CH60_HELVI
ID CH60_HELVI Reviewed; 24 AA.
AC P26317;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=60 kDa chaperonin, mitochondrial;
DE AltName: Full=P60;
DE Flags: Fragment;
OS Heliothis virescens (Tobacco budworm moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Heliothinae; Heliothis.
OX NCBI_TaxID=7102;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Testis;
RX PubMed=1974308; DOI=10.1016/0022-2836(90)90190-w;
RA Miller S.G., Leclerc R.F., Erdos G.W.;
RT "Identification and characterization of a testis-specific isoform of a
RT chaperonin in a moth, Heliothis virescens.";
RL J. Mol. Biol. 214:407-422(1990).
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 -!- SUBUNIT: Forms a single seven-member ring complex, in tight association
CC with the p63 protein.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- TISSUE SPECIFICITY: Testis.
CC -!- DEVELOPMENTAL STAGE: From the second half of the larval final-instar,
CC through the first two days of pupal development.
CC -!- MISCELLANEOUS: Shows ATPase activity.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR AlphaFoldDB; P26317; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Direct protein sequencing; Mitochondrion;
KW Nucleotide-binding.
FT CHAIN 1..>24
FT /note="60 kDa chaperonin, mitochondrial"
FT /id="PRO_0000063637"
FT NON_TER 24
SQ SEQUENCE 24 AA; 2531 MW; 2B34508F8CA981CF CRC64;
AKDVRFGADV RALMLQGVDV LADA