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 02-SEP-2026, entry version 255. 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; DOI=10.1038/387s103; 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=14; 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=9; 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=3; IntAct=EBI-8659, EBI-8603; CC P02829; P32589: SSE1; NbExp=3; IntAct=EBI-8659, EBI-8648; CC P02829; P15705: STI1; NbExp=19; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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=271-530. 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 PDB; 8OXU; X-ray; 2.94 A; A/B/C/D=439-679. DR PDB; 9Q8O; X-ray; 2.10 A; A=273-529. DR AlphaFoldDB; P02829; -. DR BMRB; P02829; -. DR MDposit; P02829; -. DR MDRepo; P02829; -. DR SMR; P02829; -. DR BioGRID; 35923; 1887. DR ComplexPortal; CPX-1276; HMC complex. DR DIP; DIP-2262N; -. DR FunCoup; P02829; 1767. DR IntAct; P02829; 394. DR MINT; P02829; -. DR STRING; 4932.YPL240C; -. DR BindingDB; P02829; -. DR ChEMBL; CHEMBL3536; -. DR DrugCentral; P02829; -. DR iPTMnet; P02829; -. DR PaxDb; 4932-YPL240C; -. DR PeptideAtlas; P02829; -. DR EnsemblFungi; YPL240C_mRNA; YPL240C; YPL240C. DR GeneID; 855836; -. DR KEGG; sce:YPL240C; -. DR AGR; SGD:S000006161; -. DR SGD; S000006161; HSP82. DR VEuPathDB; FungiDB:YPL240C; -. DR eggNOG; KOG0019; Eukaryota. DR HOGENOM; CLU_006684_1_3_1; -. DR InParanoid; P02829; -. DR OMA; MRRMKEM; -. DR OrthoDB; 28737at2759; -. DR BioCyc; YEAST:G3O-34126-MONOMER; -. DR BRENDA; 3.6.4.10; 984. DR BRENDA; 5.6.1.10; 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-8939211; ESR-mediated signaling. DR Reactome; R-SCE-9009391; Extra-nuclear estrogen signaling. DR SABIO-RK; P02829; -. DR BioGRID-ORCS; 855836; 0 hits in 10 CRISPR screens. 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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. 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:0070585; P:protein localization to mitochondrion; IPI:SGD. DR GO; GO:0051604; P:protein maturation; IMP:SGD. DR GO; GO:0042026; P:protein refolding; IMP: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; NAS:ComplexPortal. DR CDD; cd16927; HATPase_Hsp90-like; 1. DR FunFam; 1.20.120.790:FF:000001; Heat shock protein 90 alpha; 1. DR FunFam; 3.30.230.80:FF:000001; Heat shock protein 90 alpha; 1. DR FunFam; 3.40.50.11260:FF:000001; Heat shock protein 90 alpha; 1. DR FunFam; 3.30.565.10:FF:000001; Heat shock protein HSP 90-alpha; 1. DR Gene3D; 3.30.230.80; -; 1. DR Gene3D; 3.40.50.11260; -; 1. DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR HAMAP; MF_00505; HSP90; 1. DR InterPro; IPR036890; HATPase_C_sf. DR InterPro; IPR003594; HATPase_dom. 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_Su5_D2-typ_SF. DR NCBIfam; NF003555; PRK05218.1; 1. DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1. DR Pfam; PF13589; HATPase_c_3; 1. DR Pfam; PF00183; HSP90; 1. DR PIRSF; PIRSF002583; Hsp90; 1. DR PRINTS; PR00775; HEATSHOCK90. DR SMART; SM00387; HATPase_c; 1. DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. DR PROSITE; PS00298; HSP90; 1. 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 PDBsum; 8OXU; -. DR PDBsum; 9Q8O; -. 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 COMPBIAS 219..245 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 687..698 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 699..709 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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..90 FT /evidence="ECO:0007829|PDB:2IWX" FT HELIX 91..95 FT /evidence="ECO:0007829|PDB:2IWX" 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 HELIX 165..167 FT /evidence="ECO:0007829|PDB:2BRC" 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 HELIX 337..339 FT /evidence="ECO:0007829|PDB:2CGE" 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 536..546 FT /evidence="ECO:0007829|PDB:8OXU" FT HELIX 548..558 FT /evidence="ECO:0007829|PDB:8OXU" FT HELIX 559..561 FT /evidence="ECO:0007829|PDB:8OXU" FT STRAND 563..567 FT /evidence="ECO:0007829|PDB:8OXU" FT STRAND 573..580 FT /evidence="ECO:0007829|PDB:8OXU" FT STRAND 582..584 FT /evidence="ECO:0007829|PDB:2CGE" FT HELIX 587..595 FT /evidence="ECO:0007829|PDB:8OXU" FT STRAND 600..602 FT /evidence="ECO:0007829|PDB:2CGE" FT STRAND 611..615 FT /evidence="ECO:0007829|PDB:8OXU" FT HELIX 620..630 FT /evidence="ECO:0007829|PDB:8OXU" FT TURN 631..635 FT /evidence="ECO:0007829|PDB:8OXU" FT HELIX 637..653 FT /evidence="ECO:0007829|PDB:8OXU" FT HELIX 661..674 FT /evidence="ECO:0007829|PDB:8OXU" 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 //