ATP1A2

From Wikipedia, the free encyclopedia

ATPase, Na+/K+ transporting, alpha 2 (+) polypeptide

PDB rendering based on 1q3i.

Available structures: 1q3i

Identifiers

Symbol(s)

ATP1A2; FHM2; MGC59864; MHP2

External IDs

OMIM: 182340 MGI: 88106 HomoloGene: 47947

Gene ontology
Molecular Function:	• nucleotide binding • magnesium ion binding • sodium:potassium-exchanging ATPase activity • 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:	• cytoplasm • microsome • plasma membrane • sodium:potassium-exchanging ATPase complex • membrane • integral to membrane
Biological Process:	• neurotransmitter uptake • transport • potassium ion transport • sodium ion transport • regulation of striated muscle contraction • metabolic process • monovalent inorganic cation transport • ATP hydrolysis coupled proton transport • sperm motility • cellular hydrogen ion homeostasis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000702 (mRNA)
NP_000693 (protein)

NM_178405 (mRNA)
NP_848492 (protein)

Location

Chr 1: 158.35 - 158.38 Mb

Chr 1: 174.11 - 174.14 Mb

Pubmed search

[1]

[2]

ATPase, Na+/K+ transporting, alpha 2 (+) polypeptide, also known as ATP1A2, 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 2 subunit.^[1]

[edit] References

^ ^a ^b Entrez Gene: ATP1A2 ATPase, Na+/K+ transporting, alpha 2 (+) 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.
Shull MM, Pugh DG, Lingrel JB (1989). "Characterization of the human Na,K-ATPase alpha 2 gene and identification of intragenic restriction fragment length polymorphisms.". J. Biol. Chem. 264 (29): 17532–43. PMID 2477373.
Sverdlov ED, Bessarab DA, Malyshev IV, et al. (1989). "Family of human Na+,K+-ATPase genes. Structure of the putative regulatory region of the alpha+-gene.". FEBS Lett. 244 (2): 481–3. PMID 2537767.
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.
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.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
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.
Stengelin MK, Hoffman JF (1997). "Na,K-ATPase subunit isoforms in human reticulocytes: evidence from reverse transcription-PCR for the presence of alpha1, alpha3, beta2, beta3, and gamma.". Proc. Natl. Acad. Sci. U.S.A. 94 (11): 5943–8. PMID 9159180.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Ducros A, Joutel A, Vahedi K, et al. (1998). "Mapping of a second locus for familial hemiplegic migraine to 1q21-q23 and evidence of further heterogeneity.". Ann. Neurol. 42 (6): 885–90. doi:10.1002/ana.410420610. PMID 9403481.
Terwindt GM, Ophoff RA, Lindhout D, et al. (1998). "Partial cosegregation of familial hemiplegic migraine and a benign familial infantile epileptic syndrome.". Epilepsia 38 (8): 915–21. PMID 9579893.
Nagase T, Ishikawa K, Suyama M, et al. (1999). "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.". DNA Res. 5 (5): 277–86. PMID 9872452.
Katzmarzyk PT, Rankinen T, Pérusse L, et al. (1999). "Linkage and association of the sodium potassium-adenosine triphosphatase alpha2 and beta1 genes with respiratory quotient and resting metabolic rate in the Québec Family Study.". J. Clin. Endocrinol. Metab. 84 (6): 2093–7. PMID 10372716.
Rankinen T, Pérusse L, Borecki I, et al. (2000). "The Na(+)-K(+)-ATPase alpha2 gene and trainability of cardiorespiratory endurance: the HERITAGE family study.". J. Appl. Physiol. 88 (1): 346–51. PMID 10642400.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Ukkola O, Joanisse DR, Tremblay A, Bouchard C (2003). "Na+-K+-ATPase alpha 2-gene and skeletal muscle characteristics in response to long-term overfeeding.". J. Appl. Physiol. 94 (5): 1870–4. doi:10.1152/japplphysiol.00942.2002. PMID 12496141.