Abstract
Molecular aspects of the diversity of P-type ATPases are explored in this review. From the substrate specificities among different ATPase molecules, the existence of isoforms within a single class of pump becomes evident and it is now recognized as a universal phenomenon. From the phylogenetic analyses using a vast collection of the deduced amino acid sequences for the P-type ATPase subunits, it also becomes evident that the divergence of substrate-specificity occurred early in the evolution and has been conserved ever since. Further extensive analyses identify a set of novel isoforms that retain an ancestral characteristic of the Na+/K+-(H+/K+-)ATPases in invertebrates.
MeSH terms
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Amino Acid Sequence
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Animals
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Calcium-Transporting ATPases / chemistry
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Calcium-Transporting ATPases / classification
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Calcium-Transporting ATPases / genetics*
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Calcium-Transporting ATPases / metabolism
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Catalytic Domain
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Evolution, Molecular*
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H(+)-K(+)-Exchanging ATPase / chemistry
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H(+)-K(+)-Exchanging ATPase / classification
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H(+)-K(+)-Exchanging ATPase / genetics*
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H(+)-K(+)-Exchanging ATPase / metabolism
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Humans
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Isoenzymes / genetics
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Models, Molecular
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Molecular Sequence Data
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Phylogeny
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Protein Subunits
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Sequence Alignment
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Sodium-Potassium-Exchanging ATPase / chemistry
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Sodium-Potassium-Exchanging ATPase / classification
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Sodium-Potassium-Exchanging ATPase / genetics*
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Sodium-Potassium-Exchanging ATPase / metabolism
Substances
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Isoenzymes
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Protein Subunits
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H(+)-K(+)-Exchanging ATPase
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Calcium-Transporting ATPases
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Sodium-Potassium-Exchanging ATPase