CH60_BOVIN
ID CH60_BOVIN Reviewed; 573 AA.
AC P31081;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=60 kDa heat shock protein, mitochondrial;
DE EC=5.6.1.7 {ECO:0000250|UniProtKB:P10809};
DE AltName: Full=60 kDa chaperonin;
DE AltName: Full=Chaperonin 60;
DE Short=CPN60;
DE AltName: Full=Heat shock protein 60;
DE Short=HSP-60;
DE Short=Hsp60;
DE AltName: Full=Mitochondrial matrix protein P1;
DE Flags: Precursor;
GN Name=HSPD1; Synonyms=HSP60;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP PROTEIN SEQUENCE OF 27-48.
RC TISSUE=Adrenal gland;
RX PubMed=8096152; DOI=10.1016/0925-4439(93)90096-j;
RA Dai Z., Lackland H., Stein S., Li Q., Radziewicz R., Williams R.,
RA Sigal L.H.;
RT "Molecular mimicry in Lyme disease: monoclonal antibody H9724 to B.
RT burgdorferi flagellin specifically detects chaperonin-HSP60.";
RL Biochim. Biophys. Acta 1181:97-100(1993).
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:0000250|UniProtKB:P10809}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an
CC unfolded polypeptide.; EC=5.6.1.7;
CC Evidence={ECO:0000250|UniProtKB:P10809};
CC -!- SUBUNIT: Homoheptamer arranged in a ring structure. 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. Interacts
CC with 2 heptameric Hsp10 rings to form the symmetrical football complex
CC (By similarity). Interacts with HRAS (By similarity). Interacts with
CC ATAD3A. Interacts with ETFBKMT and EEF1AKMT3 (By similarity). Interacts
CC with MFHAS1 (By similarity). {ECO:0000250|UniProtKB:P10809,
CC ECO:0000250|UniProtKB:P63038}.
CC -!- INTERACTION:
CC P31081; F1N588: SMPD2; NbExp=5; IntAct=EBI-9816893, EBI-9786068;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P10809}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR PIR; A56868; A56868.
DR AlphaFoldDB; P31081; -.
DR SMR; P31081; -.
DR IntAct; P31081; 1.
DR STRING; 9913.ENSBTAP00000055431; -.
DR PaxDb; P31081; -.
DR PeptideAtlas; P31081; -.
DR PRIDE; P31081; -.
DR Ensembl; ENSBTAT00000066226; ENSBTAP00000059077; ENSBTAG00000047441.
DR VEuPathDB; HostDB:ENSBTAG00000047441; -.
DR eggNOG; KOG0356; Eukaryota.
DR GeneTree; ENSGT00390000005727; -.
DR InParanoid; P31081; -.
DR OMA; PYILINQ; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000047441; Expressed in theca cell and 79 other tissues.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IEA:UniProt.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
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:chaperone binding; IBA:GO_Central.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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:0032729; P:positive regulation of interferon-gamma 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: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; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR HAMAP; MF_00600; CH60; 1.
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 InterPro; IPR027410; TCP-1-like_intermed_sf.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00298; CHAPERONIN60.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02348; GroEL; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chaperone; Direct protein sequencing; Isomerase;
KW Isopeptide bond; Mitochondrion; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transit peptide; Ubl conjugation.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:8096152"
FT CHAIN 27..573
FT /note="60 kDa heat shock protein, mitochondrial"
FT /id="PRO_0000063635"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT BINDING 111..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT BINDING 440
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT BINDING 520
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 31
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 75
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 82
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 82
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 87
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 90
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 91
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 125
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 125
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 130
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 133
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 133
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 133
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 156
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 191
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 191
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 202
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 202
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 205
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 205
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 218
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 218
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 236
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 236
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 249
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 250
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 250
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 269
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 292
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 301
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 314
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 352
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 352
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 359
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 389
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 396
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 396
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 469
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT MOD_RES 481
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 481
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63038"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10809"
FT CROSSLNK 551
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P10809"
SQ SEQUENCE 573 AA; 61108 MW; 18C46B2CD682A20A CRC64;
MLRLPAVLRQ MRPVSRALAL HLTRAYAKDV KFGADARALM LQGVDLLADA VAVTMGPKGR
TVIIEQSWGS PRVTKDGVTV AKSIDLKDKY KNIGAKLVQD VANNTNEEAG DGTTTATVLA
RSIAKEGFEK ISKGANPVEI RRGVMLAVDA VIVELKKQSK PVTTPEEIAQ VATISANGDK
EIGNIISDAM KKVGRKGVIT VKDGKTLNDE LEIIEGMKFD RGYISPYFIN TSKGQKCEFQ
DAYVLLSEKK ISSVQSIVPA LEIANAHRKP LVIIAEDVDG EALSTLVLNR LKVGLQVVAV
KAPGFGDNRK NQLKDMAIAT GGAVFGEEGL NLNLEDVQPH DLGKVGEVIV TKDDAMLLKG
KGDKAQIEKR IQEIIEQLDI TTSEYEKEKL NERLAKLSDG VAVLKVGGTS DVEVNEKKDR
VTDALNATRA AVEEGIVLGG DCALLRCIPA LESITPANED QKTGIEIIKK TLKIPAMTIA
KNAGVEGSLI VEKIMQSSSE VGYDAMLGDF VNMVEKGIID PTKVVRTALL DAAGVASLLT
TAEVVVTEIP KEEKDPGMGG MGGMGGGMGG GMF
