ID   CH10_ORYLA              Reviewed;          99 AA.
AC   Q9W6X3;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=10 kDa heat shock protein, mitochondrial;
DE            Short=Hsp10;
DE   AltName: Full=10 kDa chaperonin;
DE   AltName: Full=Chaperonin 10;
DE            Short=CPN10;
GN   Name=hspe1; Synonyms=hsp10;
OS   Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=8090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10603084; DOI=10.1007/pl00008185;
RA   Henrich T., Wittbrodt J.;
RT   "An in situ hybridization screen for the rapid isolation of differentially
RT   expressed genes.";
RL   Dev. Genes Evol. 210:28-33(2000).
CC   -!- FUNCTION: Co-chaperonin implicated in mitochondrial protein import and
CC       macromolecular assembly. Together with Hsp60, facilitates the correct
CC       folding of imported proteins. May also prevent misfolding and promote
CC       the refolding and proper assembly of unfolded polypeptides generated
CC       under stress conditions in the mitochondrial matrix. The functional
CC       units of these chaperonins consist of heptameric rings of the large
CC       subunit Hsp60, which function as a back-to-back double ring. In a
CC       cyclic reaction, Hsp60 ring complexes bind one unfolded substrate
CC       protein per ring, followed by the binding of ATP and association with 2
CC       heptameric rings of the co-chaperonin Hsp10. This leads to
CC       sequestration of the substrate protein in the inner cavity of Hsp60
CC       where, for a certain period of time, it can fold undisturbed by other
CC       cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits
CC       results in the dissociation of the chaperonin rings and the release of
CC       ADP and the folded substrate protein. {ECO:0000250|UniProtKB:P61604}.
CC   -!- SUBUNIT: Homoheptamer arranged in a ring structure. 2 heptameric Hsp10
CC       rings interact with a Hsp60 tetradecamer in the structure of a back-to-
CC       back double heptameric ring to form the symmetrical football complex.
CC       {ECO:0000250|UniProtKB:P61604}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:P61604}.
CC   -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000305}.
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DR   EMBL; AJ238010; CAB40895.1; -; mRNA.
DR   RefSeq; NP_001098232.1; NM_001104762.1.
DR   AlphaFoldDB; Q9W6X3; -.
DR   SMR; Q9W6X3; -.
DR   STRING; 8090.ENSORLP00000025855; -.
DR   GeneID; 100049361; -.
DR   KEGG; ola:100049361; -.
DR   CTD; 3336; -.
DR   eggNOG; KOG1641; Eukaryota.
DR   InParanoid; Q9W6X3; -.
DR   OrthoDB; 1580867at2759; -.
DR   Proteomes; UP000001038; Unplaced.
DR   Proteomes; UP000265180; Chromosome 9.
DR   Proteomes; UP000265200; Chromosome 9.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0046872; F:metal ion binding; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   CDD; cd00320; cpn10; 1.
DR   Gene3D; 2.30.33.40; -; 1.
DR   HAMAP; MF_00580; CH10; 1.
DR   InterPro; IPR020818; Chaperonin_GroES.
DR   InterPro; IPR037124; Chaperonin_GroES_sf.
DR   InterPro; IPR018369; Chaprnonin_Cpn10_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   PANTHER; PTHR10772; PTHR10772; 1.
DR   Pfam; PF00166; Cpn10; 1.
DR   PRINTS; PR00297; CHAPERONIN10.
DR   SMART; SM00883; Cpn10; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   PROSITE; PS00681; CHAPERONINS_CPN10; 1.
PE   3: Inferred from homology;
KW   Chaperone; Mitochondrion; Reference proteome.
FT   CHAIN           1..99
FT                   /note="10 kDa heat shock protein, mitochondrial"
FT                   /id="PRO_0000174920"
SQ   SEQUENCE   99 AA;  10962 MW;  A63E42A0441AE063 CRC64;
     MAFRKFLPLF DRVLVERLMA ETVTKGGIML PEKSQGKVLQ ATVVAVGPGS MNQKGEVQPM
     SVKVGEKVLL PQYGGTKVVL EDKDYFLFRD ADILGKYVD