CH10_RAT
ID CH10_RAT Reviewed; 102 AA.
AC P26772;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 143.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=7904573; DOI=10.1016/0014-5793(94)80263-7;
RA Ryan M.T., Hoogenraad N.J., Hoej P.B.;
RT "Isolation of a cDNA clone specifying rat chaperonin 10, a stress-inducible
RT mitochondrial matrix protein synthesised without a cleavable presequence.";
RL FEBS Lett. 337:152-156(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PRELIMINARY PROTEIN SEQUENCE OF 2-102, CLEAVAGE OF INITIATOR METHIONINE,
RP AND ACETYLATION AT ALA-2.
RC TISSUE=Liver;
RX PubMed=1348860; DOI=10.1073/pnas.89.8.3394;
RA Hartman D.J., Hoogenraad N.J., Condron R., Hoej P.B.;
RT "Identification of a mammalian 10-kDa heat shock protein, a mitochondrial
RT chaperonin 10 homologue essential for assisted folding of trimeric
RT ornithine transcarbamoylase in vitro.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:3394-3398(1992).
RN [4]
RP PROTEIN SEQUENCE OF 2-102.
RC TISSUE=Liver;
RX PubMed=8101099; DOI=10.1016/0167-4838(93)90251-l;
RA Hartman D.J., Hoogenraad N.J., Condron R., Hoej P.B.;
RT "The complete primary structure of rat chaperonin 10 reveals a putative
RT beta alpha beta nucleotide-binding domain with homology to p21ras.";
RL Biochim. Biophys. Acta 1164:219-222(1993).
RN [5]
RP PROTEIN SEQUENCE OF 81-92, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
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 -!- INDUCTION: By stress.
CC -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000305}.
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DR EMBL; X71429; CAA50560.1; -; mRNA.
DR EMBL; BC058492; AAH58492.1; -; mRNA.
DR PIR; S41750; S41750.
DR AlphaFoldDB; P26772; -.
DR SMR; P26772; -.
DR IntAct; P26772; 1.
DR STRING; 10116.ENSRNOP00000020066; -.
DR iPTMnet; P26772; -.
DR PhosphoSitePlus; P26772; -.
DR SwissPalm; P26772; -.
DR jPOST; P26772; -.
DR PaxDb; P26772; -.
DR PRIDE; P26772; -.
DR UCSC; RGD:2844; rat.
DR RGD; 2844; Hspe1.
DR eggNOG; KOG1641; Eukaryota.
DR InParanoid; P26772; -.
DR PhylomeDB; P26772; -.
DR TreeFam; TF313814; -.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR PRO; PR:P26772; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
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; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Acetylation; Chaperone; Direct protein sequencing; Mitochondrion;
KW Phosphoprotein; Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1348860,
FT ECO:0000269|PubMed:8101099"
FT CHAIN 2..102
FT /note="10 kDa heat shock protein, mitochondrial"
FT /id="PRO_0000174919"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:1348860,
FT ECO:0000269|PubMed:8101099"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q64433"
FT MOD_RES 28
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q64433"
FT MOD_RES 40
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q64433"
FT MOD_RES 40
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 40
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q64433"
FT MOD_RES 54
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 54
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q64433"
FT MOD_RES 56
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P61604"
FT MOD_RES 56
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 56
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q64433"
FT MOD_RES 66
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q64433"
FT MOD_RES 66
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q64433"
FT MOD_RES 70
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q64433"
FT MOD_RES 70
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q64433"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P61604"
FT MOD_RES 80
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q64433"
FT MOD_RES 80
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q64433"
FT MOD_RES 86
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P61604"
FT MOD_RES 86
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q64433"
FT MOD_RES 99
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61604"
SQ SEQUENCE 102 AA; 10902 MW; 1F2AE41369AEDB78 CRC64;
MAGQAFRKFL PLFDRVLVER SAAETVTKGG IMLPEKSQGK VLQATVVAVG SGGKGKGGEI
QPVSVKVGDK VLLPEYGGTK VVLDDKDYFL FRDGDILGKY VD
