ID   CH62_CUCMA              Reviewed;         575 AA.
AC   Q05046;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Chaperonin CPN60-2, mitochondrial;
DE   AltName: Full=HSP60-2;
DE   Flags: Precursor;
GN   Name=CPN60-2;
OS   Cucurbita maxima (Pumpkin) (Winter squash).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX   NCBI_TaxID=3661;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Cotyledon;
RX   PubMed=1356771; DOI=10.1111/j.1432-1033.1992.tb17309.x;
RA   Tsugeki R., Mori H., Nishimura M.;
RT   "Purification, cDNA cloning and Northern-blot analysis of mitochondrial
RT   chaperonin 60 from pumpkin cotyledons.";
RL   Eur. J. Biochem. 209:453-458(1992).
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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- INDUCTION: By heat shock.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR   EMBL; X70868; CAA50218.1; -; mRNA.
DR   AlphaFoldDB; Q05046; -.
DR   SMR; Q05046; -.
DR   PRIDE; Q05046; -.
DR   OrthoDB; 415781at2759; -.
DR   Proteomes; UP000504608; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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: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   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Direct protein sequencing; Mitochondrion;
KW   Nucleotide-binding; Reference proteome; Stress response; Transit peptide.
FT   TRANSIT         1..32
FT                   /note="Mitochondrion"
FT   CHAIN           33..575
FT                   /note="Chaperonin CPN60-2, mitochondrial"
FT                   /id="PRO_0000005012"
SQ   SEQUENCE   575 AA;  61130 MW;  C39D5C541A86FA66 CRC64;
     MHRFASGLAS KARLARKGAN QIASRSSWSR NYAAKDVKFG VEARGLMLKG VEDLADAVKV
     TMGPKGRNVV IEQSYGAPKV TKDGVTVAKS IEFKDKVKNV GASLVKQVAN ATNDVAGDGT
     TCATILTRAI FTEGCKSVAA GMNAMDLRRG ISMAVDSVVT NLKSRARMIS TSEEIAQVGT
     ISANGEREIG ELIAKAMEKV GKEGVITISD GKTLFNELEV VEGMKLDRGY ISPYFITNQK
     NQKCELDDPL ILIHEKKISS INSVVKVLEL ALKRQRPLLI VSEDVESDAL ATLILNKLRA
     GIKVCAIKAP GFGENRKAGL HDLAVLTGGQ LITEELGMNL EKVDLDMLGS CKKITISKDD
     TVILDGAGDK KSIEERCEQI RSAIELSTSD YDKEKLQERL AKLSGGVAVL KIGGASEAEV
     GEKKDRVTDA LNATKAAVEE GIVPGGGVAL LYASKELDKL STANFDQKIG VQIIQNALKT
     PVHTIASNAG VEGAVVVGKL LEQDNPDLGY DAAKGEYVDM IKAGIIDPLK VIRTALVDAA
     SVSSLMTTTE AIVVELPKDE KEVPAMGGGM GGMDY