Introduction of ATP1B3
Human β3 subunit of Na(+)/K(+)-ATPase (ATP1B3) is an enzyme that in humans is encoded by the ATP1B3 gene. ATP1B3 belongs to the family of Na(+)/K(+) and H(+)/K(+) ATPases beta chain proteins, which are plasma membrane pumps with numerous physiologic functions. Mapped to chromosome 3q23, ATP1B3 gene encodes the beta subunit of Na(+)/K(+)-ATPase, which is responsible for the formation and structural integrity of the Na+/K+ ATPase holoenzyme. There is a pseudogene for ATP1B3 located on chromosome 2.
|Basic Information of ATP1B3|
|Protein Name||Sodium/potassium-transporting ATPase subunit beta-3|
|Aliases||Sodium/potassium-dependent ATPase subunit beta-3|
|Organism||Homo sapiens (Human)|
Function of ATP1B3 Membrane Protein
Widely distributed in prokaryotic and eukaryotic cells, Na(+)/K(+)-ATPase has been well acknowledged to play essential roles for osmoregulation, for sodium-coupled transport of a variety of organic and inorganic molecules, and for electrical excitability of nerve and muscle. As a key component of Na(+)/K(+)-ATPase, ATP1B3 is key for establishing and maintaining the electrochemical gradients of Na and K ions across the plasma membrane. Various researches have demonstrated that ATP1B3 can up-regulate lymphocyte activity and promote the production of IFN-γ, IL-2, IL-4, and IL-10, suggesting that ATP1B3 might act as a potential therapeutic target in virus infection. It is documented that ATP1B3 is a co-factor that accelerates BST-2 degradation and reduces BST-2-mediated restriction of HIV-1 production and NF-κB activation. The C-terminal part of ATP1B3 folds into an immunoglobulin-like domain, which may play a role in cell adhesion.
Fig.1 Structure of Na(+)/K(+)-ATPase. (Pieper U, 2014)
Application of ATP1B3 Membrane Protein in Literature
This article demonstrates that ATP1B3 repress EV71 replication by promoting the production of type-I interferons, meaning that knockdown of ATP1B3 can obviously enhance the replication of EV71, whereas overexpression of ATP1B3 obviously represses the replication of EV71 in RD cells. The results suggest that ATP1B3 can act as a potential therapeutic target in EV71 infection.
This article demonstrates that ATP1B3 silencing can lead to the high-level expression of BST-2 on the surface of HeLa cells, which indicates that ATP1B3 may be a co-factor that promotes BST-2 degradation and weakens BST-2-mediated restriction of NF-κB activation and HIV-1 production.
This article indicates that the quantity of ATP1B3 in the plasma membrane is mediated by the cell density, which suggests the general involvement of the β-subunits in cell-cell adhesion, supported by the possibility that the β-subunit extracellular domain may possess the Ig-fold structure for cell-cell adhesion.
This demonstrates that down-regulation of the β1- and β3-chains (ATP1B1 and ATP1B3) of the Na/K-ATPase do not affect the secretion of FGF2, suggesting that they are not associated with this process.
This article reveals that mutations within the gene coding for the beta3 subunit of the Na+, K+-ATPase pump (Atp1b3) have a connection with the inter-strain differences in the early phase formalin pain behavior.
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