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Unless otherwise stated all data on this page refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).
The F-type ATPase, also known as ATP synthase or ATP phosphohydrolase (H+-transporting), is a mitochondrial membrane-associated multimeric complex consisting of two domains, an F0 channel domain in the membrane and an F1 domain extending into the lumen. Proton transport across the inner mitochondrial membrane is used to drive the synthesis of ATP, although it is also possible for the enzyme to function as an ATPase. The ATP5O subunit (oligomycin sensitivity-conferring protein, OSCP, (P48047)), acts as a connector between F1 and F0 motors.
The F1 motor, responsible for ATP turnover, has the subunit composition α3β3γδε.
The F0 motor, responsible for ion translocation, is complex in mammals, with probably nine subunits centring on A, B, and C subunits in the membrane, together with D, E, F2, F6, G2 and 8 subunits. Multiple pseudogenes for the F0 motor proteins have been defined in the human genome.
F-type ATPase α subunit Show summary » |
F-type ATPase β subunit Show summary » |
F-type ATPase γ subunit Show summary » |
F-type ATPase δ subunit Show summary » |
F-type ATPase ε subunit Show summary » |
F-type ATPase A subunit Show summary » |
F-type ATPase B subunit Show summary » |
F-type ATPase C subunit Show summary » |
F-type ATPase D subunit Show summary » |
F-type ATPase E subunit Show summary » |
F-type ATPase F2 subunit Show summary » |
F-type ATPase F6 subunit Show summary » |
F-type ATPase G2 subunit Show summary » |
F-type ATPase 8 subunit Show summary » |
Database page citation:
F-type ATPase. Accessed on 12/11/2024. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=156.
Concise Guide to PHARMACOLOGY citation:
Alexander SPH, Fabbro D, Kelly E, Mathie AA, Peters JA, Veale EL, Armstrong JF, Faccenda E, Harding SD, Davies JA et al. (2023) The Concise Guide to PHARMACOLOGY 2023/24: Transporters. Br J Pharmacol. 180 Suppl 2:S374-469.