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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 H+/K+ ATPase is a heterodimeric protein, made up of α and β subunits. The α subunit has 10 TM domains and exhibits catalytic and pore functions, while the β subunit has a single TM domain, which appears to be required for intracellular trafficking and stabilising the α subunit. The ATP4A and ATP4B subunits are expressed together, while the ATP12A subunit is suggested to be expressed with the β1 (ATP1B1) subunit of the Na+/K+-ATPase [1].
ATP12A Show summary » |
ATP4B Show summary » |
Database page citation:
H+/K+-ATPases. Accessed on 10/06/2023. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=160.
Concise Guide to PHARMACOLOGY citation:
Alexander SP, Kelly E, Mathie A, Peters JA, Veale EL et al. (2021) THE CONCISE GUIDE TO PHARMACOLOGY 2021/22: Transporters. Br J Pharmacol. 178 Suppl 1:S412-S513.
The gastric H+/K+-ATPase is inhibited by proton pump inhibitors (PPIs, e.g. dexlansoprazole and esomeprazole) which are used to treat excessive gastric acid secretion. PPIs have a gradual onset of action. More quickly acting potassium-competitive acid blockers (P-CABs; e.g. vonoprazan, revaprazan and tegoprazan) have now entered the clinic. P-CABs are competitive and reversible H+/K+ ATPase blockers and their effect on acid suppression is stronger and more sustained compared to PPIs.