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3.A.2.1.3
H+-translocating F-type ATPase. Evidence of the proximity of ATP synthase subunit 6 is in proximity to the membrane in the supramolecular form (Velours et al., 2011).  The structure of the intact monomeric ATP synthase from the fungus, Pichia angusta, has been solved by electron cryo-microscopy (Vinothkumar et al. 2016). The Mg2+ and Ca2+-dependent enzymes are both active, but exhibit quite different behaviors (Nesci et al. 2017). Dimerization is necessary to create the inner membrane folds (cristae) characteristic of mitochondria.  Using cryo-electron microscopy, Guo et al. 2017 determined the structure of the dimeric FO complex from Saccharomyces cerevisiae at a resolution of 3.6 angstroms. The structure clarifies how the protons travel through the complex, how the complex dimerizes, and how the dimers bend the membrane to produce cristae. The crystal structure of the c-subunit ring with bound oligomycin revealed the inhibitor docked on the outer face of the proton-binding sites, deep in the transmembrane region (Zhou and Faraldo-Gómez 2018). A high resolution (3.7 Å) structure of the entire monomeric ATPase has been solved by cryo EM, suggesting how it is inhibited by oligomycin (Srivastava et al. 2018).  Absence of the e and g subunits decreases conductance of the F-ATP synthase channel about tenfold. Ablation of the first TMS of subunit b, which creates a distinct lateral domain with e and g, further affected channel activity. Thus, F-ATP synthase e, g and b subunits create a domain within the membrane that is critical for the generation of the high-conductance channel that is a prime candidate for formation of the permeability transition pore (PTP). Subunits e and g are only present in eukaryotes and may have evolved to confer this novel function to F-ATP synthases (Carraro et al. 2018). The translation rate of all yeast mitochondrial mRNAs, including all F-type ATPase subunits has been studied (Chicherin et al. 2021). Attenuated ADP-inhibition of F0F1 ATPase mitigates manifestations of mitochondrial dysfunction in yeast (Lapashina et al. 2022).

Accession Number:Q12349
Protein Name:ATP14 aka AT14 aka YLR295C aka L8003.20
Length:124
Molecular Weight:14128.00
Species:Saccharomyces cerevisiae (Baker's yeast) [4932]
Location1 / Topology2 / Orientation3: Mitochondrion1
Substrate hydron

Cross database links:

DIP: DIP-3030N
RefSeq: NP_013398.1   
Entrez Gene ID: 851002   
Pfam: PF10775   
KEGG: sce:YLR295C   

Gene Ontology

GO:0000276 C:mitochondrial proton-transporting ATP synth...
GO:0005515 F:protein binding
GO:0015986 P:ATP synthesis coupled proton transport
GO:0042407 P:cristae formation
GO:0033615 P:mitochondrial proton-transporting ATP synth...

References (4)

[1] “ATP synthase of yeast mitochondria. Isolation of the subunit h and disruption of the ATP14 gene.”  Arselin G.et.al.   8702761
[2] “The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.”  Johnston M.et.al.   9169871
[3] “Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.”  Hu Y.et.al.   17322287
[4] “Global analysis of protein expression in yeast.”  Ghaemmaghami S.et.al.   14562106
Structure:
6CP3   6CP6     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MFPIASRRIL LNASVLPLRL CNRNFTTTRI SYNVIQDLYL RELKDTKLAP STLQDAEGNV 
61:	KPWNPPQKPN LPELELQGPE ALKAYTEQNV ETAHVAKESE EGESEPIEED WLVLDDAEET 
121:	KESH