CH10_YEAST
ID CH10_YEAST Reviewed; 106 AA.
AC P38910; D6W286; E9P935;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=10 kDa heat shock protein, mitochondrial;
DE Short=HSP10;
DE AltName: Full=10 kDa chaperonin;
GN Name=HSP10; Synonyms=CPN10; OrderedLocusNames=YOR020C; ORFNames=OR26.10;
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].
RX PubMed=7903252; DOI=10.1016/0014-5793(93)80419-u;
RA Rospert S., Junne T., Glick B.S., Schatz G.;
RT "Cloning and disruption of the gene encoding yeast mitochondrial chaperonin
RT 10, the homolog of E. coli groES.";
RL FEBS Lett. 335:358-360(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7913473; DOI=10.1083/jcb.126.2.305;
RA Hoehfeld J., Hartl F.U.;
RT "Role of the chaperonin cofactor Hsp10 in protein folding and sorting in
RT yeast mitochondria.";
RL J. Cell Biol. 126:305-315(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 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 [6]
RP PROTEIN SEQUENCE OF 10-24; 29-35 AND 63-78.
RX PubMed=7902576; DOI=10.1073/pnas.90.23.10967;
RA Rospert S., Glick B.S., Jenoe P., Schatz G., Todd M.J., Lorimer G.H.,
RA Viitanen P.V.;
RT "Identification and functional analysis of chaperonin 10, the groES homolog
RT from yeast mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:10967-10971(1993).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, 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).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Eukaryotic CPN10 homolog which is essential for mitochondrial
CC protein biogenesis, together with CPN60. Binds to CPN60 in the presence
CC of Mg-ATP and suppresses the ATPase activity of the latter.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: Present with 149 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000305}.
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DR EMBL; X76853; CAA54185.1; -; Genomic_DNA.
DR EMBL; X75754; CAA53382.1; -; Genomic_DNA.
DR EMBL; X87331; CAA60769.1; -; Genomic_DNA.
DR EMBL; Z74928; CAA99210.1; -; Genomic_DNA.
DR EMBL; AY693222; AAT93241.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10802.1; -; Genomic_DNA.
DR PIR; S39463; S39463.
DR RefSeq; NP_014663.1; NM_001183439.1.
DR AlphaFoldDB; P38910; -.
DR SMR; P38910; -.
DR BioGRID; 34424; 506.
DR DIP; DIP-1483N; -.
DR IntAct; P38910; 9.
DR MINT; P38910; -.
DR STRING; 4932.YOR020C; -.
DR iPTMnet; P38910; -.
DR MaxQB; P38910; -.
DR PaxDb; P38910; -.
DR PRIDE; P38910; -.
DR TopDownProteomics; P38910; -.
DR EnsemblFungi; YOR020C_mRNA; YOR020C; YOR020C.
DR GeneID; 854185; -.
DR KEGG; sce:YOR020C; -.
DR SGD; S000005546; HSP10.
DR VEuPathDB; FungiDB:YOR020C; -.
DR eggNOG; KOG1641; Eukaryota.
DR GeneTree; ENSGT00390000006350; -.
DR HOGENOM; CLU_132825_0_0_1; -.
DR InParanoid; P38910; -.
DR OMA; EVKYSGE; -.
DR BioCyc; YEAST:G3O-33568-MON; -.
DR PRO; PR:P38910; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P38910; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IPI:SGD.
DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IMP:SGD.
DR GO; GO:0006457; P:protein folding; IDA:SGD.
DR GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IMP:SGD.
DR GO; GO:0042026; P:protein refolding; IDA:SGD.
DR CDD; cd00320; cpn10; 1.
DR Gene3D; 2.30.33.40; -; 1.
DR HAMAP; MF_00580; CH10; 1.
DR InterPro; IPR020818; Chaperonin_GroES.
DR InterPro; IPR037124; Chaperonin_GroES_sf.
DR InterPro; IPR018369; Chaprnonin_Cpn10_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR PANTHER; PTHR10772; PTHR10772; 1.
DR Pfam; PF00166; Cpn10; 1.
DR PRINTS; PR00297; CHAPERONIN10.
DR SMART; SM00883; Cpn10; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR PROSITE; PS00681; CHAPERONINS_CPN10; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Direct protein sequencing; Mitochondrion;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..106
FT /note="10 kDa heat shock protein, mitochondrial"
FT /id="PRO_0000174922"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 82
FT /note="T -> S (in Ref. 5; AAT93241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 106 AA; 11372 MW; 0453269D502C05E8 CRC64;
MSTLLKSAKS IVPLMDRVLV QRIKAQAKTA SGLYLPEKNV EKLNQAEVVA VGPGFTDANG
NKVVPQVKVG DQVLIPQFGG STIKLGNDDE VILFRDAEIL AKIAKD
