A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme family comprises three types of Ca2+-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum, in yeast, and in some bacteria. The enzymes from plasma membrane and from yeast have been shown to transport one ion per ATP hydrolysed whereas those from the sarcoplasmic reticulum transport two ions per ATP hydrolysed. In muscle cells Ca2+ is transported from the cytosol (side 1) into the sarcoplasmic reticulum (side 2).
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (P-type, Ca2+-transporting)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme family comprises three types of Ca2+-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum, in yeast, and in some bacteria. The enzymes from plasma membrane and from yeast have been shown to transport one ion per ATP hydrolysed whereas those from the sarcoplasmic reticulum transport two ions per ATP hydrolysed. In muscle cells Ca2+ is transported from the cytosol (side 1) into the sarcoplasmic reticulum (side 2).
plasma-membrane Ca2+-ATPase is a calcium pump that exports Ca2+ from the cytosol to the extracellular environment of eukaryotic cells and thus maintain overall Ca2+ homoeostasis and provide local control of intracellular Ca2+ signalling
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
ER-type Ca2+-ATPases show a strong preference for ATP as substrate. Conversely, auto-inhibited Ca2+-ATPases are able to use ITP or GTP as an alternative to ATP
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
plasma-membrane Ca2+-ATPase is a calcium pump that exports Ca2+ from the cytosol to the extracellular environment of eukaryotic cells and thus maintain overall Ca2+ homoeostasis and provide local control of intracellular Ca2+ signalling
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
in the resting state, the plant plasma-membrane Ca2+-ATPase is autoinhibited by binding of its N-terminal tail to two major intracellular loops. Activation requires the binding of calcium-bound calmodulin to this tail and a conformational change that displaces the autoinhibitory tail from the catalytic domain
in the resting state, the plant plasma-membrane Ca2+-ATPase is autoinhibited by binding of its N-terminal tail to two major intracellular loops. Activation requires the binding of calcium-bound calmodulin to this tail and a conformational change that displaces the autoinhibitory tail from the catalytic domain
in the resting state, the plant plasma-membrane Ca2+-ATPase is autoinhibited by binding of its N-terminal tail to two major intracellular loops. Activation requires the binding of calcium-bound calmodulin to this tail and a conformational change that displaces the autoinhibitory tail from the catalytic domain
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
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
knock-out mutants of isoform ACA9 displays reduced growth of pollen tubes, with high frequency of aborted fertilization leading to a 3fold reduction in seed set. Knock-out mutants of isoforms ACA8 or ACA10 do not have an altered phenotype, with a noticeable exception: knock-out of ACA10 in a genotype containing a naturally occurring dominant allele of an unlinked gene causes altered adult vegetative development and the formation of floral clusters. Isoform ECA1 knock-out mutant is indistinguishable from the wild type, but it clearly shows reduced root growth and toxicity symptoms when exposed to 0.5 mM Mn2+. An ECA3 knock-out mutant is not more sensitive than the wild type to Mn2+ toxicity, but rather requires higher Mn2+ concentrations for growth. Both isoform ECA1 and ECA3 knock-out mutants have slightly altered Ca2+ sensitivity
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
plasma-membrane Ca2+-ATPases, PMCAs, are high-affinity calcium pumps that expel Ca2+ from eukaryotic cells to maintain overall Ca2+ homoeostasis and to provide local control of intracellular Ca2+ signalling. They are of major physiological importance, with different isoforms being essential, for example, for presynaptic and postsynaptic Ca2+ regulation in neurons, feedback signalling in the heart and sperm motility
Ca2+-ATPases use the energy of ATP hydrolysis to pump Ca2+ from the cytoplasm into intracellular compartments or into the apoplast. Ca2+-ATPases play an important role in maintenance of cytoplasmic Ca2+ homeostasis. Isoform ECA3 may also play an essential role in Mn2+ nutrition. Plasma membrane-localized auto-inhibited Ca2+-ATPases are also involved in the response to pathogens, hormonal regulation, salt stress, and cold stress
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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant complex between calmodulin and the regulatory domain of the plasma-membrane Ca2+-ATPase ACA8, mixing of 0.0006 ml of protein solution, containing 16 mg/ml protein in 25 mM Tris, pH 7.0, 50 mM NaCl, 10 mM 2-mercaptoethanol, 5 mM CaCl2, with 0.001 ml reservoir solution, containing 2.0 M ammonium sulfate, 0.1 M CAPS, pH 10.5, 0.2 M lithium sulfate, at final pH 8.2, ar 20°C, X-ray diffraction structure determination and analysis at 3.0 A resolution
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
the mutant with 120% of wild type activity is deregulated by showing low activation by calmodulin and tryptic cleavage of the N-terminus. The mutant shows 10fold higher affinity towards calmodulin compared to the wild type enzyme
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
recombinant His6-tagged ACA8 residues 40-95, comprising the calmodulin binding site of the enzyme, from Escherichia coli by nickel affinity chromatography and gel filtration to homogeneity
expression of ACA8 residues 40-95, comprising the calmodulin binding site of the enzyme, in Escherichia coli as protein with an N-terminal fusion consisting of a His6 tag, a lipoyl domain and a TEV protease cleavage site
mutant enzymes are expressed in Saccharomyces cerevisiae strain K616 (devoid of endogenous Ca2+-ATPases) and His-tagged N-termini of wild type and mutant proteins are expressed in Escherichia coli strain DH5alpha
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
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
Meneghelli, S.; Fusca, T.; Luoni, L.; De Michelis, M.I.
Dual mechanism of activation of plant plasma membrane Ca2+-ATPase by acidic phospholipids: evidence for a phospholipid binding site which overlaps the calmodulin-binding site
Tidow, H.; Hein, K.L.; Baekgaard, L.; Palmgren, M.G.; Nissen, P.
Expression, purification, crystallization and preliminary X-ray analysis of calmodulin in complex with the regulatory domain of the plasma-membrane Ca2+-ATPase ACA8
Astegno, A.; Bonza, M.C.; Vallone, R.; La Verde, V.; D'Onofrio, M.; Luoni, L.; Molesini, B.; Dominici, P.
Arabidopsis calmodulin-like protein CML36 is a calcium (Ca2+) sensor that interacts with the plasma membrane Ca2+-ATPase isoform ACA8 and stimulates its activity