HSP60_YEAST
ID HSP60_YEAST Reviewed; 572 AA.
AC P19882; D6VYQ6;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Heat shock protein 60, mitochondrial;
DE AltName: Full=CPN60;
DE AltName: Full=P66;
DE AltName: Full=Stimulator factor I 66 kDa component;
DE Flags: Precursor;
GN Name=HSP60; Synonyms=MIF4; OrderedLocusNames=YLR259C; ORFNames=L8479.10;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=2575559; DOI=10.1016/0378-1119(89)90503-9;
RA Johnson R.B., Fearon K., Mason T., Jindal S.;
RT "Cloning and characterization of the yeast chaperonin HSP60 gene.";
RL Gene 84:295-302(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 200060 / W303;
RX PubMed=2563898; DOI=10.1038/337655a0;
RA Reading D.S., Hallberg R.L., Myers A.M.;
RT "Characterization of the yeast HSP60 gene coding for a mitochondrial
RT assembly factor.";
RL Nature 337:655-659(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [4]
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 [5]
RP PARTIAL NUCLEOTIDE SEQUENCE.
RX PubMed=1408806; DOI=10.1093/nar/20.18.4913;
RA Smiley J.K., Brown W.C., Campbell J.L.;
RT "The 66 kDa component of yeast SFI, stimulatory factor I, is hsp60.";
RL Nucleic Acids Res. 20:4913-4918(1992).
RN [6]
RP PROTEIN SEQUENCE OF 28-34; 101-116; 148-153; 443-450 AND 507-514, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 201238 / W303-1B;
RX PubMed=11502169; DOI=10.1021/bi010277r;
RA Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S.,
RA Schmitter J.-M.;
RT "Yeast mitochondrial dehydrogenases are associated in a supramolecular
RT complex.";
RL Biochemistry 40:9758-9769(2001).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT phosphorylation in assembly of the ATP synthase.";
RL Mol. Cell. Proteomics 6:1896-1906(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: May participate in assembly and/or disassembly of proteins
CC imported into the mitochondrion. HSP60 are ATPases and have affinity
CC for unfolded proteins.
CC -!- INTERACTION:
CC P19882; P07276: RAD2; NbExp=2; IntAct=EBI-8586, EBI-14757;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:11502169}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR EMBL; M33301; AAA34690.1; -; Genomic_DNA.
DR EMBL; U17244; AAB67380.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09572.1; -; Genomic_DNA.
DR PIR; JQ0157; JQ0157.
DR RefSeq; NP_013360.1; NM_001182146.1.
DR AlphaFoldDB; P19882; -.
DR SMR; P19882; -.
DR BioGRID; 31527; 345.
DR DIP; DIP-7648N; -.
DR IntAct; P19882; 247.
DR MINT; P19882; -.
DR STRING; 4932.YLR259C; -.
DR CarbonylDB; P19882; -.
DR iPTMnet; P19882; -.
DR SWISS-2DPAGE; P19882; -.
DR UCD-2DPAGE; P19882; -.
DR MaxQB; P19882; -.
DR PaxDb; P19882; -.
DR PRIDE; P19882; -.
DR EnsemblFungi; YLR259C_mRNA; YLR259C; YLR259C.
DR GeneID; 850963; -.
DR KEGG; sce:YLR259C; -.
DR SGD; S000004249; HSP60.
DR VEuPathDB; FungiDB:YLR259C; -.
DR eggNOG; KOG0356; Eukaryota.
DR GeneTree; ENSGT00390000005727; -.
DR HOGENOM; CLU_016503_3_0_1; -.
DR InParanoid; P19882; -.
DR OMA; TDTDKME; -.
DR BioCyc; YEAST:G3O-32361-MON; -.
DR Reactome; R-SCE-1268020; Mitochondrial protein import.
DR PRO; PR:P19882; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P19882; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0051087; F:chaperone binding; IPI:SGD.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
DR GO; GO:0051082; F:unfolded protein binding; IMP:SGD.
DR GO; GO:0006458; P:'de novo' protein folding; IMP:SGD.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IBA:GO_Central.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IMP:SGD.
DR GO; GO:0034514; P:mitochondrial unfolded protein response; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IMP:SGD.
DR GO; GO:0051604; P:protein maturation; IMP:SGD.
DR GO; GO:0042026; P:protein refolding; IDA:SGD.
DR GO; GO:0050821; P:protein stabilization; IMP:SGD.
DR CDD; cd03344; GroEL; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR HAMAP; MF_00600; CH60; 1.
DR InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR InterPro; IPR001844; Cpn60/GroEL.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00298; CHAPERONIN60.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02348; GroEL; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Direct protein sequencing; Mitochondrion;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Stress response;
KW Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..572
FT /note="Heat shock protein 60, mitochondrial"
FT /id="PRO_0000005044"
FT MOD_RES 102
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17761666"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 572 AA; 60752 MW; 279DC3AF5A2B0A3E CRC64;
MLRSSVVRSR ATLRPLLRRA YSSHKELKFG VEGRASLLKG VETLAEAVAA TLGPKGRNVL
IEQPFGPPKI TKDGVTVAKS IVLKDKFENM GAKLLQEVAS KTNEAAGDGT TSATVLGRAI
FTESVKNVAA GCNPMDLRRG SQVAVEKVIE FLSANKKEIT TSEEIAQVAT ISANGDSHVG
KLLASAMEKV GKEGVITIRE GRTLEDELEV TEGMRFDRGF ISPYFITDPK SSKVEFEKPL
LLLSEKKISS IQDILPALEI SNQSRRPLLI IAEDVDGEAL AACILNKLRG QVKVCAVKAP
GFGDNRKNTI GDIAVLTGGT VFTEELDLKP EQCTIENLGS CDSITVTKED TVILNGSGPK
EAIQERIEQI KGSIDITTTN SYEKEKLQER LAKLSGGVAV IRVGGASEVE VGEKKDRYDD
ALNATRAAVE EGILPGGGTA LVKASRVLDE VVVDNFDQKL GVDIIRKAIT RPAKQIIENA
GEEGSVIIGK LIDEYGDDFA KGYDASKSEY TDMLATGIID PFKVVRSGLV DASGVASLLA
TTEVAIVDAP EPPAAAGAGG MPGGMPGMPG MM
