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Literature summary extracted from

  • Shin, J.M.; Munson, K.; Vagin, O.; Sachs, G.
    The gastric HK-ATPase: structure, function, and inhibition (2009), Pflugers Arch., 457, 609-622.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
7.2.2.19 K791S the mutation greatly reduces enzyme activity as well as increases the Ki for 2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile Homo sapiens
7.2.2.19 K791S the mutation greatly reduces enzyme activity as well as increases the Ki for 2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile Rattus norvegicus
7.2.2.19 K791S the mutation greatly reduces enzyme activity as well as increases the Ki for 2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile Oryctolagus cuniculus
7.2.2.19 K791S the mutation greatly reduces enzyme activity as well as increases the Ki for 2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile Canis lupus familiaris
7.2.2.19 K791S the mutation greatly reduces enzyme activity as well as increases the Ki for SCH28080 Sus scrofa
7.2.2.19 additional information mutations towards the exoplasmic surface of TM4, TM5, TM6, the loop between TM5 and TM6, and one site at the end of TM8 altered either the Ki or change the nature of inhibition from strictly competitive to mixed or even non-competitive without affecting ion affinity Homo sapiens
7.2.2.19 additional information mutations towards the exoplasmic surface of TM4, TM5, TM6, the loop between TM5 and TM6, and one site at the end of TM8 altered either the Ki or change the nature of inhibition from strictly competitive to mixed or even non-competitive without affecting ion affinity Rattus norvegicus
7.2.2.19 additional information mutations towards the exoplasmic surface of TM4, TM5, TM6, the loop between TM5 and TM6, and one site at the end of TM8 altered either the Ki or change the nature of inhibition from strictly competitive to mixed or even non-competitive without affecting ion affinity Sus scrofa
7.2.2.19 additional information mutations towards the exoplasmic surface of TM4, TM5, TM6, the loop between TM5 and TM6, and one site at the end of TM8 altered either the Ki or change the nature of inhibition from strictly competitive to mixed or even non-competitive without affecting ion affinity Oryctolagus cuniculus
7.2.2.19 additional information mutations towards the exoplasmic surface of TM4, TM5, TM6, the loop between TM5 and TM6, and one site at the end of TM8 altered either the Ki or change the nature of inhibition from strictly competitive to mixed or even non-competitive without affecting ion affinity Canis lupus familiaris

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.2.2.19 2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile i.e. SCH28080 Canis lupus familiaris
7.2.2.19 2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile i.e. SCH28080 Homo sapiens
7.2.2.19 2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile i.e. SCH28080 Oryctolagus cuniculus
7.2.2.19 2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile i.e. SCH28080 Rattus norvegicus
7.2.2.19 2-methyl-8-(phenylmethoxy)imidazo[1,2-a]pyridine-3-acetonitrile i.e. SCH28080 Sus scrofa
7.2.2.19 BYK36399
-
 Canis lupus familiaris
7.2.2.19 BYK36399
-
 Homo sapiens
7.2.2.19 BYK36399
-
 Oryctolagus cuniculus
7.2.2.19 BYK36399
-
 Rattus norvegicus
7.2.2.19 BYK36399
-
 Sus scrofa
7.2.2.19 esomeprazole
-
 Canis lupus familiaris
7.2.2.19 esomeprazole
-
 Homo sapiens
7.2.2.19 esomeprazole
-
 Oryctolagus cuniculus
7.2.2.19 esomeprazole
-
 Rattus norvegicus
7.2.2.19 esomeprazole
-
 Sus scrofa
7.2.2.19 lansoprazole
-
 Canis lupus familiaris
7.2.2.19 lansoprazole
-
 Homo sapiens
7.2.2.19 lansoprazole
-
 Oryctolagus cuniculus
7.2.2.19 lansoprazole
-
 Rattus norvegicus
7.2.2.19 lansoprazole
-
 Sus scrofa
7.2.2.19 additional information inhibitor binding and inhibition kinetics Canis lupus familiaris
7.2.2.19 additional information inhibitor binding and inhibition kinetics Homo sapiens
7.2.2.19 additional information inhibitor binding and inhibition kinetics Oryctolagus cuniculus
7.2.2.19 additional information inhibitor binding and inhibition kinetics Rattus norvegicus
7.2.2.19 additional information inhibitor binding and inhibition kinetics Sus scrofa
7.2.2.19 N-methyl-BYK36399
-
 Canis lupus familiaris
7.2.2.19 N-methyl-BYK36399
-
 Homo sapiens
7.2.2.19 N-methyl-BYK36399
-
 Oryctolagus cuniculus
7.2.2.19 N-methyl-BYK36399
-
 Rattus norvegicus
7.2.2.19 N-methyl-BYK36399
-
 Sus scrofa
7.2.2.19 Omeprazole
-
 Canis lupus familiaris
7.2.2.19 Omeprazole
-
 Homo sapiens
7.2.2.19 Omeprazole
-
 Oryctolagus cuniculus
7.2.2.19 Omeprazole
-
 Rattus norvegicus
7.2.2.19 Omeprazole
-
 Sus scrofa
7.2.2.19 pantoprazole
-
 Canis lupus familiaris
7.2.2.19 pantoprazole
-
 Homo sapiens
7.2.2.19 pantoprazole
-
 Oryctolagus cuniculus
7.2.2.19 pantoprazole
-
 Rattus norvegicus
7.2.2.19 pantoprazole
-
 Sus scrofa
7.2.2.19 rabeprazole
-
 Canis lupus familiaris
7.2.2.19 rabeprazole
-
 Homo sapiens
7.2.2.19 rabeprazole
-
 Oryctolagus cuniculus
7.2.2.19 rabeprazole
-
 Rattus norvegicus
7.2.2.19 rabeprazole
-
 Sus scrofa
7.2.2.19 timoprazole
-
 Canis lupus familiaris
7.2.2.19 timoprazole
-
 Homo sapiens
7.2.2.19 timoprazole
-
 Oryctolagus cuniculus
7.2.2.19 timoprazole
-
 Rattus norvegicus
7.2.2.19 timoprazole
-
 Sus scrofa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.2.2.19 membrane apical membrane Sus scrofa 16020
-
7.2.2.19 membrane apical membrane Oryctolagus cuniculus 16020
-
7.2.2.19 membrane apical membrane Canis lupus familiaris 16020
-
7.2.2.19 membrane apical membrane, cytoplasmic tubular membranes in the resting state Homo sapiens 16020
-
7.2.2.19 membrane apical membrane, cytoplasmic tubular membranes in the resting state Rattus norvegicus 16020
-
7.2.2.19 microsome relatively ion tight vesicles Sus scrofa
-
-
7.2.2.19 microvillus microvilli of the expanded secretory canaliculus in the stimulated state of the parietal cell Homo sapiens 5902
-
7.2.2.19 microvillus microvilli of the expanded secretory canaliculus in the stimulated state of the parietal cell Rattus norvegicus 5902
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.2.2.19 Mg2+ required Homo sapiens
7.2.2.19 Mg2+ required Rattus norvegicus
7.2.2.19 Mg2+ required Sus scrofa
7.2.2.19 Mg2+ required Oryctolagus cuniculus
7.2.2.19 Mg2+ required Canis lupus familiaris

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.2.2.19 ATP + H2O + H+/in + K+/out Homo sapiens the H,K-ATPase is the final step of acid secretion ADP + phosphate + H+/out + K+/in
-
 ?
7.2.2.19 ATP + H2O + H+/in + K+/out Rattus norvegicus the H,K-ATPase is the final step of acid secretion ADP + phosphate + H+/out + K+/in
-
 ?
7.2.2.19 ATP + H2O + H+/in + K+/out Sus scrofa the H,K-ATPase is the final step of acid secretion ADP + phosphate + H+/out + K+/in
-
 ?
7.2.2.19 ATP + H2O + H+/in + K+/out Oryctolagus cuniculus the H,K-ATPase is the final step of acid secretion ADP + phosphate + H+/out + K+/in
-
 ?
7.2.2.19 ATP + H2O + H+/in + K+/out Canis lupus familiaris the H,K-ATPase is the final step of acid secretion ADP + phosphate + H+/out + K+/in
-
 ?
7.2.2.19 additional information Homo sapiens a K+ efflux channel is associated with the gastric H,K-ATPase, KCNQ1-KCNE2 appears to be the K+ efflux channel that is essential for gastric acid secretion ?
-
 ?
7.2.2.19 additional information Rattus norvegicus a K+ efflux channel is associated with the gastric H,K-ATPase, KCNQ1-KCNE2 appears to be the K+ efflux channel that is essential for gastric acid secretion ?
-
 ?
7.2.2.19 additional information Sus scrofa a K+ efflux channel is associated with the gastric H,K-ATPase, KCNQ1-KCNE2 appears to be the K+ efflux channel that is essential for gastric acid secretion ?
-
 ?
7.2.2.19 additional information Oryctolagus cuniculus a K+ efflux channel is associated with the gastric H,K-ATPase, KCNQ1-KCNE2 appears to be the K+ efflux channel that is essential for gastric acid secretion ?
-
 ?
7.2.2.19 additional information Canis lupus familiaris a K+ efflux channel is associated with the gastric H,K-ATPase, KCNQ1-KCNE2 appears to be the K+ efflux channel that is essential for gastric acid secretion ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.2.2.19 Canis lupus familiaris
-
-
-
7.2.2.19 Homo sapiens
-
-
-
7.2.2.19 Oryctolagus cuniculus
-
-
-
7.2.2.19 Rattus norvegicus
-
-
-
7.2.2.19 Sus scrofa
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
7.2.2.19 glycoprotein N-glycosylation of the beta subunit Homo sapiens
7.2.2.19 glycoprotein N-glycosylation of the beta subunit Rattus norvegicus
7.2.2.19 glycoprotein N-glycosylation of the beta subunit Sus scrofa
7.2.2.19 glycoprotein N-glycosylation of the beta subunit Oryctolagus cuniculus
7.2.2.19 glycoprotein N-glycosylation of the beta subunit Canis lupus familiaris

Reaction

EC Number Reaction Comment Organism Reaction ID
7.2.2.19 ATP + H2O + H+[side 1] + K+[side 2] = ADP + phosphate + H+[side 2] + K+[side 1] orientation of the subunits in the membrane towards cytoplasmic and periplasmic sides and reaction mechanism, detailed overview Homo sapiens
a
7.2.2.19 ATP + H2O + H+[side 1] + K+[side 2] = ADP + phosphate + H+[side 2] + K+[side 1] orientation of the subunits in the membrane towards cytoplasmic and periplasmic sides and reaction mechanism, detailed overview Rattus norvegicus
a
7.2.2.19 ATP + H2O + H+[side 1] + K+[side 2] = ADP + phosphate + H+[side 2] + K+[side 1] orientation of the subunits in the membrane towards cytoplasmic and periplasmic sides and reaction mechanism, detailed overview Sus scrofa
a
7.2.2.19 ATP + H2O + H+[side 1] + K+[side 2] = ADP + phosphate + H+[side 2] + K+[side 1] orientation of the subunits in the membrane towards cytoplasmic and periplasmic sides and reaction mechanism, detailed overview Oryctolagus cuniculus
a
7.2.2.19 ATP + H2O + H+[side 1] + K+[side 2] = ADP + phosphate + H+[side 2] + K+[side 1] orientation of the subunits in the membrane towards cytoplasmic and periplasmic sides and reaction mechanism, detailed overview Canis lupus familiaris
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
7.2.2.19 oxyntic cell
-
 Homo sapiens
-
7.2.2.19 oxyntic cell
-
 Rattus norvegicus
-
7.2.2.19 oxyntic cell
-
 Sus scrofa
-
7.2.2.19 oxyntic cell
-
 Oryctolagus cuniculus
-
7.2.2.19 oxyntic cell
-
 Canis lupus familiaris
-
7.2.2.19 renal medulla
-
 Homo sapiens
-
7.2.2.19 renal medulla
-
 Rattus norvegicus
-
7.2.2.19 renal medulla
-
 Sus scrofa
-
7.2.2.19 renal medulla
-
 Oryctolagus cuniculus
-
7.2.2.19 renal medulla
-
 Canis lupus familiaris
-
7.2.2.19 stomach
-
 Homo sapiens
-
7.2.2.19 stomach
-
 Rattus norvegicus
-
7.2.2.19 stomach
-
 Sus scrofa
-
7.2.2.19 stomach
-
 Oryctolagus cuniculus
-
7.2.2.19 stomach
-
 Canis lupus familiaris
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.2.2.19 ATP + H2O + H+/in + K+/out
-
 Homo sapiens ADP + phosphate + H+/out + K+/in
-
 ?
7.2.2.19 ATP + H2O + H+/in + K+/out
-
 Rattus norvegicus ADP + phosphate + H+/out + K+/in
-
 ?
7.2.2.19 ATP + H2O + H+/in + K+/out
-
 Sus scrofa ADP + phosphate + H+/out + K+/in
-
 ?
7.2.2.19 ATP + H2O + H+/in + K+/out
-
 Oryctolagus cuniculus ADP + phosphate + H+/out + K+/in
-
 ?
7.2.2.19 ATP + H2O + H+/in + K+/out
-
 Canis lupus familiaris ADP + phosphate + H+/out + K+/in
-
 ?
7.2.2.19 ATP + H2O + H+/in + K+/out the H,K-ATPase is the final step of acid secretion Homo sapiens ADP + phosphate + H+/out + K+/in
-
 ?
7.2.2.19 ATP + H2O + H+/in + K+/out the H,K-ATPase is the final step of acid secretion Rattus norvegicus ADP + phosphate + H+/out + K+/in
-
 ?
7.2.2.19 ATP + H2O + H+/in + K+/out the H,K-ATPase is the final step of acid secretion Sus scrofa ADP + phosphate + H+/out + K+/in
-
 ?
7.2.2.19 ATP + H2O + H+/in + K+/out the H,K-ATPase is the final step of acid secretion Oryctolagus cuniculus ADP + phosphate + H+/out + K+/in
-
 ?
7.2.2.19 ATP + H2O + H+/in + K+/out the H,K-ATPase is the final step of acid secretion Canis lupus familiaris ADP + phosphate + H+/out + K+/in
-
 ?
7.2.2.19 additional information a K+ efflux channel is associated with the gastric H,K-ATPase, KCNQ1-KCNE2 appears to be the K+ efflux channel that is essential for gastric acid secretion Homo sapiens ?
-
 ?
7.2.2.19 additional information a K+ efflux channel is associated with the gastric H,K-ATPase, KCNQ1-KCNE2 appears to be the K+ efflux channel that is essential for gastric acid secretion Rattus norvegicus ?
-
 ?
7.2.2.19 additional information a K+ efflux channel is associated with the gastric H,K-ATPase, KCNQ1-KCNE2 appears to be the K+ efflux channel that is essential for gastric acid secretion Sus scrofa ?
-
 ?
7.2.2.19 additional information a K+ efflux channel is associated with the gastric H,K-ATPase, KCNQ1-KCNE2 appears to be the K+ efflux channel that is essential for gastric acid secretion Oryctolagus cuniculus ?
-
 ?
7.2.2.19 additional information a K+ efflux channel is associated with the gastric H,K-ATPase, KCNQ1-KCNE2 appears to be the K+ efflux channel that is essential for gastric acid secretion Canis lupus familiaris ?
-
 ?

Subunits

EC Number Subunits Comment Organism
7.2.2.19 heterodimer alphabeta structure, determination of the primary structure of the gastric H,K-ATPase alpha subunit containing the catalytic site, sequence comparison Homo sapiens
7.2.2.19 heterodimer alphabeta structure, determination of the primary structure of the gastric H,K-ATPase alpha subunit containing the catalytic site, sequence comparison Rattus norvegicus
7.2.2.19 heterodimer alphabeta structure, determination of the primary structure of the gastric H,K-ATPase alpha subunit containing the catalytic site, sequence comparison Sus scrofa
7.2.2.19 heterodimer alphabeta structure, determination of the primary structure of the gastric H,K-ATPase alpha subunit containing the catalytic site, sequence comparison Oryctolagus cuniculus
7.2.2.19 heterodimer alphabeta structure, determination of the primary structure of the gastric H,K-ATPase alpha subunit containing the catalytic site, sequence comparison Canis lupus familiaris
7.2.2.19 More a cluster of intramembranal carboxylic amino acids is located in the middle of the transmembrane segments TM4, TM5,TM6, and TM8 of the alpha-subunit that contains the ion binding domain in this enzyme and the ATPase Homo sapiens
7.2.2.19 More a cluster of intramembranal carboxylic amino acids is located in the middle of the transmembrane segments TM4, TM5,TM6, and TM8 of the alpha-subunit that contains the ion binding domain in this enzyme and the ATPase Rattus norvegicus
7.2.2.19 More a cluster of intramembranal carboxylic amino acids is located in the middle of the transmembrane segments TM4, TM5,TM6, and TM8 of the alpha-subunit that contains the ion binding domain in this enzyme and the ATPase Sus scrofa
7.2.2.19 More a cluster of intramembranal carboxylic amino acids is located in the middle of the transmembrane segments TM4, TM5,TM6, and TM8 of the alpha-subunit that contains the ion binding domain in this enzyme and the ATPase Oryctolagus cuniculus
7.2.2.19 More a cluster of intramembranal carboxylic amino acids is located in the middle of the transmembrane segments TM4, TM5,TM6, and TM8 of the alpha-subunit that contains the ion binding domain in this enzyme and the ATPase Canis lupus familiaris

Synonyms

EC Number Synonyms Comment Organism
7.2.2.19 gastric HK-ATPase
-
 Homo sapiens
7.2.2.19 gastric HK-ATPase
-
 Rattus norvegicus
7.2.2.19 gastric HK-ATPase
-
 Sus scrofa
7.2.2.19 gastric HK-ATPase
-
 Oryctolagus cuniculus
7.2.2.19 gastric HK-ATPase
-
 Canis lupus familiaris
7.2.2.19 More the enzyme is a member of the P2-type ATPase family Homo sapiens
7.2.2.19 More the enzyme is a member of the P2-type ATPase family Rattus norvegicus
7.2.2.19 More the enzyme is a member of the P2-type ATPase family Sus scrofa
7.2.2.19 More the enzyme is a member of the P2-type ATPase family Oryctolagus cuniculus
7.2.2.19 More the enzyme is a member of the P2-type ATPase family Canis lupus familiaris

Cofactor

EC Number Cofactor Comment Organism Structure
7.2.2.19 ATP
-
 Homo sapiens
7.2.2.19 ATP
-
 Rattus norvegicus
7.2.2.19 ATP
-
 Sus scrofa
7.2.2.19 ATP
-
 Oryctolagus cuniculus
7.2.2.19 ATP
-
 Canis lupus familiaris