The family of human Na,K‐ATPase genesATP1AL1 gene is transcriptionally competent and probably encodes the related ion transport ATPase

@article{Modyanov1991TheFO,
  title={The family of human Na,K‐ATPase genesATP1AL1 gene is transcriptionally competent and probably encodes the related ion transport ATPase},
  author={Nikolai N. Modyanov and K. E. Petrukhin and Vladimir E. Sverdlov and Grishin Av and Marianna Orlova and Maria B Kostina and O I Makarevich and Natalia E. Broude and Galina Sergeevna Monastyrskaya and Eugene D. Sverdlov},
  journal={FEBS Letters},
  year={1991},
  volume={278}
}
Cloning and Characterization of a New Member of the Family of Na + /K + -ATPase Genes
TLDR
The data on cloning and characterization of a new Na+/K+-ATPase α subunit related gene from rabbit is reported and two additional genes with high similarity to the α genes have been cloned and partly sequenced.
Human Nongastric H,K-ATPase: Current View On Structure And Functional Properties
TLDR
The recently discovered catalytic a-subunits of nongastric H,K-ATPases encoded by the human ATP1 AL1 (alternative name ATP12A) gene and its animal homologues represent the third distinct group.
Human nongastric H+-K+-ATPase: transport properties of ATP1al1 assembled with different beta-subunits.
TLDR
Results provide new evidence that the human nongastric H+-K+-ATPase interacts with and transports Na+ in exchange for K+ and that beta-isoforms have a distinct effect on the overall structural integrity of AL1 but influence its transport properties less than those of the Na+- K+- ATPase alpha-subunit.
Acid/Base Regulation in Renal Epithelia by H,K-ATPases
TLDR
A recent report using a genetic approach to quantify the contribution of two a-subunit isoforms of the H,K-ATPase to acid secretion has confirmed years of pharmacological studies from many laboratories and demonstrates that both iso forms of this enzyme are normally active in the CD.
Renal expression of the gene encoding the gastric H(+)-K(+)-ATPase beta-subunit.
TLDR
Analysis of RNA hybridizations, polymerase chain reaction analysis of kidney RNA, and sequence analysis of cDNAs indicate that gastric H(+)-K( +)-ATPase beta-subunit mRNA is present in kidney and probably associates with the gastric K(+-K(+)ATPases alpha-subunits and/or other P-type ATPase alpha- Subunits, thus contributing to acid-base and potassium homeostasis.
PROTON AND POTASSIUM TRANSPORT BY H+/K+‐ATPases
TLDR
The physiological and pharmacological significance of the prototypical H+/K+‐ATPase is the protein that acidifies gastric luminal contents and has led to a detailed investigation of its biochemistry and molecular and cell biology.
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References

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Multiple genes encode the human Na+,K+-ATPase catalytic subunit.
  • M. Shull, J. Lingrel
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1987
TLDR
A human genomic library was constructed and screened with hybridization probes derived from sheep and rat cDNAs encoding the alpha and alpha(+) isoforms, respectively, of the Na+,K+-ATPase catalytic subunit cDNA sequences but do not correspond to any previously identified isoforms.
Primary structure of the alpha-subunit of human Na,K-ATPase deduced from cDNA sequence.
TLDR
Total genomic Southern hybridization indicated the existence of at most two copies, possibly only one, of the gene encoding the Na,K-ATPase alpha-subunit in the human genome.
Molecular genetics of Na,K-ATPase.
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