HSP60_SCHPO
ID HSP60_SCHPO Reviewed; 582 AA.
AC Q09864; Q10285;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Heat shock protein 60, mitochondrial;
DE Short=HSP60;
DE Flags: Precursor;
GN Name=hsp60; Synonyms=mcp60; ORFNames=SPAC12G12.04;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / HM123;
RX PubMed=8566770; DOI=10.1016/0378-1119(96)82966-0;
RA Yoshida H., Yanagi H., Yura T.;
RT "Cloning and characterization of the mitochondrial HSP60-encoding gene of
RT Schizosaccharomyces pombe.";
RL Gene 167:163-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-92, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(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 -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR EMBL; CU329670; CAA91499.1; -; Genomic_DNA.
DR EMBL; D50609; BAA09171.1; -; Genomic_DNA.
DR PIR; S62535; S62535.
DR PIR; T43369; T43369.
DR RefSeq; NP_592894.1; NM_001018294.2.
DR AlphaFoldDB; Q09864; -.
DR SMR; Q09864; -.
DR BioGRID; 279563; 10.
DR IntAct; Q09864; 2.
DR MINT; Q09864; -.
DR STRING; 4896.SPAC12G12.04.1; -.
DR iPTMnet; Q09864; -.
DR MaxQB; Q09864; -.
DR PaxDb; Q09864; -.
DR PRIDE; Q09864; -.
DR EnsemblFungi; SPAC12G12.04.1; SPAC12G12.04.1:pep; SPAC12G12.04.
DR GeneID; 2543131; -.
DR KEGG; spo:SPAC12G12.04; -.
DR PomBase; SPAC12G12.04; -.
DR VEuPathDB; FungiDB:SPAC12G12.04; -.
DR eggNOG; KOG0356; Eukaryota.
DR HOGENOM; CLU_016503_3_0_1; -.
DR InParanoid; Q09864; -.
DR OMA; TDTDKME; -.
DR PhylomeDB; Q09864; -.
DR Reactome; R-SPO-1268020; Mitochondrial protein import.
DR PRO; PR:Q09864; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:PomBase.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:PomBase.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:PomBase.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISS:PomBase.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; ISO:PomBase.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
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; 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.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Mitochondrion; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..582
FT /note="Heat shock protein 60, mitochondrial"
FT /id="PRO_0000005043"
FT REGION 561..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 392
FT /note="Y -> S (in Ref. 1; BAA09171)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="G -> A (in Ref. 1; BAA09171)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 582 AA; 62167 MW; E5434436A98AFDC5 CRC64;
MVSFLSSSVS RLPLRIAGRR IPGRFAVPQV RTYAKDLKFG VDARASLLTG VDTLARAVSV
TLGPKGRNVL IDQPFGSPKI TKDGVTVARS VSLKDKFENL GARLVQDVAS KTNEVAGDGT
TTATVLTRAI FSETVRNVAA GCNPMDLRRG IQLAVDNVVE FLQANKRDIT TSEEISQVAT
ISANGDTHIG ELLAKAMERV GKEGVITVKE GRTISDELEV TEGMKFDRGY ISPYFITDVK
SQKVEFENPL ILLSEKKVSA VQDILPSLEL AAQQRRPLVI IAEDVDGEAL AACILNKLRG
QLQVVAIKAP GFGDNRRNML GDLAVLTDSA VFNDEIDVSI EKAQPHHLGS CGSVTVTKED
TIIMKGAGDH VKVNDRCEQI RGVMADPNLT EYEKEKLQER LAKLSGGIAV IKVGGSSEVE
VNEKKDRIVD ALNAVKAAVS EGVLPGAGTS FVKASLRLGD IPTNNFDQKL GVEIVRKAIT
RPAQTILENA GLEGNLIVGK LKELYGKEFN IGYDIAKDRF VDLNEIGVLD PLKVVRTGLV
DASGVASLMG TTECAIVDAP EESKAPAGPP GMGGMGGMPG MM
