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http://purl.uniprot.org/citations/7485470http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7485470http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7485470http://www.w3.org/2000/01/rdf-schema#comment"The cDNA for ATP1AL1, the fifth member of the human Na-K-adenosinetriphosphatase (ATPase)/H-K-ATPase gene family, was recently cloned (A. V. Grishin, V. E. Sverdlov, M. B. Kostina, and N. N. Modyanov. FEBS Lett. 349: 144-150, 1994). The encoded protein (ATP1AL1) has all the primary structural features common to the catalytic alpha-subunit of ion-transporting P-type ATPases and is similar (63-64% identity) to the Na-K-ATPase alpha-subunit isoforms and the gastric H-K-ATPase alpha-subunit. In this study, ATP1AL1 was expressed in Xenopus laevis oocytes in combination with the beta-subunit of rabbit gastric H-K-ATPase. The functional properties of the stable alpha/beta-complex were studied by 86Rb+ uptake and demonstrated that ATP1AL1 is a novel human K(+)-dependent ATPase [apparent half-constant activation/(K1/2) for K+ approximately 375 microM)]. ATP1AL1-mediated inward K+ transport was inhibited by ouabain (inhibition constant approximately 13 microM) and was found to be inhibited by high concentrations of SCH-28080 (approximately 70% at 500 microM). ATP1AL1 expression resulted in the alkalinization of the oocytes' cytoplasm and ouabain-sensitive proton extrusion, as measured with pH-sensitive microelectrodes. These data argue that ATP1AL1 is the catalytic alpha-subunit of a human nongastric P-type ATPase capable of exchanging extracellular potassium for intracellular protons."xsd:string
http://purl.uniprot.org/citations/7485470http://purl.org/dc/terms/identifier"doi:10.1152/ajpcell.1995.269.4.c992"xsd:string
http://purl.uniprot.org/citations/7485470http://purl.org/dc/terms/identifier"doi:10.1152/ajpcell.1995.269.4.c992"xsd:string
http://purl.uniprot.org/citations/7485470http://purl.uniprot.org/core/author"Modyanov N.N."xsd:string
http://purl.uniprot.org/citations/7485470http://purl.uniprot.org/core/author"Modyanov N.N."xsd:string
http://purl.uniprot.org/citations/7485470http://purl.uniprot.org/core/author"Beguin P."xsd:string
http://purl.uniprot.org/citations/7485470http://purl.uniprot.org/core/author"Beguin P."xsd:string
http://purl.uniprot.org/citations/7485470http://purl.uniprot.org/core/author"Beggah A.T."xsd:string
http://purl.uniprot.org/citations/7485470http://purl.uniprot.org/core/author"Beggah A.T."xsd:string
http://purl.uniprot.org/citations/7485470http://purl.uniprot.org/core/author"Geering K."xsd:string
http://purl.uniprot.org/citations/7485470http://purl.uniprot.org/core/author"Geering K."xsd:string
http://purl.uniprot.org/citations/7485470http://purl.uniprot.org/core/author"Grishin A.V."xsd:string
http://purl.uniprot.org/citations/7485470http://purl.uniprot.org/core/author"Grishin A.V."xsd:string
http://purl.uniprot.org/citations/7485470http://purl.uniprot.org/core/author"Horisberger J.D."xsd:string
http://purl.uniprot.org/citations/7485470http://purl.uniprot.org/core/author"Horisberger J.D."xsd:string
http://purl.uniprot.org/citations/7485470http://purl.uniprot.org/core/author"Mathews P.M."xsd:string
http://purl.uniprot.org/citations/7485470http://purl.uniprot.org/core/author"Mathews P.M."xsd:string
http://purl.uniprot.org/citations/7485470http://purl.uniprot.org/core/author"Rossier B.C."xsd:string
http://purl.uniprot.org/citations/7485470http://purl.uniprot.org/core/author"Rossier B.C."xsd:string
http://purl.uniprot.org/citations/7485470http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7485470http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7485470http://purl.uniprot.org/core/name"Am. J. Physiol."xsd:string
http://purl.uniprot.org/citations/7485470http://purl.uniprot.org/core/name"Am. J. Physiol."xsd:string