ID   CH60_BRANA              Reviewed;         587 AA.
AC   P35480;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Chaperonin CPN60, mitochondrial;
DE   Flags: Precursor;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seed;
RX   PubMed=7913239; DOI=10.1104/pp.105.1.451;
RA   Cole K.P., Blakeley S.D., Dennis D.T.;
RT   "Isolation of a full-length cDNA encoding Brassica napus mitochondrial
RT   chaperonin-60.";
RL   Plant Physiol. 105:451-451(1994).
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   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR   EMBL; Z27165; CAA81689.1; -; mRNA.
DR   PIR; S38634; S38634.
DR   RefSeq; NP_001302985.1; NM_001316056.1.
DR   AlphaFoldDB; P35480; -.
DR   SMR; P35480; -.
DR   PRIDE; P35480; -.
DR   GeneID; 106437789; -.
DR   KEGG; bna:106437789; -.
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   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Mitochondrion; Nucleotide-binding; Stress response;
KW   Transit peptide.
FT   TRANSIT         1..32
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..587
FT                   /note="Chaperonin CPN60, mitochondrial"
FT                   /id="PRO_0000005010"
SQ   SEQUENCE   587 AA;  62355 MW;  09AAC1691E31E097 CRC64;
     MYRLISSIAS KARVARNCTS QIGSRLSSTR NYAAKDIRFG VEGRALMLRG VEELADAVKV
     TIPPKGRNVI IEQSWGAPKV TKDGVTVAKS IEFKDRVKNV GASLVKQVAN RPTQLNRCLG
     DGTTCATVLT RAIFTEGCKS VAAGMNAMDL RRGIKLAVDT VVTKLKSRAR MISTSEEIAQ
     VGTISANGDR ELVTDCKAME SVGKEGVITI QDGKTLFNEL EVVEGMKIDR GYISPYFITN
     QKNQKCELED PLILIHEKKI SNLNSMVKVL ELALKSQRSL LIVAADLESD ALAVLILNKL
     RAGIKVCAVK APGFGENRKA NMHDLATLTG AQVITEELGM NLEKIDLSML GNCKKITVSK
     DDTVFLGWGA GDKKAIGERC EQIRSMVEAS ESDYDKEKLQ ERLAKLSGGV AVLKIGGASE
     SEVGEKKDRV TDALNATKAA VEEGIVPGGG VALLYASKEL DKLSTANFDH KIGVQIIQNA
     LKTPVYTIAS NAGVEGAVIV GKLLESDNPD LGYDAAKGEY VDMVKSGIID PVKVIRTALV
     DAASVSSLLT TTEAVVTEIP TKEDASPAMG GGGGGMGGMG GMGGMGF