CH10_BOVIN
ID CH10_BOVIN Reviewed; 102 AA.
AC P61603; O95421; Q04984; Q3SZV9;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=8104547; DOI=10.3109/10425179309020826;
RA Pilkington S.J., Walker J.E.;
RT "Complementary DNA sequence of bovine cpn10 (Hsp10), a chaperone protein
RT from mitochondria.";
RL DNA Seq. 3:291-295(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GroES chaperonin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X69556; CAA49288.1; -; mRNA.
DR EMBL; BC102684; AAI02685.1; -; mRNA.
DR PIR; A56682; A56682.
DR RefSeq; NP_776771.1; NM_174346.2.
DR AlphaFoldDB; P61603; -.
DR SMR; P61603; -.
DR STRING; 9913.ENSBTAP00000016712; -.
DR PaxDb; P61603; -.
DR PeptideAtlas; P61603; -.
DR PRIDE; P61603; -.
DR Ensembl; ENSBTAT00000016712; ENSBTAP00000016712; ENSBTAG00000012589.
DR GeneID; 281833; -.
DR KEGG; bta:281833; -.
DR CTD; 3336; -.
DR VEuPathDB; HostDB:ENSBTAG00000012589; -.
DR VGNC; VGNC:49071; HSPE1.
DR eggNOG; KOG1641; Eukaryota.
DR GeneTree; ENSGT00390000006350; -.
DR HOGENOM; CLU_132825_0_1_1; -.
DR InParanoid; P61603; -.
DR OMA; EVKYSGE; -.
DR OrthoDB; 1580867at2759; -.
DR TreeFam; TF313814; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000012589; Expressed in oocyte and 105 other tissues.
DR ExpressionAtlas; P61603; baseline and differential.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
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 3: Inferred from homology;
KW Acetylation; Chaperone; Mitochondrion; Phosphoprotein; Reference proteome;
KW Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P61604"
FT CHAIN 2..102
FT /note="10 kDa heat shock protein, mitochondrial"
FT /id="PRO_0000174916"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P61604"
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; 10932 MW; 1F3192C81F6EDB78 CRC64;
MAGQAFRKFL PLFDRVLVER SAAETVTKGG IMLPEKSQGK VLQATVVAVG SGSKGKGGEI
QPVSVKVGDK VLLPEYGGTK VVLDDKDYFL FRDGDILGKY VD
