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http://purl.uniprot.org/citations/9430707http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9430707http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9430707http://www.w3.org/2000/01/rdf-schema#comment"Two genes isolated from Schwanniomyces occidentalis, ENA1 and ENA2, encode P-type ATPases highly homologous to the Na-ATPases of Saccharomyces cerevisiae and complement the Na+ sensitivity of an S. cerevisiae mutant strain lacking its own Na-ATPases. The expression of both ENA1 and ENA2 was highly dependent on a high external pH, but whereas a high pH was sufficient for the expression of ENA2, the expression of ENA1 required a high pH and the presence of Na+. Disruption of ENA1 rendered the cells less tolerant to Na+ than the wild-type strain and decreased their capacity for Na+ extrusion. Disruption of ENA2 did not affect Na+ tolerance, but decreased both the growth at high pH and K+ efflux. We discuss these results and propose that fungal Na-ATPases should be considered alkali cation ATPases. By sequence comparison, we found that fungal Na-ATPases form a homogeneous group that can be distinguished from other cation-pumping P-type ATPases, except from the cta3 Ca-ATPase of Schizosaccharomyces pombe."xsd:string
http://purl.uniprot.org/citations/9430707http://purl.org/dc/terms/identifier"doi:10.1074/jbc.273.3.1640"xsd:string
http://purl.uniprot.org/citations/9430707http://purl.org/dc/terms/identifier"doi:10.1074/jbc.273.3.1640"xsd:string
http://purl.uniprot.org/citations/9430707http://purl.uniprot.org/core/author"Rodriguez-Navarro A."xsd:string
http://purl.uniprot.org/citations/9430707http://purl.uniprot.org/core/author"Rodriguez-Navarro A."xsd:string
http://purl.uniprot.org/citations/9430707http://purl.uniprot.org/core/author"Banuelos M.A."xsd:string
http://purl.uniprot.org/citations/9430707http://purl.uniprot.org/core/author"Banuelos M.A."xsd:string
http://purl.uniprot.org/citations/9430707http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9430707http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9430707http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9430707http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9430707http://purl.uniprot.org/core/pages"1640-1646"xsd:string
http://purl.uniprot.org/citations/9430707http://purl.uniprot.org/core/pages"1640-1646"xsd:string
http://purl.uniprot.org/citations/9430707http://purl.uniprot.org/core/title"P-type ATPases mediate sodium and potassium effluxes in Schwanniomyces occidentalis."xsd:string
http://purl.uniprot.org/citations/9430707http://purl.uniprot.org/core/title"P-type ATPases mediate sodium and potassium effluxes in Schwanniomyces occidentalis."xsd:string
http://purl.uniprot.org/citations/9430707http://purl.uniprot.org/core/volume"273"xsd:string
http://purl.uniprot.org/citations/9430707http://purl.uniprot.org/core/volume"273"xsd:string
http://purl.uniprot.org/citations/9430707http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9430707
http://purl.uniprot.org/citations/9430707http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9430707
http://purl.uniprot.org/citations/9430707http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9430707
http://purl.uniprot.org/citations/9430707http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9430707
http://purl.uniprot.org/uniprot/O13397http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9430707
http://purl.uniprot.org/uniprot/O13398http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9430707