ATP1B3

ATPase, Na+/K+ transporting, beta 3 polypeptide
Identifiers
Symbols	ATP1B3 ; ATPB-3; CD298
External IDs	OMIM: 601867 MGI: 107788 HomoloGene: 37510 ChEMBL: 3256 GeneCards: ATP1B3 Gene
EC number	3.6.3.9
Gene ontology Molecular function • ATPase activator activity • sodium:potassium-exchanging ATPase activity • ATPase binding Cellular component • plasma membrane • sodium:potassium-exchanging ATPase complex • caveola • melanosome • extracellular exosome Biological process • transport • cellular sodium ion homeostasis • blood coagulation • potassium ion import • cellular potassium ion homeostasis • positive regulation of ATPase activity • ion transmembrane transport • sodium ion export from cell • protein stabilization • leukocyte migration • transmembrane transport • protein localization to plasma membrane • membrane repolarization • positive regulation of potassium ion transmembrane transporter activity • positive regulation of sodium ion export from cell • positive regulation of potassium ion import Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	483	11933
Ensembl	ENSG00000069849	ENSMUSG00000032412
UniProt	P54709	P97370
RefSeq (mRNA)	NM_001679	NM_007502
RefSeq (protein)	NP_001670	NP_031528
Location (UCSC)	Chr 3: 141.88 – 141.93 Mb	Chr 9: 96.33 – 96.36 Mb
PubMed search

Sodium/potassium-transporting ATPase subunit beta-3 is an enzyme that in humans is encoded by the ATP1B3 gene.^[1][2][3] ATP1B3 has also been designated as CD298 (cluster of differentiation 298).

The protein encoded by this gene belongs to the family of Na+/K+ and H+/K+ ATPases beta chain proteins, 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 beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane. The glycoprotein subunit of Na+/K+ -ATPase is encoded by multiple genes. This gene encodes a beta 3 subunit. A pseudogene exists for this gene, and it is located on chromosome 2.^[3]

References

1. Malik N, Canfield VA, Beckers MC, Gros P, Levenson R (Nov 1996). "Identification of the mammalian Na,K-ATPase 3 subunit". J Biol Chem 271 (37): 22754–8. doi:10.1074/jbc.271.37.22754. PMID 8798450.
2. Malik N, Canfield V, Sanchez-Watts G, Watts AG, Scherer S, Beatty BG, Gros P, Levenson R (Mar 1998). "Structural organization and chromosomal localization of the human Na,K-ATPase beta 3 subunit gene and pseudogene". Mamm Genome 9 (2): 136–43. doi:10.1007/s003359900704. PMID 9457675.
3. "Entrez Gene: ATP1B3 ATPase, Na+/K+ transporting, beta 3 polypeptide".

Further reading

• Lingrel JB, Orlowski J, Shull MM, Price EM (1990). "Molecular genetics of Na,K-ATPase". Prog. Nucleic Acid Res. Mol. Biol. Progress in Nucleic Acid Research and Molecular Biology 38: 37–89. doi:10.1016/S0079-6603(08)60708-4. ISBN 978-0-12-540038-1. PMID 2158121.
• Jørgensen PL (1982). "Mechanism of the Na+, K+ pump. Protein structure and conformations of the pure (Na+ +K+)-ATPase". Biochim. Biophys. Acta 694 (1): 27–68. doi:10.1016/0304-4157(82)90013-2. PMID 6289898.
• Chiampanichayakul S, Szekeres A, Khunkaewla P; et al. (2003). "Engagement of Na,K-ATPase beta3 subunit by a specific mAb suppresses T and B lymphocyte activation". Int. Immunol. 14 (12): 1407–14. doi:10.1093/intimm/dxf112. PMID 12456588.
• 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. PMC 139241. PMID 12477932.
• Zhang H, Li XJ, Martin DB, Aebersold R (2003). "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry". Nat. Biotechnol. 21 (6): 660–6. doi:10.1038/nbt827. PMID 12754519.
• 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.
• 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. PMC 528928. PMID 15489334.
• Chi A, Valencia JC, Hu ZZ; et al. (2007). "Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes". J. Proteome Res. 5 (11): 3135–44. doi:10.1021/pr060363j. PMID 17081065.
• Chiampanichayakul S, Khunkaewla P, Pata S, Kasinrerk W (2007). "Na, K ATPase beta3 subunit (CD298): association with alpha subunit and expression on peripheral blood cells". Tissue Antigens 68 (6): 509–17. doi:10.1111/j.1399-0039.2006.00726.x. PMID 17176442.
• Ewing RM, Chu P, Elisma F; et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
• Aughey RJ, Murphy KT, Clark SA; et al. (2007). "Muscle Na+-K+-ATPase activity and isoform adaptations to intense interval exercise and training in well-trained athletes". J. Appl. Physiol. 103 (1): 39–47. doi:10.1152/japplphysiol.00236.2006. PMID 17446412.

External links

• ATP1B3 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.