ID F1MUZ9_BOVIN Unreviewed; 573 AA. AC F1MUZ9; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 28-JUN-2023, entry version 89. 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|Ensembl:ENSBTAP00000016708.5, GN 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:ENSBTAP00000016708.5, ECO:0000313|Proteomes:UP000009136}; RN [1] {ECO:0000313|Ensembl:ENSBTAP00000016708.5, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000016708.5, 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:ENSBTAP00000016708.5} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000016708.5}; RG Ensembl; RL Submitted (MAR-2023) to UniProtKB. 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 chaperonin (HSP60) family. CC {ECO:0000256|ARBA:ARBA00006607, ECO:0000256|RuleBase:RU000418}. 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 RefSeq; NP_001160080.1; NM_001166608.1. DR RefSeq; NP_001160081.1; NM_001166609.1. DR RefSeq; NP_001160082.1; NM_001166610.1. DR Ensembl; ENSBTAT00000016708.6; ENSBTAP00000016708.5; ENSBTAG00000012586.6. DR Ensembl; ENSBTAT00000064253.2; ENSBTAP00000055431.1; ENSBTAG00000012586.6. DR GeneID; 511913; -. 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 Proteomes; UP000009136; Chromosome 2. DR Bgee; ENSBTAG00000012586; Expressed in diaphragm and 105 other 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; 1. DR Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 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 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; 1. DR PRINTS; PR00298; CHAPERONIN60. DR SUPFAM; SSF52029; GroEL apical domain-like; 1. DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1. DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1. DR TIGRFAMs; TIGR02348; GroEL; 1. DR PROSITE; PS00296; CHAPERONINS_CPN60; 1. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Chaperone {ECO:0000256|ARBA:ARBA00023186}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Proteomics identification {ECO:0007829|PeptideAtlas:F1MUZ9}; KW Reference proteome {ECO:0000313|Proteomes:UP000009136}. SQ SEQUENCE 573 AA; 60978 MW; A89C00A4C74010AE CRC64; MLRLPAVLRQ MRPVSRALAP HLTRAYAKDV KFGADARALM LQGVDLLADA 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 NLNLEDVQPH DLGKVGEVIV TKDDAMLLKG KGDKAQIEKR IQEIIEQLDI TTSEYEKEKL NERLAKLSDG VAVLKVGGTS DVEVNEKKDR VTDALNATRA AVEEGIVLGG GCALLRCIPA LESITPANED QKTGIEIIKK TLKIPAMTIA KNAGVEGSLI VEKIMQSSSE VGYDAMLGDF VNMVEKGIID PTKVVRTALL DAAGVASLLT TAEVVVTEIP KEEKDPGMGG MGGMGGGMGG GMF //