Application | Comment | Organism |
---|---|---|
agriculture | the ability to manipulate metal transporters, such as by altering substrate specificity, is an essential step in developing genetically engineered plants that can be used for phytoremediation strategies for specific metals | Arabidopsis thaliana |
biotechnology | the ability to manipulate metal transporters, such as by altering substrate specificity, is an essential step in developing genetically engineered plants that can be used for phytoremediation strategies for specific metals | Arabidopsis thaliana |
Protein Variants | Comment | Organism |
---|---|---|
D100A | site-directed mutagenesis, substitution of Asp100 or Asp136 with Ala in IRT1 eliminates the ability of IRT1 to complement both Fe- and Mn-sensitive yeast mutants, but retains the ability to complement a Zn-sensitive yeast strain | Saccharomyces cerevisiae |
D136A | site-directed mutagenesis, substitution of Asp100 or Asp136 with Ala in IRT1 eliminates the ability of IRT1 to complement both Fe- and Mn-sensitive yeast mutants, but retains the ability to complement a Zn-sensitive yeast strain | Saccharomyces cerevisiae |
additional information | recombinant ECA1 shows ability to confer tolerance to toxic concentrations of Mn when heterologously expressed in a Mn-sensitive mutant yeast strain. The Arabidopsis IAA-leucine resistant 2 (ilr2) mutant has a slight tolerance to Mn stress. Transport characterization of microsomal membrane vesicles from ilr2 plants demonstrates a significant increase in ATP-dependent Mn2+ transport compared to wild-type plants | Arabidopsis thaliana |
R123I | site-directed mutagenesis, when Arg123 of ShMTP1 is mutated to Ile, the ability to confer Mn tolerance to either yeast or Arabidopsis is completely lost | Arabidopsis thaliana |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
endoplasmic reticulum | - |
Arabidopsis thaliana | 5783 | - |
Golgi apparatus | - |
Saccharomyces cerevisiae | 5794 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Arabidopsis thaliana | |
Mg2+ | required | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + Ca2+[side 1] | Arabidopsis thaliana | - |
ADP + phosphate + Ca2+[side 2] | - |
? | |
ATP + H2O + Ca2+[side 1] | Saccharomyces cerevisiae | - |
ADP + phosphate + Ca2+[side 2] | - |
? | |
ATP + H2O + Ca2+[side 1] | Saccharomyces cerevisiae ATCC 204508 | - |
ADP + phosphate + Ca2+[side 2] | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Arabidopsis thaliana | P92939 | - |
- |
Saccharomyces cerevisiae | P13586 | - |
- |
Saccharomyces cerevisiae ATCC 204508 | P13586 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + Ca2+[side 1] | - |
Arabidopsis thaliana | ADP + phosphate + Ca2+[side 2] | - |
? | |
ATP + H2O + Ca2+[side 1] | - |
Saccharomyces cerevisiae | ADP + phosphate + Ca2+[side 2] | - |
? | |
ATP + H2O + Ca2+[side 1] | - |
Saccharomyces cerevisiae ATCC 204508 | ADP + phosphate + Ca2+[side 2] | - |
? | |
additional information | the Arabidopsis thaliana endoplasmic reticulum-localized Ca2+-ATPase, ECA1, with homology to PMR1, can also transport Mn2+. Molecular determinants of the Mn2+ specificity of transport proteins | Arabidopsis thaliana | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
AtECA1 | - |
Arabidopsis thaliana |
Mn2+-transporting P-type ATPase | - |
Arabidopsis thaliana |
Mn2+-transporting P-type ATPase | - |
Saccharomyces cerevisiae |
More | cf. EC 7.2.2.22 | Arabidopsis thaliana |
More | cf. EC 7.2.2.22 | Saccharomyces cerevisiae |
plasma membrane ATPase related 1 | - |
Saccharomyces cerevisiae |
PMR1 | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Arabidopsis thaliana | |
ATP | - |
Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
malfunction | a T-DNA knockout of ECA1, grown on high-Mn media, displays a strong stress phenotype when compared to wild-type plants. This phenotype includes a significant reduction in fresh weight, dramatic leaf chlorosis, a significant inhibition of leaf expansion and root elongation, and a loss of root hair tip growth. The Arabidopsis IAA-leucine resistant 2 (ilr2) mutant has a slight tolerance to Mn stress. Transport characterization of microsomal membrane vesicles from ilr2 plants demonstrated a significant increase in ATP-dependent Mn2+ transport compared to wild-type plants. ILR2 might act as a regulator of Mn2+ transport, possibly acting on Mn2+ efflux from the cell mediated by either an ATPase or an ABC transporter | Arabidopsis thaliana |
metabolism | several transporter gene families have been implicated in Mn2+ transport, including cation/H+ antiporters, natural resistance-associated macrophage protein (Nramp) transporters, zinc-regulated transporter/iron-regulated transporter (ZRT/IRT1)-related protein (ZIP) transporters, the cation diffusion facilitator (CDF) transporter family, and P-type ATPases | Arabidopsis thaliana |
metabolism | several transporter gene families have been implicated in Mn2+ transport, including cation/H+ antiporters, natural resistance-associated macrophage protein (Nramp) transporters, zinc-regulated transporter/iron-regulated transporter (ZRT/IRT1)-related protein (ZIP) transporters, the cation diffusion facilitator (CDF) transporter family, and P-type ATPases | Saccharomyces cerevisiae |
additional information | a subfamily of P-type ATPases, the P1B-ATPases, catalyse transition metal efflux in many organisms including plants, and are predicted to transport either Zn2+/Cd2+/Pb2+/Co2+ or Cu2+/Ag2+, but there is no evidence that Mn2+ is a substrate for P1B-ATPases from any organism | Arabidopsis thaliana |
additional information | a subfamily of P-type ATPases, the P1B-ATPases, catalyse transition metal efflux in many organisms including plants, and are predicted to transport either Zn2+/Cd2+/Pb2+/Co2+ or Cu2+/Ag2+, but there is no evidence that Mn2+ is a substrate for P1B-ATPases from any organism | Saccharomyces cerevisiae |
physiological function | ECA1 is originally identified as Ca2+ transporter, but has subsequently been shown to also transport Mn2+. AtECA1 is an endoplasmic reticulum (ER) Ca2+- and Mn2+-transporting P-type ATPase (see also EC 7.2.2.22). Manganese (Mn) is an essential nutrient in plants. It is of particular importance in photosynthetic organisms where a cluster of Mn atoms is required as the catalytic centre for light-induced water oxidation in photosystem II, and is required as a cofactor for a variety of enzymes, such as the Mn2+-dependent superoxide dismutase (MnSOD). Mn can be particularly toxic to plant growth and a variety of mechanisms exist to overcome such toxicity, including the conversion of the metal to a metabolically inactive compound, such as a Mn2+-chelate complex, or sequestration of the Mn2+ ion or a Mn2+-chelate complex into an internal compartment such as the vacuole. At the cellular level, Mn2+ accumulates predominantly in the vacuole and to some extent in chloroplasts, and can be associated with the cell wall fraction. Mn2+ has a critical role in the water oxidation step of photosynthesis, and the chloroplast is the second-largest sink for Mn2+ in the cell | Arabidopsis thaliana |
physiological function | PMR1 is a Golgi Ca2+- and Mn2+-transporting P-type ATPase (see also EC 7.2.2.22). Manganese (Mn) is an essential nutrient in plants. It is of particular importance in photosynthetic organisms where a cluster of Mn atoms is required as the catalytic centre for light-induced water oxidation in photosystem II, and is required as a cofactor for a variety of enzymes, such as the Mn2+-dependent superoxide dismutase (MnSOD). Mn can be particularly toxic to plant growth and a variety of mechanisms exist to overcome such toxicity, including the conversion of the metal to a metabolically inactive compound, such as a Mn2+-chelate complex, or sequestration of the Mn2+ ion or a Mn2+-chelate complex into an internal compartment such as the vacuole. At the cellular level, Mn2+ accumulates predominantly in the vacuole and to some extent in chloroplasts, and can be associated with the cell wall fraction | Saccharomyces cerevisiae |