CH60_PONAB
ID CH60_PONAB Reviewed; 573 AA.
AC Q5NVM5;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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 Flags: Precursor;
GN Name=HSPD1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P10809}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR EMBL; CR925996; CAI29638.1; -; mRNA.
DR RefSeq; NP_001127086.1; NM_001133614.1.
DR AlphaFoldDB; Q5NVM5; -.
DR SMR; Q5NVM5; -.
DR STRING; 9601.ENSPPYP00000014577; -.
DR PRIDE; Q5NVM5; -.
DR GeneID; 100174117; -.
DR KEGG; pon:100174117; -.
DR CTD; 3329; -.
DR eggNOG; KOG0356; Eukaryota.
DR InParanoid; Q5NVM5; -.
DR OrthoDB; 415781at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR GO; GO:0009409; P:response to cold; ISS:AgBase.
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; 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 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.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Chaperone; Isomerase; Isopeptide bond;
KW Mitochondrion; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transit peptide; Ubl conjugation.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 27..573
FT /note="60 kDa heat shock protein, mitochondrial"
FT /id="PRO_0000005028"
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 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; 60998 MW; 973612AC6570DD64 CRC64;
MLRLPTVFRQ MRPVSRVLAP HLTRAYAKDV KFGADARALM LRGVDLLADA VAVTMGPKGR
TVIIEQSWGS PKVTKDGVTV AKSIDLKDKY KNIGAKLVQD VANNTNEEAG DGTTTATVLA
RSIAKEGFEK ISKGANPVEI RRGVMLAVDA VIAELKKQSK PVTTPEEIAQ VATISANGDK
EIGNIISDAM KKVGRKGVIT VKDGKTLNDE LEIIEGMKFD RGYISPYFIN TSKGQKCEFQ
DAYVLLSEKK ISSVQSIVPA LEIANAHRKP LVIIAEDVDG EALSTLVLNR LKVGLQVVAV
KAPGFGDNRK NQLKDMAIAT GGAVFGEEGL TLNLEDVQPH DLGKVGEVIV TKDDAMLLEG
KGDKAQIEKR IQEIIEQLDV TTSEYEKEKL NERLAKLSDG VAVLKVGGTS DVEVNEKKDR
VTDALNATRA AAEEGIVLGG GCALLRCIPA LDSLTPANED QKIGIEIIKR TLKIPAMTIA
KNAGVEGSLI VEKIMQSSSE VGYDAMVGDF VNMVGKGIID PTKVVRTALL DAAGVASLLT
TAEVVVTEIP KEEKDPGMGA MGGMGGGMGG GMF
