ATP1A3

From Wikipedia, the free encyclopedia

ATPase, Na+/K+ transporting, alpha 3 polypeptide

Identifiers

ATP1A3; DYT12; MGC13276; RDP

External IDs

OMIM: 182350 MGI: 88107 HomoloGene: 49323

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:	• nucleus • cytoplasm • endoplasmic reticulum • Golgi apparatus • plasma membrane • sodium:potassium-exchanging ATPase complex • membrane • integral to membrane
Biological Process:	• transport • potassium ion transport • sodium ion transport • 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_152296 (mRNA)
NP_689509 (protein)

XM_989612 (mRNA)
XP_994706 (protein)

Location

Chr 19: 47.16 - 47.19 Mb

Chr 7: 24.69 - 24.71 Mb

Pubmed search

[1]

[2]

ATPase, Na+/K+ transporting, alpha 3 polypeptide, also known as ATP1A3, 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 3 subunit.^[1]

[edit] References

^ ^a ^b Entrez Gene: ATP1A3 ATPase, Na+/K+ transporting, alpha 3 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.
Sverdlov ED, Monastyrskaia GS, Broude NE, et al. (1988). "[The family of human Na+,K+-ATPase genes. Structure of the gene for isozyme alphaII]". Dokl. Akad. Nauk SSSR 297 (6): 1488–94. PMID 2834163.
Ovchinnikov YuA , Monastyrskaya GS, Broude NE, et al. (1988). "Family of human Na+, K+-ATPase genes. Structure of the gene for the catalytic subunit (alpha III-form) and its relationship with structural features of the protein.". FEBS Lett. 233 (1): 87–94. PMID 2838329.
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.
Harley HG, Brook JD, Jackson CL, et al. (1989). "Localization of a human Na+,K+-ATPase alpha subunit gene to chromosome 19q12----q13.2 and linkage to the myotonic dystrophy locus.". Genomics 3 (4): 380–4. PMID 2907504.
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.
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.
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.
Kramer PL, Mineta M, Klein C, et al. (1999). "Rapid-onset dystonia-parkinsonism: linkage to chromosome 19q13.". Ann. Neurol. 46 (2): 176–82. PMID 10443882.
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.
Esplin MS, Fausett MB, Faux DS, Graves SW (2003). "Changes in the isoforms of the sodium pump in the placenta and myometrium of women in labor.". Am. J. Obstet. Gynecol. 188 (3): 759–64. PMID 12634653.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
de Carvalho Aguiar P, Sweadner KJ, Penniston JT, et al. (2004). "Mutations in the Na+/K+ -ATPase alpha3 gene ATP1A3 are associated with rapid-onset dystonia parkinsonism.". Neuron 43 (2): 169–75. doi:10.1016/j.neuron.2004.06.028. PMID 15260953.
Benfante R, Antonini RA, Vaccari M, et al. (2005). "The expression of the human neuronal alpha3 Na+,K+-ATPase subunit gene is regulated by the activity of the Sp1 and NF-Y transcription factors.". Biochem. J. 386 (Pt 1): 63–72. doi:10.1042/BJ20041294. PMID 15462673.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Lim J, Hao T, Shaw C, et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration.". Cell 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569.