Primary Information | |
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BoMiProt ID | Bomi4138 |
Protein Name | ATP synthase subunit beta, mitochondrial/ATP synthase F1 subunit beta |
Organism | Bos taurus |
Uniprot ID | P00829 |
Milk Fraction | Whey |
Ref Sequence ID | NP_786990.1 |
Aminoacid Length | 528 |
Molecular Weight | 56284 |
FASTA Sequence | Download |
Gene Name | ATP5F1B/ATP5B |
Gene ID | 327675 |
Protein Existence Status | reviewed |
Secondary Information | |
Protein Function | It is a subunit of ATP synthase (F1F0 ATP synthase or Complex V) which is a part of ETS,producing ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. |
Biochemical Properties | β-F1 -ATPase forms the catalytic site of the enzyme ATP synthase |
PTMs | Acetylation, Glycosylation, Phosphorylation |
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | >sp|P00829|ATPB_BOVIN ATP synthase subunit beta, mitochondrial OS=Bos taurus OX=9913 GN=ATP5F1B PE=1 SV=2 MLGLVGRVVAASASGALRGLSPSAPLPQAQLLLRAAPAALQPARDYAAQASPSPKAGATT GRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGES*106TVRTIAMDGTEGLV RGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQ EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERT REGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQD VLLFIDNIFRFT*312QAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAI YVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGS*415EHYDV ARGVQKILQDYKS*433LQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHLGK LVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHS |
SCOP | Class : All alpha proteins Fold : Left-handed alpha-alpha superhelix Superfamily : ATP synthase alpha/beta C-terminal domain-like and RecA-like P-loop NTPases Family : ATP synthase nucleotide-binding domain-like Domain Name : 2JDI D:127-445 Class : Alpha and beta proteins (a/b) Fold : RecA-like basic Superfamily : RecA-like P-loop NTPases Family : ATP synthase nucleotide-binding domain-like Domain Name : 2JDI D:127-445 Class : All beta proteins Fold : ATP synthase beta-barrel domain-like Superfamily : ATP synthase alpha/beta N-terminal domain-like Family : ATP synthase alpha/beta N-terminal domain-like Domain Name : 2JDI D:9-81 |
CATH | Matched CATH superfamily 1.10.1140.10 2.40.10.170 3.40.50.300 |
Predicted Disorder Regions | NA |
DisProt Annotation | |
TM Helix Prediction | no TM helices |
PDB ID | 1BMF,1COW,1E1Q,1E1R,1E79,1EFR,1H8E,1H8H,1NBM,1OHH,1QO1,1W0J,1W0K,2CK3,2JDI,2JIZ,2JJ1,2JJ2,2V7Q,2W6E,2W6F,2W6G,2W6H,2W6I,2W6J,2WSS,2XND,4ASU,4TSF,4TT3,4YXW,4Z1M,5ARA,5ARE,5ARH,5ARI,5FIJ,5FIK,5FIL,6YY0,6Z1R,6Z1U,6ZPO,6ZQM,6ZQN,7AJB,7AJC,7AJD,7AJE,7AJF,7AJG,7AJH,7AJI,7AJJ., |
Additional Comments | Humans with obesity have lower synthesis rate of β-F1-ATPase and ATP synthase specific activity in muscle. These findings indicate that reduced production of subunits forming the ATP synthase in muscle may contribute to impaired generation of ATP in obesity. |
Bibliography | 1.Tran L, Langlais PR, Hoffman N, Roust L, Katsanos CS. Mitochondrial ATP synthase β-subunit production rate and ATP synthase specific activity are reduced in skeletal muscle of humans with obesity. Exp Physiol. 2019 Jan;104(1):126-135. doi: 10.1113/EP087278. Epub 2018 Nov 12. PMID: 30362197; PMCID: PMC6312454. |