CH60_CAEEL
ID CH60_CAEEL Reviewed; 568 AA.
AC P50140; Q965Q0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Chaperonin homolog Hsp-60, mitochondrial;
DE AltName: Full=Heat shock protein 60;
DE Short=HSP-60;
DE Flags: Precursor;
GN Name=hsp-60; Synonyms=hsp60; ORFNames=Y22D7AL.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CB1392;
RA Musso G., la Volpe A.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP INDUCTION BY MITOCHONDRIAL STRESS.
RX PubMed=26212459; DOI=10.1016/j.molcel.2015.06.027;
RA Labbadia J., Morimoto R.I.;
RT "Repression of the heat shock response is a programmed event at the onset
RT of reproduction.";
RL Mol. Cell 59:639-650(2015).
CC -!- FUNCTION: Implicated in mitochondrial protein import and macromolecular
CC assembly. May facilitate the correct folding of imported proteins. May
CC also prevent misfolding and promote the refolding and proper assembly
CC of unfolded polypeptides generated under stress conditions in the
CC mitochondrial matrix (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- INDUCTION: By mitochondrial stress. {ECO:0000269|PubMed:26212459}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR EMBL; L36035; AAA28077.1; -; mRNA.
DR EMBL; FO081783; CCD73746.1; -; Genomic_DNA.
DR RefSeq; NP_497429.1; NM_065028.7.
DR AlphaFoldDB; P50140; -.
DR SMR; P50140; -.
DR BioGRID; 40572; 45.
DR IntAct; P50140; 3.
DR STRING; 6239.Y22D7AL.5a.2; -.
DR World-2DPAGE; 0011:P50140; -.
DR EPD; P50140; -.
DR PaxDb; P50140; -.
DR PeptideAtlas; P50140; -.
DR PRIDE; P50140; -.
DR EnsemblMetazoa; Y22D7AL.5a.1; Y22D7AL.5a.1; WBGene00002025.
DR EnsemblMetazoa; Y22D7AL.5a.2; Y22D7AL.5a.2; WBGene00002025.
DR GeneID; 175316; -.
DR KEGG; cel:CELE_Y22D7AL.5; -.
DR CTD; 175316; -.
DR WormBase; Y22D7AL.5a; CE27244; WBGene00002025; hsp-60.
DR eggNOG; KOG0356; Eukaryota.
DR HOGENOM; CLU_016503_3_0_1; -.
DR InParanoid; P50140; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 415781at2759; -.
DR PhylomeDB; P50140; -.
DR PRO; PR:P50140; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00002025; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; P50140; baseline and differential.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0034514; P:mitochondrial unfolded protein response; IMP:WormBase.
DR GO; GO:0007005; P:mitochondrion organization; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
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: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; 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 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..568
FT /note="Chaperonin homolog Hsp-60, mitochondrial"
FT /id="PRO_0000005030"
FT CONFLICT 111
FT /note="A -> T (in Ref. 1; AAA28077)"
FT /evidence="ECO:0000305"
FT CONFLICT 121..125
FT /note="SIRQG -> RHSSR (in Ref. 1; AAA28077)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="E -> Q (in Ref. 1; AAA28077)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="T -> A (in Ref. 1; AAA28077)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="T -> S (in Ref. 1; AAA28077)"
FT /evidence="ECO:0000305"
FT CONFLICT 319..325
FT /note="DSNLIKI -> ETLDLRL (in Ref. 1; AAA28077)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="H -> E (in Ref. 1; AAA28077)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="Q -> R (in Ref. 1; AAA28077)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 568 AA; 60101 MW; 814E3D209961E8B1 CRC64;
MLRLARKGLQ TAVVRSYAKD VKFGAEGRQA MLVGVNLLAD AVSVTMGPKG RNVIIEQSWG
SPKITKDGVT VAKSIDLKDK YQNLGAKLIQ DVANKANEEA GDGTTCATVL ARAIAKEGFE
SIRQGGNAVE IRRGVMNAVE VVVAELKKIS KKVTTPEEIA QVATISANGD TVVGNLISDA
MKKVGTTGVI TVKDGKTLND ELELIEGMKF DRGYISPYFI TSAKGAKVEY EKALVLLSEK
KISQVQDIVP ALELANKLRR PLVIIAEDVD GEALTTLVLN RLKVGLQVVA IKAPGFGDNR
KNTLKDMGIA TGATIFGDDS NLIKIEDITA NDLGEVDEVT ITKDDTLLLR GRGDQTEIEK
RIEHITDEIE QSTSDYEKEK LNERLAKLSK GVAVLKIGGG SEVEVGEKKD RVTDALCATR
AAVEEGIVPG GGVALLRSLT ALKNYKAANE DQQIGVNIVK KALTQPIATI VKNAGLEPSS
IIDEVTGNSN TSYGYDALNG KFVDMFEAGI IDPTKVVRTA LQDASGVASL LATTECVVTE
IPKEEAVGGP AGGMGGMGGM GGMGGMGF
