HSP82_YEAST
ID HSP82_YEAST Reviewed; 709 AA.
AC P02829; D6W3D1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 236.
DE RecName: Full=ATP-dependent molecular chaperone HSP82;
DE AltName: Full=82 kDa heat shock protein;
DE AltName: Full=Heat shock protein Hsp90 heat-inducible isoform;
GN Name=HSP82; Synonyms=HSP90; OrderedLocusNames=YPL240C;
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.
RX PubMed=6325446; DOI=10.1016/s0021-9258(18)91077-x;
RA Farrelly F.W., Finkelstein D.B.;
RT "Complete sequence of the heat shock-inducible HSP90 gene of Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 259:5745-5751(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
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 [4]
RP INDUCTION.
RX PubMed=2674684; DOI=10.1128/mcb.9.9.3919-3930.1989;
RA Borkovich K.A., Farrelly F.W., Finkelstein D.B., Taulien J., Lindquist S.;
RT "hsp82 is an essential protein that is required in higher concentrations
RT for growth of cells at higher temperatures.";
RL Mol. Cell. Biol. 9:3919-3930(1989).
RN [5]
RP ATPASE ACTIVITY.
RX PubMed=8419347; DOI=10.1016/s0021-9258(18)54100-4;
RA Nadeau K., Das A., Walsh C.T.;
RT "Hsp90 chaperonins possess ATPase activity and bind heat shock
RT transcription factors and peptidyl prolyl isomerases.";
RL J. Biol. Chem. 268:1479-1487(1993).
RN [6]
RP MUTAGENESIS OF GLY-313; GLU-431; THR-525; ALA-576 AND ARG-579.
RX PubMed=8248264; DOI=10.1073/pnas.90.23.11424;
RA Bohen S.P., Yamamoto K.R.;
RT "Isolation of Hsp90 mutants by screening for decreased steroid receptor
RT function.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:11424-11428(1993).
RN [7]
RP INTERACTION WITH STI1 AND CPR6.
RX PubMed=7929182; DOI=10.1016/s0021-9258(17)31486-2;
RA Chang H.-C.J., Lindquist S.;
RT "Conservation of Hsp90 macromolecular complexes in Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 269:24983-24988(1994).
RN [8]
RP MUTAGENESIS OF THR-22; ALA-41; GLY-81; THR-101; GLY-170; GLY-313; GLU-381
RP AND ALA-587.
RX PubMed=7791797; DOI=10.1128/mcb.15.7.3917;
RA Nathan D.F., Lindquist S.;
RT "Mutational analysis of Hsp90 function: interactions with a steroid
RT receptor and a protein kinase.";
RL Mol. Cell. Biol. 15:3917-3925(1995).
RN [9]
RP INTERACTION WITH CPR6 AND CPR7.
RX PubMed=8939862; DOI=10.1126/science.274.5293.1713;
RA Duina A.A., Chang H.-C.J., Marsh J.A., Lindquist S., Gaber R.F.;
RT "A cyclophilin function in Hsp90-dependent signal transduction.";
RL Science 274:1713-1715(1996).
RN [10]
RP INDUCTION.
RX PubMed=9296388; DOI=10.1242/jcs.110.16.1879;
RA Zarzov P., Boucherie H., Mann C.;
RT "A yeast heat shock transcription factor (Hsf1) mutant is defective in both
RT Hsc82/Hsp82 synthesis and spindle pole body duplication.";
RL J. Cell Sci. 110:1879-1891(1997).
RN [11]
RP INTERACTION WITH SBA1.
RX PubMed=9817749; DOI=10.1083/jcb.143.4.901;
RA Obermann W.M., Sondermann H., Russo A.A., Pavletich N.P., Hartl F.U.;
RT "In vivo function of Hsp90 is dependent on ATP binding and ATP
RT hydrolysis.";
RL J. Cell Biol. 143:901-910(1998).
RN [12]
RP INTERACTION WITH SBA1, AND MUTAGENESIS OF ALA-97 AND SER-485.
RX PubMed=9632755; DOI=10.1128/mcb.18.7.3727;
RA Fang Y., Fliss A.E., Rao J., Caplan A.J.;
RT "SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate
RT p23 proteins.";
RL Mol. Cell. Biol. 18:3727-3734(1998).
RN [13]
RP INTERACTION WITH HAP1.
RX PubMed=9632766; DOI=10.1128/mcb.18.7.3819;
RA Zhang L., Hach A., Wang C.;
RT "Molecular mechanism governing heme signaling in yeast: a higher-order
RT complex mediates heme regulation of the transcriptional activator HAP1.";
RL Mol. Cell. Biol. 18:3819-3828(1998).
RN [14]
RP INTERACTION WITH CNS1.
RX PubMed=9819421; DOI=10.1128/mcb.18.12.7344;
RA Dolinski K.J., Cardenas M.E., Heitman J.;
RT "CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae
RT that suppresses cyclophilin 40 mutations and interacts with Hsp90.";
RL Mol. Cell. Biol. 18:7344-7352(1998).
RN [15]
RP INTERACTION WITH SSE1.
RX PubMed=10480867; DOI=10.1074/jbc.274.38.26654;
RA Liu X.-D., Morano K.A., Thiele D.J.;
RT "The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone.";
RL J. Biol. Chem. 274:26654-26660(1999).
RN [16]
RP INTERACTION WITH GCN2.
RX PubMed=10567567; DOI=10.1128/mcb.19.12.8422;
RA Donze O., Picard D.;
RT "Hsp90 binds and regulates Gcn2, the ligand-inducible kinase of the alpha
RT subunit of eukaryotic translation initiation factor 2.";
RL Mol. Cell. Biol. 19:8422-8432(1999).
RN [17]
RP BINDING TO TPR REPEATS.
RX PubMed=10786835; DOI=10.1016/s0092-8674(00)80830-2;
RA Scheufler C., Brinker A., Bourenkov G., Pegoraro S., Moroder L.,
RA Bartunik H., Hartl F.U., Moarefi I.;
RT "Structure of TPR domain-peptide complexes: critical elements in the
RT assembly of the Hsp70-Hsp90 multichaperone machine.";
RL Cell 101:199-210(2000).
RN [18]
RP ATPASE ACTIVITY, AND MUTAGENESIS OF ALA-107.
RX PubMed=10944121; DOI=10.1093/emboj/19.16.4383;
RA Prodromou C., Panaretou B., Chohan S., Siligardi G., O'Brien R.,
RA Ladbury J.E., Roe S.M., Piper P.W., Pearl L.H.;
RT "The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient
RT dimerization of the N-terminal domains.";
RL EMBO J. 19:4383-4392(2000).
RN [19]
RP INTERACTION WITH CDC37 AND STE11.
RX PubMed=10664467; DOI=10.1016/s0014-5793(00)01134-0;
RA Abbas-Terki T., Donze O., Picard D.;
RT "The molecular chaperone Cdc37 is required for Ste11 function and
RT pheromone-induced cell cycle arrest.";
RL FEBS Lett. 467:111-116(2000).
RN [20]
RP INTERACTION WITH AHA1 AND HCH1.
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 [21]
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 [22]
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 [23]
RP MUTAGENESIS OF GLY-83.
RX PubMed=18256191; DOI=10.1242/dev.018150;
RA Hawkins T.A., Haramis A.P., Etard C., Prodromou C., Vaughan C.K.,
RA Ashworth R., Ray S., Behra M., Holder N., Talbot W.S., Pearl L.H.,
RA Strahle U., Wilson S.W.;
RT "The ATPase-dependent chaperoning activity of Hsp90a regulates thick
RT filament formation and integration during skeletal muscle
RT myofibrillogenesis.";
RL Development 135:1147-1156(2008).
RN [24]
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 [25] {ECO:0007744|PDB:1AH6, ECO:0007744|PDB:1AH8}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=9187656; DOI=10.1038/nsb0697-477;
RA Prodromou C., Roe S.M., Piper P.W., Pearl L.H.;
RT "A molecular clamp in the crystal structure of the N-terminal domain of the
RT yeast Hsp90 chaperone.";
RL Nat. Struct. Biol. 4:477-482(1997).
RN [26] {ECO:0007744|PDB:1A4H, ECO:0007744|PDB:1AM1, ECO:0007744|PDB:1AMW}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-214 IN COMPLEX WITH ADP AND
RP GELDANAMYCIN.
RX PubMed=9230303; DOI=10.1016/s0092-8674(00)80314-1;
RA Prodromou C., Roe S.M., O'Brien R., Ladbury J.E., Piper P.W., Pearl L.H.;
RT "Identification and structural characterization of the ATP/ADP-binding site
RT in the Hsp90 molecular chaperone.";
RL Cell 90:65-75(1997).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 273-560, AND MUTAGENESIS OF
RP PHE-349; ARG-380 AND GLN-384.
RX PubMed=12667448; DOI=10.1016/s1097-2765(03)00065-0;
RA Meyer P., Prodromou C., Hu B., Vaughan C.K., Roe S.M., Panaretou B.,
RA Piper P.W., Pearl L.H.;
RT "Structural and functional analysis of the middle segment of hsp90:
RT implications for ATP hydrolysis and client protein and cochaperone
RT interactions.";
RL Mol. Cell 11:647-658(2003).
RN [28] {ECO:0007744|PDB:1US7}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-214 IN COMPLEX WITH HUMAN CDC37.
RX PubMed=14718169; DOI=10.1016/s0092-8674(03)01027-4;
RA Roe S.M., Ali M.M., Meyer P., Vaughan C.K., Panaretou B., Piper P.W.,
RA Prodromou C., Pearl L.H.;
RT "The Mechanism of Hsp90 regulation by the protein kinase-specific
RT cochaperone p50(cdc37).";
RL Cell 116:87-98(2004).
RN [29] {ECO:0007744|PDB:1USU, ECO:0007744|PDB:1USV}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 272-530 IN COMPLEX WITH AHA1, AND
RP MUTAGENESIS OF LYS-387.
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 [30]
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).
RN [31]
RP MUTAGENESIS OF ALA-577.
RX PubMed=19696785; DOI=10.1038/embor.2009.153;
RA Retzlaff M., Stahl M., Eberl H.C., Lagleder S., Beck J., Kessler H.,
RA Buchner J.;
RT "Hsp90 is regulated by a switch point in the C-terminal domain.";
RL EMBO Rep. 10:1147-1153(2009).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-214 IN COMPLEX WITH RADICICOL,
RP AND ATPASE ACTIVITY.
RX PubMed=9925731; DOI=10.1021/jm980403y;
RA Roe S.M., Prodromou C., O'Brien R., Ladbury J.E., Piper P.W., Pearl L.H.;
RT "Structural basis for inhibition of the Hsp90 molecular chaperone by the
RT antitumor antibiotics radicicol and geldanamycin.";
RL J. Med. Chem. 42:260-266(1999).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1-214 IN COMPLEX WITH INHIBITORS,
RP AND FUNCTION.
RX PubMed=17114002; DOI=10.1016/j.chembiol.2006.09.015;
RA Proisy N., Sharp S.Y., Boxall K., Connelly S., Roe S.M., Prodromou C.,
RA Slawin A.M., Pearl L.H., Workman P., Moody C.J.;
RT "Inhibition of Hsp90 with synthetic macrolactones: synthesis and structural
RT and biological evaluation of ring and conformational analogs of
RT radicicol.";
RL Chem. Biol. 13:1203-1215(2006).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 25-210, AND ATPASE ACTIVITY.
RX PubMed=16461354; DOI=10.1074/jbc.m510142200;
RA Richter K., Moser S., Hagn F., Friedrich R., Hainzl O., Heller M.,
RA Schlee S., Kessler H., Reinstein J., Buchner J.;
RT "Intrinsic inhibition of the Hsp90 ATPase activity.";
RL J. Biol. Chem. 281:11301-11311(2006).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1-677 IN COMPLEX WITH SBA1 AND
RP ATP, AND SUBUNIT.
RX PubMed=16625188; DOI=10.1038/nature04716;
RA Ali M.M., Roe S.M., Vaughan C.K., Meyer P., Panaretou B., Piper P.W.,
RA Prodromou C., Pearl L.H.;
RT "Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone
RT complex.";
RL Nature 440:1013-1017(2006).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-219 IN COMPLEX WITH INHIBITOR,
RP AND ATPASE ACTIVITY.
RX PubMed=18357975; DOI=10.1021/jm701558c;
RA Martin C.J., Gaisser S., Challis I.R., Carletti I., Wilkinson B.,
RA Gregory M., Prodromou C., Roe S.M., Pearl L.H., Boyd S.M., Zhang M.Q.;
RT "Molecular characterization of macbecin as an Hsp90 inhibitor.";
RL J. Med. Chem. 51:2853-2857(2008).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-220 IN COMPLEX WITH ADP;
RP GELDANAMYCIN AND RADICICOL.
RX PubMed=19236053; DOI=10.1021/cb9000316;
RA Prodromou C., Nuttall J.M., Millson S.H., Roe S.M., Sim T.S., Tan D.,
RA Workman P., Pearl L.H., Piper P.W.;
RT "Structural basis of the radicicol resistance displayed by a fungal
RT hsp90.";
RL ACS Chem. Biol. 4:289-297(2009).
CC -!- FUNCTION: Molecular chaperone that promotes the maturation, structural
CC maintenance and proper regulation of specific target proteins involved
CC in cell cycle control and signal transduction. Undergoes a functional
CC cycle that is linked to its ATPase activity. The nucleotide-free form
CC of the dimer is found in an open conformation in which the N-termini
CC are not dimerized and the complex is ready for client protein binding.
CC Binding of ATP induces large conformational changes, resulting in the
CC formation of a ring-like closed structure in which the N-terminal
CC domains associate intramolecularly with the middle domain and also
CC dimerize with each other, stimulating their intrinsic ATPase activity
CC and acting as a clamp on the substrate. Finally, ATP hydrolysis results
CC in the release of the substrate. This cycle probably induces
CC conformational changes in the client proteins, thereby causing their
CC activation. Interacts dynamically with various co-chaperones that
CC modulate its substrate recognition, ATPase cycle and chaperone
CC function. Required for growth at high temperatures.
CC {ECO:0000269|PubMed:17114002}.
CC -!- ACTIVITY REGULATION: Inhibited by geldanamycin, macbecin I and
CC radicicol, which bind to the ATP-binding pocket. Co-chaperones CDC37,
CC SBA1 and STI1 reduce ATPase activity. Co-chaperones AHA1 and HCH1
CC increase ATPase activity.
CC -!- SUBUNIT: Homodimer. Interacts with the co-chaperones AHA1, CDC37, CNS1,
CC CPR6, CPR7, HCH1, SBA1, SSE1 and STI1. CNS1, CPR6, CPR7 and STI1.
CC Interacts directly with the substrates GCN2, HAP1 and STE11.
CC {ECO:0000269|PubMed:10480867, ECO:0000269|PubMed:10567567,
CC ECO:0000269|PubMed:10664467, ECO:0000269|PubMed:12504007,
CC ECO:0000269|PubMed:14718169, ECO:0000269|PubMed:14739935,
CC ECO:0000269|PubMed:16625188, ECO:0000269|PubMed:17114002,
CC ECO:0000269|PubMed:18357975, ECO:0000269|PubMed:19236053,
CC ECO:0000269|PubMed:7929182, ECO:0000269|PubMed:8939862,
CC ECO:0000269|PubMed:9230303, ECO:0000269|PubMed:9632755,
CC ECO:0000269|PubMed:9632766, ECO:0000269|PubMed:9817749,
CC ECO:0000269|PubMed:9819421, ECO:0000269|PubMed:9925731}.
CC -!- INTERACTION:
CC P02829; P60010: ACT1; NbExp=2; IntAct=EBI-8659, EBI-2169;
CC P02829; P27616: ADE1; NbExp=2; IntAct=EBI-8659, EBI-14257;
CC P02829; Q12449: AHA1; NbExp=13; IntAct=EBI-8659, EBI-37072;
CC P02829; P53858: BNI4; NbExp=2; IntAct=EBI-8659, EBI-3704;
CC P02829; P06101: CDC37; NbExp=3; IntAct=EBI-8659, EBI-4266;
CC P02829; P33313: CNS1; NbExp=6; IntAct=EBI-8659, EBI-4806;
CC P02829; P53691: CPR6; NbExp=13; IntAct=EBI-8659, EBI-5429;
CC P02829; P47103: CPR7; NbExp=6; IntAct=EBI-8659, EBI-5436;
CC P02829; P02829: HSP82; NbExp=11; IntAct=EBI-8659, EBI-8659;
CC P02829; P43581: HXT10; NbExp=2; IntAct=EBI-8659, EBI-8750;
CC P02829; P27705: MIG1; NbExp=3; IntAct=EBI-8659, EBI-10913;
CC P02829; P35198: MTH1; NbExp=3; IntAct=EBI-8659, EBI-11561;
CC P02829; P32832: NPL6; NbExp=2; IntAct=EBI-8659, EBI-12202;
CC P02829; P38768: PIH1; NbExp=4; IntAct=EBI-8659, EBI-24499;
CC P02829; Q03407: PKH1; NbExp=2; IntAct=EBI-8659, EBI-32467;
CC P02829; P53043: PPT1; NbExp=8; IntAct=EBI-8659, EBI-13796;
CC P02829; P32264: PRO1; NbExp=3; IntAct=EBI-8659, EBI-13879;
CC P02829; P28707: SBA1; NbExp=7; IntAct=EBI-8659, EBI-26838;
CC P02829; P41811: SEC27; NbExp=2; IntAct=EBI-8659, EBI-4898;
CC P02829; Q08446: SGT1; NbExp=2; IntAct=EBI-8659, EBI-17070;
CC P02829; Q00772: SLT2; NbExp=5; IntAct=EBI-8659, EBI-17372;
CC P02829; P41808: SMK1; NbExp=3; IntAct=EBI-8659, EBI-17457;
CC P02829; P10591: SSA1; NbExp=3; IntAct=EBI-8659, EBI-8591;
CC P02829; P10592: SSA2; NbExp=2; IntAct=EBI-8659, EBI-8603;
CC P02829; P32589: SSE1; NbExp=3; IntAct=EBI-8659, EBI-8648;
CC P02829; P15705: STI1; NbExp=18; IntAct=EBI-8659, EBI-18418;
CC P02829; P25638: TAH1; NbExp=10; IntAct=EBI-8659, EBI-21956;
CC P02829; Q12407: YDL199C; NbExp=2; IntAct=EBI-8659, EBI-33162;
CC P02829; P0CS82: HAP1; Xeno; NbExp=3; IntAct=EBI-8659, EBI-5419;
CC P02829; P04637: TP53; Xeno; NbExp=8; IntAct=EBI-8659, EBI-366083;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Expressed constitutively and induced by high temperatures
CC dependent on transcription factor HSF1. According to PubMed:2674684, it
CC is constitutively expressed at low levels, however, due to the
CC specificity of the antibody, this result is unsure.
CC {ECO:0000269|PubMed:2674684, ECO:0000269|PubMed:9296388}.
CC -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC repeat-containing proteins like the co-chaperones AHA1, CDC37, CNS1,
CC CPR6, CPR7, HCH1, SBA1, SSE1 and STI1. CNS1, CPR6, CPR7 and STI1.
CC -!- MISCELLANEOUS: Present with 444943 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; K01387; AAA02743.1; -; Unassigned_RNA.
DR EMBL; Z67751; CAA91604.1; -; Genomic_DNA.
DR EMBL; Z73596; CAA97961.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11197.1; -; Genomic_DNA.
DR PIR; A03313; HHBY90.
DR RefSeq; NP_015084.1; NM_001184054.1.
DR PDB; 1A4H; X-ray; 2.50 A; A=1-220.
DR PDB; 1AH6; X-ray; 1.80 A; A=1-220.
DR PDB; 1AH8; X-ray; 2.10 A; A/B=1-220.
DR PDB; 1AM1; X-ray; 2.00 A; A=2-214.
DR PDB; 1AMW; X-ray; 1.85 A; A=1-214.
DR PDB; 1BGQ; X-ray; 2.50 A; A=1-214.
DR PDB; 1HK7; X-ray; 2.50 A; A/B=273-560.
DR PDB; 1US7; X-ray; 2.30 A; A=1-214.
DR PDB; 1USU; X-ray; 2.15 A; A=273-530.
DR PDB; 1USV; X-ray; 2.70 A; A/C/E/G=272-530.
DR PDB; 1ZW9; X-ray; 1.90 A; A=1-220.
DR PDB; 1ZWH; X-ray; 1.65 A; A=1-220.
DR PDB; 2AKP; X-ray; 1.94 A; A/B=25-210.
DR PDB; 2BRC; X-ray; 1.60 A; A=1-214.
DR PDB; 2BRE; X-ray; 2.00 A; A/B=1-219.
DR PDB; 2CG9; X-ray; 3.10 A; A/B=1-677.
DR PDB; 2CGE; X-ray; 3.00 A; A/B/D=273-677.
DR PDB; 2CGF; X-ray; 2.20 A; A=1-214.
DR PDB; 2FXS; X-ray; 2.00 A; A=1-220.
DR PDB; 2IWS; X-ray; 2.70 A; A=1-214.
DR PDB; 2IWU; X-ray; 2.80 A; A=1-214.
DR PDB; 2IWX; X-ray; 1.50 A; A=1-214.
DR PDB; 2LSV; NMR; -; B=701-709.
DR PDB; 2VW5; X-ray; 1.90 A; A/B/C/D=1-214.
DR PDB; 2VWC; X-ray; 2.40 A; A=1-219.
DR PDB; 2WEP; X-ray; 2.00 A; A=1-220.
DR PDB; 2WEQ; X-ray; 2.20 A; A=1-220.
DR PDB; 2WER; X-ray; 1.60 A; A/B=1-220.
DR PDB; 2XD6; X-ray; 2.20 A; A=1-214.
DR PDB; 2XX2; X-ray; 1.85 A; A/B/C/D=1-214.
DR PDB; 2XX4; X-ray; 2.20 A; A=1-214.
DR PDB; 2XX5; X-ray; 2.00 A; A=1-214.
DR PDB; 2YGA; X-ray; 2.37 A; A=1-220.
DR PDB; 2YGE; X-ray; 1.96 A; A=1-220.
DR PDB; 2YGF; X-ray; 2.00 A; A=1-220.
DR PDB; 3C0E; X-ray; 1.90 A; A=1-220.
DR PDB; 3C11; X-ray; 1.60 A; A=1-220.
DR PDB; 3FP2; X-ray; 1.98 A; Q=698-709.
DR PDB; 4AS9; X-ray; 2.71 A; A=1-220.
DR PDB; 4ASA; X-ray; 2.25 A; A=1-220.
DR PDB; 4ASB; X-ray; 3.08 A; A=1-220.
DR PDB; 4ASF; X-ray; 2.60 A; A=1-220.
DR PDB; 4ASG; X-ray; 2.20 A; A=1-220.
DR PDB; 4CE1; X-ray; 2.01 A; A=1-214.
DR PDB; 4CE2; X-ray; 2.38 A; A=1-214.
DR PDB; 4CE3; X-ray; 2.31 A; A=1-214.
DR PDB; 5MGX; X-ray; 2.18 A; A/B/C/D=702-709.
DR PDBsum; 1A4H; -.
DR PDBsum; 1AH6; -.
DR PDBsum; 1AH8; -.
DR PDBsum; 1AM1; -.
DR PDBsum; 1AMW; -.
DR PDBsum; 1BGQ; -.
DR PDBsum; 1HK7; -.
DR PDBsum; 1US7; -.
DR PDBsum; 1USU; -.
DR PDBsum; 1USV; -.
DR PDBsum; 1ZW9; -.
DR PDBsum; 1ZWH; -.
DR PDBsum; 2AKP; -.
DR PDBsum; 2BRC; -.
DR PDBsum; 2BRE; -.
DR PDBsum; 2CG9; -.
DR PDBsum; 2CGE; -.
DR PDBsum; 2CGF; -.
DR PDBsum; 2FXS; -.
DR PDBsum; 2IWS; -.
DR PDBsum; 2IWU; -.
DR PDBsum; 2IWX; -.
DR PDBsum; 2LSV; -.
DR PDBsum; 2VW5; -.
DR PDBsum; 2VWC; -.
DR PDBsum; 2WEP; -.
DR PDBsum; 2WEQ; -.
DR PDBsum; 2WER; -.
DR PDBsum; 2XD6; -.
DR PDBsum; 2XX2; -.
DR PDBsum; 2XX4; -.
DR PDBsum; 2XX5; -.
DR PDBsum; 2YGA; -.
DR PDBsum; 2YGE; -.
DR PDBsum; 2YGF; -.
DR PDBsum; 3C0E; -.
DR PDBsum; 3C11; -.
DR PDBsum; 3FP2; -.
DR PDBsum; 4AS9; -.
DR PDBsum; 4ASA; -.
DR PDBsum; 4ASB; -.
DR PDBsum; 4ASF; -.
DR PDBsum; 4ASG; -.
DR PDBsum; 4CE1; -.
DR PDBsum; 4CE2; -.
DR PDBsum; 4CE3; -.
DR PDBsum; 5MGX; -.
DR AlphaFoldDB; P02829; -.
DR BMRB; P02829; -.
DR SMR; P02829; -.
DR BioGRID; 35923; 1868.
DR ComplexPortal; CPX-1276; HMC complex.
DR DIP; DIP-2262N; -.
DR IntAct; P02829; 382.
DR MINT; P02829; -.
DR STRING; 4932.YPL240C; -.
DR BindingDB; P02829; -.
DR ChEMBL; CHEMBL3536; -.
DR DrugCentral; P02829; -.
DR iPTMnet; P02829; -.
DR SWISS-2DPAGE; P02829; -.
DR MaxQB; P02829; -.
DR PaxDb; P02829; -.
DR PRIDE; P02829; -.
DR EnsemblFungi; YPL240C_mRNA; YPL240C; YPL240C.
DR GeneID; 855836; -.
DR KEGG; sce:YPL240C; -.
DR SGD; S000006161; HSP82.
DR VEuPathDB; FungiDB:YPL240C; -.
DR eggNOG; KOG0019; Eukaryota.
DR GeneTree; ENSGT01020000230401; -.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; P02829; -.
DR OMA; MRRMKEM; -.
DR BioCyc; YEAST:G3O-34126-MON; -.
DR BRENDA; 3.6.4.10; 984.
DR Reactome; R-SCE-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-SCE-203615; eNOS activation.
DR Reactome; R-SCE-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-SCE-3371511; HSF1 activation.
DR Reactome; R-SCE-3371571; HSF1-dependent transactivation.
DR Reactome; R-SCE-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-844456; The NLRP3 inflammasome.
DR Reactome; R-SCE-9009391; Extra-nuclear estrogen signaling.
DR SABIO-RK; P02829; -.
DR EvolutionaryTrace; P02829; -.
DR PHI-base; PHI:463; -.
DR PRO; PR:P02829; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P02829; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR GO; GO:0006458; P:'de novo' protein folding; IDA:SGD.
DR GO; GO:0000492; P:box C/D snoRNP assembly; IMP:SGD.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IDA:SGD.
DR GO; GO:0043248; P:proteasome assembly; IDA:SGD.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0051604; P:protein maturation; IMP:SGD.
DR GO; GO:0042026; P:protein refolding; IMP:SGD.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IPI:SGD.
DR GO; GO:0032204; P:regulation of telomere maintenance; IMP:CACAO.
DR GO; GO:0006970; P:response to osmotic stress; IMP:SGD.
DR GO; GO:0070482; P:response to oxygen levels; IC:ComplexPortal.
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 Phosphoprotein; Reference proteome; Repeat; Stress response.
FT CHAIN 1..709
FT /note="ATP-dependent molecular chaperone HSP82"
FT /id="PRO_0000062957"
FT REPEAT 221..225
FT /note="1"
FT /evidence="ECO:0000269|PubMed:10786835"
FT REPEAT 226..230
FT /note="2"
FT /evidence="ECO:0000269|PubMed:10786835"
FT REPEAT 231..235
FT /note="3"
FT /evidence="ECO:0000269|PubMed:10786835"
FT REPEAT 237..241
FT /note="4"
FT /evidence="ECO:0000269|PubMed:10786835"
FT REPEAT 250..254
FT /note="5"
FT /evidence="ECO:0000269|PubMed:10786835"
FT REGION 219..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..263
FT /note="5 X 5 AA repeats of [DE]-[DE]-[DE]-K-K; highly
FT charged region"
FT REGION 679..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 705..709
FT /note="TPR repeat-binding"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16625188,
FT ECO:0007744|PDB:2CG9"
FT BINDING 37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16625188,
FT ECO:0000269|PubMed:9230303, ECO:0007744|PDB:1AM1,
FT ECO:0007744|PDB:1AMW, ECO:0007744|PDB:2CG9,
FT ECO:0007744|PDB:2WEP"
FT BINDING 79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16625188,
FT ECO:0000269|PubMed:9230303, ECO:0007744|PDB:1AM1,
FT ECO:0007744|PDB:1AMW, ECO:0007744|PDB:2CG9,
FT ECO:0007744|PDB:2WEP"
FT BINDING 84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16625188,
FT ECO:0007744|PDB:2CG9"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16625188,
FT ECO:0007744|PDB:2CG9"
FT BINDING 98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16625188,
FT ECO:0007744|PDB:2CG9"
FT BINDING 99..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16625188,
FT ECO:0007744|PDB:2CG9"
FT BINDING 119..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16625188,
FT ECO:0000269|PubMed:9230303, ECO:0007744|PDB:1AM1,
FT ECO:0007744|PDB:1AMW, ECO:0007744|PDB:2CG9,
FT ECO:0007744|PDB:2WEP"
FT BINDING 171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16625188,
FT ECO:0007744|PDB:2CG9"
FT BINDING 380
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16625188,
FT ECO:0007744|PDB:2CG9"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15108"
FT MUTAGEN 22
FT /note="T->I: Induces a 6-fold increase in ATPase activity
FT and a reduced client protein activation activity, leading
FT to growth defect at high temperatures."
FT /evidence="ECO:0000269|PubMed:7791797"
FT MUTAGEN 41
FT /note="A->V: Causes a 98% reduction in ATPase activity and
FT a reduced client protein activation activity, leading to
FT growth defect at high temperatures."
FT /evidence="ECO:0000269|PubMed:7791797"
FT MUTAGEN 81
FT /note="G->S: Reduces client protein activation activity,
FT leading to growth defect at high temperatures."
FT /evidence="ECO:0000269|PubMed:7791797"
FT MUTAGEN 83
FT /note="G->D: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:18256191"
FT MUTAGEN 97
FT /note="A->I: Abolishes interaction with SBA1."
FT /evidence="ECO:0000269|PubMed:9632755"
FT MUTAGEN 101
FT /note="T->I: Causes a 90% reduction in ATPase activity and
FT a reduced client protein activation activity, leading to
FT growth defect at high temperatures."
FT /evidence="ECO:0000269|PubMed:7791797"
FT MUTAGEN 107
FT /note="A->N: Induces a 6-fold increase in ATPase activity."
FT /evidence="ECO:0000269|PubMed:10944121"
FT MUTAGEN 170
FT /note="G->D: Induces a total loss of function at 34 degrees
FT Celsius. Abolishes interaction with SBA1."
FT /evidence="ECO:0000269|PubMed:7791797"
FT MUTAGEN 313
FT /note="G->N,S: Reduces client protein activation activity,
FT leading to growth defect at high temperatures."
FT /evidence="ECO:0000269|PubMed:7791797,
FT ECO:0000269|PubMed:8248264"
FT MUTAGEN 349
FT /note="F->A,Q: Induces a loss of ATPase activity. Can be
FT reactivated by AHA1."
FT /evidence="ECO:0000269|PubMed:12667448"
FT MUTAGEN 380
FT /note="R->A: Induces a loss of ATPase activity."
FT /evidence="ECO:0000269|PubMed:12667448"
FT MUTAGEN 381
FT /note="E->K: Reduces client protein activation activity.
FT Resistant to ATPase activation by AHA1."
FT /evidence="ECO:0000269|PubMed:7791797"
FT MUTAGEN 384
FT /note="Q->A: Induces a loss of ATPase activity."
FT /evidence="ECO:0000269|PubMed:12667448"
FT MUTAGEN 387
FT /note="K->A: Decreases AHA1 binding affinity, but has no
FT effect on client protein activation activity."
FT /evidence="ECO:0000269|PubMed:14739935"
FT MUTAGEN 387
FT /note="K->D: Decreases AHA1 binding affinity and
FT substantially reduces client protein activation activity."
FT /evidence="ECO:0000269|PubMed:14739935"
FT MUTAGEN 431
FT /note="E->K: Specifically reduces the activation of the
FT exogenous ligand glucocorticoid receptor."
FT /evidence="ECO:0000269|PubMed:8248264"
FT MUTAGEN 485
FT /note="S->Y: Abolishes interaction with SBA1."
FT /evidence="ECO:0000269|PubMed:9632755"
FT MUTAGEN 525
FT /note="T->I: Abolishes interaction with SBA1. Reduces
FT client protein activation activity, leading to growth
FT defect at high temperatures."
FT /evidence="ECO:0000269|PubMed:8248264"
FT MUTAGEN 576
FT /note="A->T: Reduces client protein activation activity;
FT when associated with K-579."
FT /evidence="ECO:0000269|PubMed:8248264"
FT MUTAGEN 577
FT /note="A->C: Enhances ATPase activity and client protein
FT activation."
FT /evidence="ECO:0000269|PubMed:19696785"
FT MUTAGEN 577
FT /note="A->D: Reduces ATPase activity and client protein
FT activation."
FT /evidence="ECO:0000269|PubMed:19696785"
FT MUTAGEN 577
FT /note="A->I: Enhances homodimerization, ATPase activity and
FT client protein activation."
FT /evidence="ECO:0000269|PubMed:19696785"
FT MUTAGEN 577
FT /note="A->N: Reduces homodimerization, ATPase activity and
FT client protein activation."
FT /evidence="ECO:0000269|PubMed:19696785"
FT MUTAGEN 579
FT /note="R->K: Reduces client protein activation activity;
FT when associated with T-576."
FT /evidence="ECO:0000269|PubMed:8248264"
FT MUTAGEN 587
FT /note="A->T: No effect on ATPase activity. Reduces client
FT protein activation activity, leading to growth defect at
FT high temperatures."
FT /evidence="ECO:0000269|PubMed:7791797"
FT CONFLICT 481
FT /note="A -> S (in Ref. 27)"
FT /evidence="ECO:0000305"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:2IWX"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:2IWX"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:4ASB"
FT HELIX 29..48
FT /evidence="ECO:0007829|PDB:2IWX"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:2IWX"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:2IWX"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:2IWX"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:2IWX"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:2IWX"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:2IWX"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:2BRC"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:2IWX"
FT HELIX 114..120
FT /evidence="ECO:0007829|PDB:2IWX"
FT HELIX 123..129
FT /evidence="ECO:0007829|PDB:2IWX"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:2IWX"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:2IWX"
FT STRAND 152..160
FT /evidence="ECO:0007829|PDB:2IWX"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:2IWX"
FT STRAND 168..177
FT /evidence="ECO:0007829|PDB:2IWX"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:2IWX"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:2IWX"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:2AKP"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:2IWX"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:1USU"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:1USU"
FT HELIX 286..297
FT /evidence="ECO:0007829|PDB:1USU"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:1USU"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:1USU"
FT STRAND 317..323
FT /evidence="ECO:0007829|PDB:1USU"
FT TURN 329..332
FT /evidence="ECO:0007829|PDB:1USU"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:2CG9"
FT STRAND 341..345
FT /evidence="ECO:0007829|PDB:1USU"
FT STRAND 348..352
FT /evidence="ECO:0007829|PDB:1USU"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:1HK7"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:1USU"
FT STRAND 366..373
FT /evidence="ECO:0007829|PDB:1USU"
FT HELIX 380..383
FT /evidence="ECO:0007829|PDB:1HK7"
FT HELIX 387..408
FT /evidence="ECO:0007829|PDB:1USU"
FT HELIX 411..431
FT /evidence="ECO:0007829|PDB:1USU"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:1USU"
FT HELIX 436..440
FT /evidence="ECO:0007829|PDB:1USU"
FT STRAND 444..447
FT /evidence="ECO:0007829|PDB:1USU"
FT STRAND 450..456
FT /evidence="ECO:0007829|PDB:1USU"
FT HELIX 457..462
FT /evidence="ECO:0007829|PDB:1USU"
FT STRAND 470..475
FT /evidence="ECO:0007829|PDB:1USU"
FT HELIX 479..483
FT /evidence="ECO:0007829|PDB:1USU"
FT HELIX 488..493
FT /evidence="ECO:0007829|PDB:1USU"
FT STRAND 498..501
FT /evidence="ECO:0007829|PDB:1USU"
FT HELIX 504..513
FT /evidence="ECO:0007829|PDB:1USU"
FT STRAND 519..523
FT /evidence="ECO:0007829|PDB:1USU"
FT TURN 524..526
FT /evidence="ECO:0007829|PDB:1HK7"
FT STRAND 530..533
FT /evidence="ECO:0007829|PDB:2CGE"
FT HELIX 535..558
FT /evidence="ECO:0007829|PDB:2CGE"
FT STRAND 563..567
FT /evidence="ECO:0007829|PDB:2CGE"
FT STRAND 573..580
FT /evidence="ECO:0007829|PDB:2CGE"
FT STRAND 582..584
FT /evidence="ECO:0007829|PDB:2CGE"
FT HELIX 587..597
FT /evidence="ECO:0007829|PDB:2CGE"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:2CGE"
FT STRAND 611..615
FT /evidence="ECO:0007829|PDB:2CGE"
FT HELIX 620..629
FT /evidence="ECO:0007829|PDB:2CGE"
FT TURN 630..632
FT /evidence="ECO:0007829|PDB:2CGE"
FT HELIX 633..635
FT /evidence="ECO:0007829|PDB:2CGE"
FT HELIX 637..653
FT /evidence="ECO:0007829|PDB:2CGE"
FT HELIX 661..676
FT /evidence="ECO:0007829|PDB:2CGE"
SQ SEQUENCE 709 AA; 81406 MW; D7C35676D668FB63 CRC64;
MASETFEFQA EITQLMSLII NTVYSNKEIF LRELISNASD ALDKIRYKSL SDPKQLETEP
DLFIRITPKP EQKVLEIRDS GIGMTKAELI NNLGTIAKSG TKAFMEALSA GADVSMIGQF
GVGFYSLFLV ADRVQVISKS NDDEQYIWES NAGGSFTVTL DEVNERIGRG TILRLFLKDD
QLEYLEEKRI KEVIKRHSEF VAYPIQLVVT KEVEKEVPIP EEEKKDEEKK DEEKKDEDDK
KPKLEEVDEE EEKKPKTKKV KEEVQEIEEL NKTKPLWTRN PSDITQEEYN AFYKSISNDW
EDPLYVKHFS VEGQLEFRAI LFIPKRAPFD LFESKKKKNN IKLYVRRVFI TDEAEDLIPE
WLSFVKGVVD SEDLPLNLSR EMLQQNKIMK VIRKNIVKKL IEAFNEIAED SEQFEKFYSA
FSKNIKLGVH EDTQNRAALA KLLRYNSTKS VDELTSLTDY VTRMPEHQKN IYYITGESLK
AVEKSPFLDA LKAKNFEVLF LTDPIDEYAF TQLKEFEGKT LVDITKDFEL EETDEEKAER
EKEIKEYEPL TKALKEILGD QVEKVVVSYK LLDAPAAIRT GQFGWSANME RIMKAQALRD
SSMSSYMSSK KTFEISPKSP IIKELKKRVD EGGAQDKTVK DLTKLLYETA LLTSGFSLDE
PTSFASRINR LISLGLNIDE DEETETAPEA STAAPVEEVP ADTEMEEVD
