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Literature summary extracted from

  • Hayashi, Y.; Nakamura, S.; Takemiya, A.; Takahashi, Y.; Shimazaki, K.; Kinoshita, T.
    Biochemical characterization of in vitro phosphorylation and dephosphorylation of the plasma membrane H+-ATPase (2010), Plant Cell Physiol., 51, 1186-1196.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
7.1.2.1 additional information the plasma membrane H + -ATPase is activated via phosphorylation of the penultimate threonine in the C-terminus leading to subsequent binding of a 14-3-3 protein Vicia faba
7.1.2.1 additional information the plasma membrane H + -ATPase is activated via phosphorylation of the penultimate threonine in the C-terminus leading to subsequent binding of a 14-3-3 protein Arabidopsis thaliana

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.1.2.1 K-252a a potent inhibitor of protein kinase Arabidopsis thaliana
7.1.2.1 K-252a a potent inhibitor of protein kinase Vicia faba
7.1.2.1 Triton X-100 strong inhibition Arabidopsis thaliana
7.1.2.1 Triton X-100 strong inhibition Vicia faba

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.2.1 microsome
-
 Vicia faba
-
-
7.1.2.1 microsome
-
 Arabidopsis thaliana
-
-
7.1.2.1 plasma membrane
-
 Vicia faba 5886
-
7.1.2.1 plasma membrane
-
 Arabidopsis thaliana 5886
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.1.2.1 Mg2+ required Vicia faba
7.1.2.1 Mg2+ required Arabidopsis thaliana

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
7.1.2.1 95000
-
 x * 95000, SDS-PAGE Vicia faba

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.1.2.1 ATP + H2O + H+/in Vicia faba
-
 ADP + phosphate + H+/out
-
 ?
7.1.2.1 ATP + H2O + H+/in Arabidopsis thaliana
-
 ADP + phosphate + H+/out
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.1.2.1 Arabidopsis thaliana
-
 isozymes AHA1 and AHA2
-
7.1.2.1 Vicia faba
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
7.1.2.1 phosphoprotein the plasma membrane H+-ATPase is activated via phosphorylation of the penultimate threonine in the C-terminus leading to subsequent binding of a 14-3-3 protein. H+-ATPase is phosphorylated in vitro on the penultimate threonine in the C-terminus in isolated microsomes from guard cell protoplasts of Vicia faba. Phosphorylated H+-ATPase is dephosphorylated in vitro, dephosphorylation is inhibited by EDTA, but not by calyculin A, an inhibitor of type 1 and 2A protein phosphatases. Dephosphorylation requires Mg2+ but not Ca2+ Vicia faba
7.1.2.1 phosphoprotein the plasma membrane H+-ATPase is activated via phosphorylation of the penultimate threonine in the C-terminus leading to subsequent binding of a 14-3-3 protein. H+-ATPase is phosphorylated in vitro on the penultimate threonine in the C-terminus in isolated microsomes from guard cell protoplasts of Vicia faba. Phosphorylated H+-ATPase is dephosphorylated in vitro, dephosphorylation is inhibited by EDTA, but not by calyculin A, an inhibitor of type 1 and 2A protein phosphatases. Dephosphorylation requires Mg2+ but not Ca2+ Arabidopsis thaliana

Source Tissue

EC Number Source Tissue Comment Organism Textmining
7.1.2.1 guard cell
-
 Vicia faba
-
7.1.2.1 seedling etiolated Arabidopsis thaliana
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.2.1 ATP + H2O + H+/in
-
 Vicia faba ADP + phosphate + H+/out
-
 ?
7.1.2.1 ATP + H2O + H+/in
-
 Arabidopsis thaliana ADP + phosphate + H+/out
-
 ?

Subunits

EC Number Subunits Comment Organism
7.1.2.1 ? x * 95000, SDS-PAGE Vicia faba

Synonyms

EC Number Synonyms Comment Organism
7.1.2.1 H+-ATPase
-
 Vicia faba
7.1.2.1 H+-ATPase
-
 Arabidopsis thaliana
7.1.2.1 plasma membrane H+-ATPase
-
 Vicia faba
7.1.2.1 plasma membrane H+-ATPase
-
 Arabidopsis thaliana

General Information

EC Number General Information Comment Organism
7.1.2.1 additional information a protein kinase-phosphatase pair, K-252a-insensitive protein kinase and Mg2+ -dependent type 2C protein phosphatase, co-localizes at least in part with the H+-ATPase in the plasma membrane and regulates the phosphorylation status of the penultimate threonine of the H+-ATPase Vicia faba
7.1.2.1 additional information a protein kinase-phosphatase pair, K-252a-insensitive protein kinase and Mg2+ -dependent type 2C protein phosphatase, co-localizes at least in part with the H+-ATPase in the plasma membrane and regulates the phosphorylation status of the penultimate threonine of the H+-ATPase Arabidopsis thaliana
7.1.2.1 physiological function the plasma membrane H + -ATPase drives the stomatal opening, which is mediated by blue light receptor phototropins, by activation of via phosphorylation of the penultimate threonine in the C-terminus and subsequent binding of a 14-3-3 protein Vicia faba
7.1.2.1 physiological function the plasma membrane H + -ATPase drives the stomatal opening, which is mediated by blue light receptor phototropins, by activation of via phosphorylation of the penultimate threonine in the C-terminus and subsequent binding of a 14-3-3 protein Arabidopsis thaliana