Search by BoMiProt ID - Bomi44


Primary Information

BoMiProt ID Bomi44
Protein Name Sodium/potassium-transporting ATPase subunit beta-3
Organism Bos taurus
Uniprot IdQ3T0C6
Milk FractionMFGM
Ref Sequence Id NP_001030470.1
Amino Acid Lenth 279
Molecular Weight 31521
Fasta Sequence https://www.uniprot.org/uniprot/Q3T0C6.fasta
Gene Name ATP1B3
Gene Id 532844
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondry Information

Presence in other biological fluids/tissue/cells highly expressed in kidneys; brain; sperm cells express a unique Na,K-ATPase isoform
Protein Function αsubunit is responsible for the catalytic activity of the Na,K-ATPase while the ß subunit is important in the maturation and transport of the enzyme to the plasma membrane; maintains the gradient of sodium and potassium across plasma membrane; main kidney functions are to filter the blood of waste products to reabsorb glucose and amino acids, to regulate electrolytes and to maintain pH; in sperm cells - regulation of ions and membrane potential is crucial for motility and the acrosome reaction and is essential for male fertility; in brain- required to fire action potential
Biochemical Properties beta subunit has three conserved disulfide bonds in the extracellular domain, which are important for forming a stable pump; Na,K-ATPase exists as a heterodimer consisting of a large catalytic α subunit and a smaller glycoslated ß subunit; α subunit possesses eight transmembrane domains and the ß subunit only one; Ouabain binds at the permeation pathway of the Na /K ATPase
Significance in milk nutrient transport systems for milk precursors and constituents
PTMs ß domain has domain has three, eight, and two glycosylation sites in beta1, 2, and 3, respectively
Significance of PTMs Removal of the glycosylations causes retention in the endoplasmatic reticulumof beta2, but not of beta1 or 3, suggesting that the glycosylations play individual roles in the different isoforms
Linking IDs Bomi619
Bibliography 1. Jimenez, T., McDermott, J. P., Sánchez, G., & Blanco, G. (2011). Na, K-ATPase α4 isoform is essential for sperm fertility. Proceedings of the National Academy of Sciences of the United States of America, 108(2), 644–649. https://doi.org/10.1073/pnas.1016902108.
2. Tokhtaeva, E., Clifford, R. J., Kaplan, J. H., Sachs, G., & Vagin, O. (2012). Subunit isoform selectivity in assembly of Na,K-ATPase α-β heterodimers. The Journal of Biological Chemistry, 287(31), 26115–26125. https://doi.org/10.1074/jbc.M112.370734.
3. Noguchi, S., Mutoh, Y., & Kawamura, M. (1994). The functional roles of disulfide bonds in the beta-subunit of (Na,K)ATPase as studied by site-directed mutagenesis. FEBS Letters, 341(2–3), 233–238. https://doi.org/10.1016/0014-5793(94)80463-x.
4. El Mernissi, G., & Doucet, A. (1984). Quantitation of [3H]ouabain binding and turnover of Na-K-ATPase along the rabbit nephron. American Journal of Physiology-Renal Physiology, 247(1), F158–F167. https://doi.org/10.1152/ajprenal.1984.247.1.F158.
5. Sandtner, W., Egwolf, B., Khalili-Araghi, F., Sánchez-Rodríguez, J. E., Roux, B., Bezanilla, F., & Holmgren, M. (2011). Ouabain binding site in a functioning Na+/K+ ATPase. The Journal of Biological Chemistry, 286(44), 38177–38183. https://doi.org/10.1074/jbc.M111.267682.
6. Price, E. M., & Lingrel, J. B. (1988). Structure-function relationships in the Na,K-ATPase alpha subunit: site-directed mutagenesis of glutamine-111 to arginine and asparagine-122 to aspartic acid generates a ouabain-resistant enzyme. Biochemistry, 27(22), 8400–8408. https://doi.org/10.1021/bi00422a016.