|CD298||ATP1β3 (Na/K ATPase β3-subunit)|
|Molecule Type||Antigen Expression||Molecular Weight|
Min / Max
|Non-lineage Restricted Molecule|
Type 2 glycoprotein
|32 / 32|
|CD298 is expressed on all leukocytes. Studies with non-hemopoietic cell lines suggest the protein is also expressed by many other tissues. Expression is high in CNS and testis.|
|MOLECULAR FAMILY NAME: Belongs to the ATPase β-chain family.|
CD298 is a single-pass type-2 279 aa integral glycoprotein. It contains a 223 aa extracellular domain containing 2 potential N-linked glycosylation sites, a 21 aa 1 putative transmembrane domain and a 35 aa cytoplasmic domain. The protein belongs to the family of Na/K and H/K ATPases β chain proteins, and to the subfamily of Na/K -ATPases. CD298 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 three subunits, a large catalytic subunit (α) and a smaller glycoprotein subunit (β) and a γ subunit. The β subunit regulates, through assembly of α/β heterodimers, the number of sodium pumps transported to the plasma membrane. The glycoprotein subunit of CD298 is encoded by multiple genes. This gene encodes a β3 subunit. A pseudogene exists for this gene.
POST-TRANSCRIPTIONAL MODIFICATION: No information.
CD298 has 2 potential N-linked glycosylation sites.
|LIGANDS AND MOLECULE ASSOCIATES WITH CD298|
CD298 dimerizes with ATPα1, 2 or 3.
|CD298 (N/K ATPase) is a membrane localized enzyme involved in Na/K transport. Its expression is induced in leukocytes upon activation. The function of the CD298 is a non-catalytic component to exchange and transport sodium and potassium ions across the cell membrane. This protein is made up of a catalytic α subunit and a β subunit. Both subunits are required for the functionally active enzyme. Three β subunit isoforms have been identified. The combination of the various α and β subunits is thought to regulate/modify enzymatic activity of the heterodimer. The specific role of the non-catalytic β-chain is not known. |
BIOCHEMICAL ACTIVITY: No information.
DISEASE RELEVANCE AND FUNCTION OF CD298 IN INTACT ANIMAL: No information.
PROTEINS AND DNA ELEMENTS WHICH REGULATE TRANSCRIPTION OF CD298: No information.
SUBSTRATES: No information.
ENZYMES WHICH MODIFY CD298: No information.
For further information see Malik, N. et al (1996) J. Biol. Chem. 271 22754-22758.
Database accession numbers
Revised June 25, 2008