Abstract
The P-type ATPases comprise a large number of highly diverse transport ATPases that are predominantly involved in the active transport of cations across biological membranes. All of these ion pumps share a common feature: formation of a phosphorylated intermediate during the reaction cycle (26,39). Different K+-dependent animal ATPases (X,K-ATPases) are the most closely related among various P-type ATPases. All of the known X,K-ATPases function as cation exchangers that pump K+ into the cell and Na+ or H+ out of the cell. X,K-ATPases exhibit a much higher level of sequence homology between their catalytic α-subunits than with other P-ATPases, and contain a second component, a ß-subunit which is absent in other P-ATPases (26,39,53). The catalytic α-subunits are large polytopic proteins (~110 kDa) with 10 transmembrane segments and contain most of the ATPase functional domains such as the ATP-hydrolyzing center and the binding sites for cations and specific inhibitors (8,26,53). The glycosylated ß-subunits (core protein ~ 30–35 kDa) have a relatively short cytoplasmic N-terminal domain, a single transmembrane segment, and a large ectodomain containing three conserved disulfide bridges and several carbohydrate chains (11,19). The X,K-ATPase family combines three distinct groups of ion pumps. Two groups, one consisting of the Na,K-ATPase isozymes formed by four α three ß isoforms and the second which includes the gastric H,K-ATPase, have long been known and studied extensively (26,53). The recently discovered catalytic a-subunits of nongastric H,K-ATPases encoded by the human ATP1 AL1 (alternative name ATP12A) gene and its animal homologues represent the third distinct group (23,27,36).
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Adams, G., Tillekeratne, M., Pestov, N.B., Modyanov, N.N. (2002). Human Nongastric H,K-ATPase: Current View On Structure And Functional Properties. In: Urushidani, T., Forte, J.G., Sachs, G. (eds) Mechanisms and Consequences of Proton Transport. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0971-4_2
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