD; -.
DR PDBsum; 6XLE; -.
DR PDBsum; 6XLF; -.
DR PDBsum; 6XLG; -.
DR PDBsum; 6XLH; -.
DR AlphaFoldDB; Q12449; -.
DR BMRB; Q12449; -.
DR SMR; Q12449; -.
DR BioGRID; 32268; 143.
DR DIP; DIP-1831N; -.
DR IntAct; Q12449; 55.
DR MINT; Q12449; -.
DR STRING; 4932.YDR214W; -.
DR CarbonylDB; Q12449; -.
DR iPTMnet; Q12449; -.
DR MaxQB; Q12449; -.
DR PaxDb; Q12449; -.
DR PRIDE; Q12449; -.
DR EnsemblFungi; YDR214W_mRNA; YDR214W; YDR214W.
DR GeneID; 851800; -.
DR KEGG; sce:YDR214W; -.
DR SGD; S000002622; AHA1.
DR VEuPathDB; FungiDB:YDR214W; -.
DR eggNOG; KOG2936; Eukaryota.
DR GeneTree; ENSGT00940000173240; -.
DR HOGENOM; CLU_049046_1_0_1; -.
DR OMA; CEVNQRK; -.
DR BioCyc; YEAST:G3O-29796-MON; -.
DR EvolutionaryTrace; Q12449; -.
DR PRO; PR:Q12449; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12449; protein.
DR GO; GO:0005737; C:cytoplasm; IPI:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0001671; F:ATPase activator activity; IDA:UniProtKB.
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 Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR013538; Activator_of_Hsp90_ATPase.
DR InterPro; IPR036338; Aha1.
DR InterPro; IPR039981; AHSA-like.
DR InterPro; IPR015310; AHSA1_N.
DR InterPro; IPR023393; START-like_dom_sf.
DR PANTHER; PTHR13009; PTHR13009; 1.
DR Pfam; PF09229; Aha1_N; 1.
DR Pfam; PF08327; AHSA1; 1.
DR SMART; SM01000; Aha1_N; 1.
DR SUPFAM; SSF103111; SSF103111; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Reference proteome; Stress response.
FT CHAIN 1..350
FT /note="Hsp90 co-chaperone AHA1"
FT /id="PRO_0000215822"
FT REGION 158..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 53
FT /note="D->A: No effect on Hsp90 ATPase activity but reduces
FT Hsp90 binding affinity."
FT /evidence="ECO:0000269|PubMed:14739935"
FT MUTAGEN 53
FT /note="D->K: Decreases activation of Hsp90 ATPase activity
FT and substantially reduces Hsp90 binding affinity."
FT /evidence="ECO:0000269|PubMed:14739935"
FT MUTAGEN 59
FT /note="R->A: Decreases activation of Hsp90 ATPase activity
FT with a small reduction in Hsp90 binding affinity."
FT /evidence="ECO:0000269|PubMed:14739935"
FT MUTAGEN 60
FT /note="K->A: Decreased activation of Hsp90 ATPase activity
FT with a small reduction in Hsp90 binding affinity."
FT /evidence="ECO:0000269|PubMed:14739935"
FT MUTAGEN 62
FT /note="K->A: Decreased activation of Hsp90 ATPase activity
FT with a small reduction in Hsp90 binding affinity."
FT /evidence="ECO:0000269|PubMed:14739935"
FT CONFLICT 28
FT /note="L -> I (in Ref. 11)"
FT /evidence="ECO:0000305"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:6XLH"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:6XLH"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:1USU"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1USV"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:6XLH"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:1USU"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:1USU"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1USV"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6XLH"
FT STRAND 68..78
FT /evidence="ECO:0007829|PDB:1USU"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:1USV"
FT STRAND 88..99
FT /evidence="ECO:0007829|PDB:1USU"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:1USU"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1USU"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:6XLH"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:1USU"
FT HELIX 132..150
FT /evidence="ECO:0007829|PDB:1USU"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:6XLF"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:6XLH"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:6XLH"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:6XLE"
FT HELIX 226..232
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:6XLG"
FT TURN 264..267
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 268..275
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 297..305
FT /evidence="ECO:0007829|PDB:6XLG"
FT TURN 306..309
FT /evidence="ECO:0007829|PDB:6XLG"
FT STRAND 310..321
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 325..330
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:6XLG"
FT HELIX 338..343
FT /evidence="ECO:0007829|PDB:6XLG"
SQ SEQUENCE 350 AA; 39436 MW; 06DF6B40EB5050BE CRC64;
MVVNNPNNWH WVDKNCIGWA KEYFKQKLVG VEAGSVKDKK YAKIKSVSSI EGDCEVNQRK
GKVISLFDLK ITVLIEGHVD SKDGSALPFE GSINVPEVAF DSEASSYQFD ISIFKETSEL
SEAKPLIRSE LLPKLRQIFQ QFGKDLLATH GNDIQVPESQ VKSNYTRGNQ KSSFTEIKDS
ASKPKKNALP SSTSTSAPVS STNKVPQNGS GNSTSIYLEP TFNVPSSELY ETFLDKQRIL
AWTRSAQFFN SGPKLETKEK FELFGGNVIS ELVSCEKDKK LVFHWKLKDW SAPFNSTIEM
TFHESQEFHE TKLQVKWTGI PVGEEDRVRA NFEEYYVRSI KLTFGFGAVL
