CH60_TRYCR
ID CH60_TRYCR Reviewed; 562 AA.
AC Q95046; Q27795;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Chaperonin HSP60, mitochondrial;
DE Short=Protein Cpn60;
DE AltName: Full=Heat shock protein 60;
DE AltName: Full=groEL protein;
DE Flags: Precursor;
GN Name=HSP60;
OS Trypanosoma cruzi.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=5693;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CL;
RX PubMed=8096324; DOI=10.1016/0166-6851(93)90087-e;
RA Giambiagi-De Marval M., Gottesdiener K., Rondinelli E.,
RA Van der Ploeg L.H.T.;
RT "Predicted amino acid sequence and genomic organization of Trypanosoma
RT cruzi hsp 60 genes.";
RL Mol. Biochem. Parasitol. 58:25-32(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=PBOL;
RX PubMed=7739666; DOI=10.1016/0166-6851(94)90165-1;
RA Sullivan M.A., Olson C.L., Winquist A.G., Engman D.M.;
RT "Expression and localization of Trypanosoma cruzi hsp60.";
RL Mol. Biochem. Parasitol. 68:197-208(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 matrix.
CC -!- INDUCTION: By heat shock. There are multiple isoforms that, with
CC increasing temperature, shift in relative abundance from the more basic
CC to the more acidic.
CC -!- MISCELLANEOUS: Exists in at least five isoforms that are not related by
CC a simple post-translational modification and may represent the products
CC of different genes.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR EMBL; X67473; CAA47819.1; -; Genomic_DNA.
DR EMBL; L08791; AAA30203.1; -; mRNA.
DR PIR; S61295; S61295.
DR AlphaFoldDB; Q95046; -.
DR SMR; Q95046; -.
DR PRIDE; Q95046; -.
DR VEuPathDB; TriTrypDB:BCY84_01744; -.
DR VEuPathDB; TriTrypDB:BCY84_01745; -.
DR VEuPathDB; TriTrypDB:BCY84_01747; -.
DR VEuPathDB; TriTrypDB:BCY84_01748; -.
DR VEuPathDB; TriTrypDB:BCY84_01749; -.
DR VEuPathDB; TriTrypDB:BCY84_10774; -.
DR VEuPathDB; TriTrypDB:BCY84_10775; -.
DR VEuPathDB; TriTrypDB:BCY84_10777; -.
DR VEuPathDB; TriTrypDB:BCY84_10778; -.
DR VEuPathDB; TriTrypDB:BCY84_10779; -.
DR VEuPathDB; TriTrypDB:BCY84_10780; -.
DR VEuPathDB; TriTrypDB:BCY84_10788; -.
DR VEuPathDB; TriTrypDB:BCY84_10789; -.
DR VEuPathDB; TriTrypDB:BCY84_22916; -.
DR VEuPathDB; TriTrypDB:BCY84_22918; -.
DR VEuPathDB; TriTrypDB:BCY84_22920; -.
DR VEuPathDB; TriTrypDB:C3747_57g233; -.
DR VEuPathDB; TriTrypDB:C3747_57g234; -.
DR VEuPathDB; TriTrypDB:C3747_57g236; -.
DR VEuPathDB; TriTrypDB:C3747_57g237; -.
DR VEuPathDB; TriTrypDB:C4B63_48g86; -.
DR VEuPathDB; TriTrypDB:C4B63_48g87; -.
DR VEuPathDB; TriTrypDB:C4B63_48g88; -.
DR VEuPathDB; TriTrypDB:C4B63_48g89; -.
DR VEuPathDB; TriTrypDB:C4B63_48g90; -.
DR VEuPathDB; TriTrypDB:C4B63_81g101; -.
DR VEuPathDB; TriTrypDB:C4B63_81g102; -.
DR VEuPathDB; TriTrypDB:Tc_MARK_3716; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0017150; -.
DR VEuPathDB; TriTrypDB:TcCL_Unassigned03937; -.
DR VEuPathDB; TriTrypDB:TcCLB.507641.290; -.
DR VEuPathDB; TriTrypDB:TcCLB.510187.551; -.
DR VEuPathDB; TriTrypDB:TCDM_02151; -.
DR VEuPathDB; TriTrypDB:TcG_08163; -.
DR VEuPathDB; TriTrypDB:TCSYLVIO_004969; -.
DR VEuPathDB; TriTrypDB:TcYC6_0126180; -.
DR GO; GO:0005759; C:mitochondrial matrix; 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..8
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 9..562
FT /note="Chaperonin HSP60, mitochondrial"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005039"
FT VARIANT 142
FT /note="S -> N (in strain: PBOL)"
FT VARIANT 249
FT /note="R -> G (in strain: PBOL)"
FT VARIANT 457
FT /note="R -> P (in strain: PBOL)"
FT VARIANT 521
FT /note="A -> P (in strain: PBOL)"
FT VARIANT 531
FT /note="A -> T (in strain: PBOL)"
FT VARIANT 534
FT /note="A -> S (in strain: PBOL)"
FT VARIANT 538
FT /note="L -> F (in strain: PBOL)"
SQ SEQUENCE 562 AA; 59411 MW; F90C705E555C0898 CRC64;
MFRSAARFAG KEIRFGTEAR QSMQKGVQRA VSAVATTLGP KGRNVIIEQS YGAPKITKDG
VTVAKAIEFK DPFENMGAQL VRQVCNKTND LAGDGTTTSA VLVASVFSES LRCIATGTNP
IDMKRGMDRA VGVILQSVAE QSRKVTSTEN IVQVATISAN GDEELGRLIG QAMEKVGKDG
VITTQDGKTM TTELEVVEGM SIDRGYISPY FVTDAKAQKA ELEDAFVLVS AKKVSSIHTI
LPALNHVVRT GRPLLIIADD VESEALTTMI FNKLQGKLKI ACVKAPGFGD NKTAMMQDIA
IFAGARLVGE EGSGLELDAE NFDPAILGTV KKATITKDDT VLLNGGGESS MVKERVELLR
GLIDGETSDY NREKLQERLA KLSGGVAVIK VGGGSEVEVN EKKDRITDAL CSTRAAVQEG
IVPGGGVALL RASKALDSLL GDSSLTADQR TGVQIIRNAV RLPAHTIVLN AGKEGAVVVE
KVLENNDVTV GYDAQRDRYV NMFEAGIIDP ARVVRVAITD AVSVASLMMT AEAAIVDLPK
EETPAAGGMG GMGGMGGMGD MY
