Activating Compound | Comment | Organism | Structure |
---|---|---|---|
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 | |
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 | Comment | Organism | Structure |
---|---|---|---|
K-252a | a potent inhibitor of protein kinase | Arabidopsis thaliana | |
K-252a | a potent inhibitor of protein kinase | Vicia faba | |
Triton X-100 | strong inhibition | Arabidopsis thaliana | |
Triton X-100 | strong inhibition | Vicia faba |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
microsome | - |
Vicia faba | - |
- |
microsome | - |
Arabidopsis thaliana | - |
- |
plasma membrane | - |
Vicia faba | 5886 | - |
plasma membrane | - |
Arabidopsis thaliana | 5886 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Vicia faba | |
Mg2+ | required | Arabidopsis thaliana |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
95000 | - |
x * 95000, SDS-PAGE | Vicia faba |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + H+/in | Vicia faba | - |
ADP + phosphate + H+/out | - |
? | |
ATP + H2O + H+/in | Arabidopsis thaliana | - |
ADP + phosphate + H+/out | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Arabidopsis thaliana | - |
isozymes AHA1 and AHA2 | - |
Vicia faba | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
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 |
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 | Comment | Organism | Textmining |
---|---|---|---|
guard cell | - |
Vicia faba | - |
seedling | etiolated | Arabidopsis thaliana | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + H+/in | - |
Vicia faba | ADP + phosphate + H+/out | - |
? | |
ATP + H2O + H+/in | - |
Arabidopsis thaliana | ADP + phosphate + H+/out | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 95000, SDS-PAGE | Vicia faba |
Synonyms | Comment | Organism |
---|---|---|
H+-ATPase | - |
Vicia faba |
H+-ATPase | - |
Arabidopsis thaliana |
plasma membrane H+-ATPase | - |
Vicia faba |
plasma membrane H+-ATPase | - |
Arabidopsis thaliana |
General Information | Comment | Organism |
---|---|---|
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 |
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 |
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 |
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 |