ATP1A1

From Wikipedia, the free encyclopedia

ATPase, Na+/K+ transporting, alpha 1 polypeptide

PDB rendering based on 1mo7.

Available structures: 1mo7, 1mo8

Identifiers

Symbol(s)

ATP1A1; MGC3285; MGC51750

External IDs

OMIM: 182310 MGI: 88105 HomoloGene: 564

Gene ontology
Molecular Function:	• nucleotide binding • magnesium ion binding • 4-nitrophenylphosphatase activity • sodium:potassium-exchanging ATPase activity • protein binding • ATP binding • monovalent inorganic cation transmembrane transporter activity • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism • hydrolase activity • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances • potassium ion binding • sodium ion binding
Cellular Component:	• membrane fraction • microsome • sodium:potassium-exchanging ATPase complex • membrane • basolateral plasma membrane • sarcolemma
Biological Process:	• cardiac inotropy • transport • cation transport • potassium ion transport • sodium ion transport • metabolic process • blood pressure regulation • ATP hydrolysis coupled proton transport • sperm motility • cellular hydrogen ion homeostasis • negative regulation of heart contraction • positive regulation of heart contraction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000701 (mRNA)
NP_000692 (protein)

NM_144900 (mRNA)
NP_659149 (protein)

Location

Chr 1: 116.72 - 116.75 Mb

Chr 3: 101.71 - 101.73 Mb

Pubmed search

[1]

[2]

ATPase, Na+/K+ transporting, alpha 1 polypeptide, also known as ATP1A1, is a human gene.^[1]

The protein encoded by this gene belongs to the family of P-type cation transport ATPases, and to the subfamily of Na+/K+-ATPases. Na+/K+ -ATPase is an integral membrane protein responsible for establishing and maintaining the electrochemical gradients of Na and K ions across the plasma membrane. These gradients are essential for osmoregulation, for sodium-coupled transport of a variety of organic and inorganic molecules, and for electrical excitability of nerve and muscle. This enzyme is composed of two subunits, a large catalytic subunit (alpha) and a smaller glycoprotein subunit (beta). The catalytic subunit of Na+/K+ -ATPase is encoded by multiple genes. This gene encodes an alpha 1 subunit. Alternatively spliced transcript variants encoding different isoforms have been identified.^[1]

[edit] References

^ ^a ^b Entrez Gene: ATP1A1 ATPase, Na+/K+ transporting, alpha 1 polypeptide.

[edit] Further reading

Lingrel JB, Orlowski J, Shull MM, Price EM (1990). "Molecular genetics of Na,K-ATPase.". Prog. Nucleic Acid Res. Mol. Biol. 38: 37-89. PMID 2158121.
Dunbar LA, Caplan MJ (2001). "Ion pumps in polarized cells: sorting and regulation of the Na+, K+- and H+, K+-ATPases.". J. Biol. Chem. 276 (32): 29617-20. doi:10.1074/jbc.R100023200. PMID 11404365.
Wangemann P (2002). "K+ cycling and the endocochlear potential.". Hear. Res. 165 (1-2): 1-9. PMID 12031509.
Xie Z, Cai T (2004). "Na+-K+--ATPase-mediated signal transduction: from protein interaction to cellular function.". Mol. Interv. 3 (3): 157-68. doi:10.1124/mi.3.3.157. PMID 14993422.
Shull MM, Pugh DG, Lingrel JB (1990). "The human Na, K-ATPase alpha 1 gene: characterization of the 5'-flanking region and identification of a restriction fragment length polymorphism.". Genomics 6 (3): 451-60. PMID 1970326.
Herrera VL, Ruiz-Opazo N (1990). "Alteration of alpha 1 Na+,K(+)-ATPase 86Rb+ influx by a single amino acid substitution.". Science 249 (4972): 1023-6. PMID 1975705.
Kawakami K, Ohta T, Nojima H, Nagano K (1986). "Primary structure of the alpha-subunit of human Na,K-ATPase deduced from cDNA sequence.". J. Biochem. 100 (2): 389-97. PMID 2430951.
Yang-Feng TL, Schneider JW, Lindgren V, et al. (1988). "Chromosomal localization of human Na+, K+-ATPase alpha- and beta-subunit genes.". Genomics 2 (2): 128-38. PMID 2842249.
Sverdlov ED, Broude NE, Sverdlov VE, et al. (1987). "Family of Na+,K+-ATPase genes. Intra-individual tissue-specific restriction fragment length polymorphism.". FEBS Lett. 221 (1): 129-33. PMID 2887455.
Chehab FF, Kan YW, Law ML, et al. (1987). "Human placental Na+,K+-ATPase alpha subunit: cDNA cloning, tissue expression, DNA polymorphism, and chromosomal localization.". Proc. Natl. Acad. Sci. U.S.A. 84 (22): 7901-5. PMID 2891135.
Ovchinnikov YuA , Monastyrskaya GS, Broude NE, et al. (1987). "The family of human Na+,K+-ATPase genes. A partial nucleotide sequence related to the alpha-subunit.". FEBS Lett. 213 (1): 73-80. PMID 3030810.
Shull MM, Lingrel JB (1987). "Multiple genes encode the human Na+,K+-ATPase catalytic subunit.". Proc. Natl. Acad. Sci. U.S.A. 84 (12): 4039-43. PMID 3035563.
Sverdlov ED, Monastyrskaya GS, Broude NE, et al. (1987). "The family of human Na+,K+-ATPase genes. No less than five genes and/or pseudogenes related to the alpha-subunit.". FEBS Lett. 217 (2): 275-8. PMID 3036582.
Ruiz A, Bhat SP, Bok D (1995). "Characterization and quantification of full-length and truncated Na,K-ATPase alpha 1 and beta 1 RNA transcripts expressed in human retinal pigment epithelium.". Gene 155 (2): 179-84. PMID 7536695.
Hundal HS, Maxwell DL, Ahmed A, et al. (1995). "Subcellular distribution and immunocytochemical localization of Na,K-ATPase subunit isoforms in human skeletal muscle.". Mol. Membr. Biol. 11 (4): 255-62. PMID 7711835.
Feschenko MS, Sweadner KJ (1995). "Structural basis for species-specific differences in the phosphorylation of Na,K-ATPase by protein kinase C.". J. Biol. Chem. 270 (23): 14072-7. PMID 7775468.
Ruiz-Opazo N, Barany F, Hirayama K, Herrera VL (1994). "Confirmation of mutant alpha 1 Na,K-ATPase gene and transcript in Dahl salt-sensitive/JR rats.". Hypertension 24 (3): 260-70. PMID 8082931.
Zahler R, Gilmore-Hebert M, Baldwin JC, et al. (1993). "Expression of alpha isoforms of the Na,K-ATPase in human heart.". Biochim. Biophys. Acta 1149 (2): 189-94. PMID 8391840.
Wang J, Schwinger RH, Frank K, et al. (1996). "Regional expression of sodium pump subunits isoforms and Na+-Ca++ exchanger in the human heart.". J. Clin. Invest. 98 (7): 1650-8. PMID 8833915.