ID F1MUZ9_BOVIN Unreviewed; 541 AA.
AC F1MUZ9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 2.
DT 02-OCT-2024, entry version 96.
DE RecName: Full=60 kDa heat shock protein, mitochondrial {ECO:0000256|ARBA:ARBA00019981};
DE EC=5.6.1.7 {ECO:0000256|ARBA:ARBA00012198};
DE AltName: Full=60 kDa chaperonin {ECO:0000256|ARBA:ARBA00029756};
DE AltName: Full=Chaperonin 60 {ECO:0000256|ARBA:ARBA00031799};
DE AltName: Full=Heat shock protein 60 {ECO:0000256|ARBA:ARBA00030005};
GN Name=HSPD1 {ECO:0000313|VGNC:VGNC:49070};
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 {ECO:0000313|Ensembl:ENSBTAP00000016708.6, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000016708.6, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000016708.6,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000016708.6}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000016708.6};
RG Ensembl;
RL Submitted (JUN-2024) to UniProtKB.
CC -!- FUNCTION: Chaperonin implicated in mitochondrial protein import and
CC macromolecular assembly. Together with Hsp10, 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:0000256|ARBA:ARBA00037436}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an
CC unfolded polypeptide.; EC=5.6.1.7;
CC Evidence={ECO:0000256|ARBA:ARBA00034033};
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
CC {ECO:0000256|ARBA:ARBA00008020}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000256|ARBA:ARBA00006607}.
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DR AlphaFoldDB; F1MUZ9; -.
DR STRING; 9913.ENSBTAP00000016708; -.
DR Ensembl; ENSBTAT00000016708.7; ENSBTAP00000016708.6; ENSBTAG00000012586.7.
DR KEGG; bta:511913; -.
DR CTD; 3329; -.
DR VEuPathDB; HostDB:ENSBTAG00000012586; -.
DR VGNC; VGNC:49070; HSPD1.
DR GeneTree; ENSGT00390000005727; -.
DR HOGENOM; CLU_016503_3_0_1; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 123639at2759; -.
DR TreeFam; TF300475; -.
DR Reactome; R-BTA-1268020; Mitochondrial protein import.
DR Reactome; R-BTA-9837999; Mitochondrial protein degradation.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000012586; Expressed in diaphragm and 105 other cell types or tissues.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IEA:UniProt.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
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:0051087; F:protein-folding chaperone binding; IBA:GO_Central.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IBA:GO_Central.
DR GO; GO:0034514; P:mitochondrial unfolded protein response; IBA:GO_Central.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; IBA:GO_Central.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IBA:GO_Central.
DR GO; GO:0050870; P:positive regulation of T cell activation; IBA:GO_Central.
DR GO; GO:0032729; P:positive regulation of type II interferon production; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR GO; GO:0009409; P:response to cold; ISS:AgBase.
DR GO; GO:0042110; P:T cell activation; IBA:GO_Central.
DR CDD; cd03344; GroEL; 1.
DR Gene3D; 3.50.7.10; GroEL; 1.
DR Gene3D; 1.10.560.10; GroEL-like equatorial domain; 2.
DR InterPro; IPR017998; Chaperone_TCP-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 PANTHER; PTHR45633; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45633:SF3; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00118; Cpn60_TCP1; 2.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136}.
SQ SEQUENCE 541 AA; 57682 MW; C1E505E9AA8CA26D CRC64;
MLRLPAVLRQ MRPVSRALAP HLTRAYAKDV KFGADARALM LQGVDLLADA VAVTMGPKGR
TVIIEQSWGS PKVTKDGVTV AKSIDLKDKY KNIGAKLVQD VANNTNEEAG DGTTTATVLA
RSIAKEGFEK ISKGANPVEI RRGVMLAVDA VIAELKKQSK PVTTPEEIAQ DGKTLNDELE
IIEGMKFDRG YISPYFINTS KGQKCEFQDA YVLLSEKKIS SVQSIVPALE IANAHRKPLV
IIAEDVDGEA LSTLVLNRLK VGLQVVAVKA PGFGDNRKNQ LKDMAIATGG AVFGEEGLNL
NLEDVQPHDL GKVGEVIVTK DDAMLLKGKG DKAQIEKRIQ EIIEQLDITT SEYEKEKLNE
RLAKLSDGVA VLKVGGTSDV EVNEKKDRVT DALNATRAAV EEGIVLGGGC ALLRCIPALE
SITPANEDQK TGIEIIKKTL KIPAMTIAKN AGVEGSLIVE KIMQSSSEVG YDAMLGDFVN
MVEKGIIDPT KVVRTALLDA AGVASLLTTA EVVVTEIPKE EKDPGMGGMG GMGGGMGGGM
F
//