Primary Information | |
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BoMiProt ID | Bomi619 |
Protein Name | Sodium/potassium-transporting ATPase subunit alpha-1 |
Organism | Bos taurus |
Uniprot ID | Q08DA1 |
Milk Fraction | MFGM |
Ref Sequence ID | NP_001070266.1 |
Aminoacid Length | 1021 |
Molecular Weight | 112643 |
FASTA Sequence | Download |
Gene Name | ATP1A1 |
Gene ID | 282144 |
Protein Existence Status | Reveiwed:Experimental evidence at protein level |
Secondary 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 | Bomi44 |
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. |
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | |
Predicted Disorder Regions | (1-36) |
DisProt Annotation | |
TM Helix Prediction | 10TMHs; (94-116), (128-146), (289-311), (320-342), (774-796), (800-822), (850-872), (911-933), (953-975), (981-999) |