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http://purl.uniprot.org/citations/10373490http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10373490http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10373490http://www.w3.org/2000/01/rdf-schema#comment"The product of the FEN2 gene of Saccharomyces cerevisiae has previously been described as a protein conferring sensitivity to the antifungal agent fenpropimorph. Fen2p was postulated to act as a common regulator of carbon and nitrogen catabolite repression and of amino acid and ergosterol biosynthesis. In this paper, we present experimental evidence characterizing Fen2p as a plasma membrane-localized transporter for the vitamin pantothenate. The high affinity transport system (Km = 3.5 microM) is sensitive to uncouplers, suggesting a H+-pantothenate cotransport. Pantothenate transport rates in yeast are modulated by extracellular pantothenate, being maximal at low pantothenate concentrations. It is demonstrated that beta-alanine can suppress the growth defect of FEN2 wild-type and fen2 mutant cells on pantothenate-free medium. Evidence is presented that beta-alanine is transported by the general amino acid permease Gap1p. The relation among pantothenate transport, nitrogen catabolite repression, and sensitivity to the antifungal agent fenpropimorph is discussed."xsd:string
http://purl.uniprot.org/citations/10373490http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.26.18747"xsd:string
http://purl.uniprot.org/citations/10373490http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.26.18747"xsd:string
http://purl.uniprot.org/citations/10373490http://purl.uniprot.org/core/author"Sauer N."xsd:string
http://purl.uniprot.org/citations/10373490http://purl.uniprot.org/core/author"Sauer N."xsd:string
http://purl.uniprot.org/citations/10373490http://purl.uniprot.org/core/author"Stolz J."xsd:string
http://purl.uniprot.org/citations/10373490http://purl.uniprot.org/core/author"Stolz J."xsd:string
http://purl.uniprot.org/citations/10373490http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10373490http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10373490http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10373490http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10373490http://purl.uniprot.org/core/pages"18747-18752"xsd:string
http://purl.uniprot.org/citations/10373490http://purl.uniprot.org/core/pages"18747-18752"xsd:string
http://purl.uniprot.org/citations/10373490http://purl.uniprot.org/core/title"The fenpropimorph resistance gene FEN2 from Saccharomyces cerevisiae encodes a plasma membrane H+-pantothenate symporter."xsd:string
http://purl.uniprot.org/citations/10373490http://purl.uniprot.org/core/title"The fenpropimorph resistance gene FEN2 from Saccharomyces cerevisiae encodes a plasma membrane H+-pantothenate symporter."xsd:string
http://purl.uniprot.org/citations/10373490http://purl.uniprot.org/core/volume"274"xsd:string
http://purl.uniprot.org/citations/10373490http://purl.uniprot.org/core/volume"274"xsd:string
http://purl.uniprot.org/citations/10373490http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10373490
http://purl.uniprot.org/citations/10373490http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10373490
http://purl.uniprot.org/citations/10373490http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10373490
http://purl.uniprot.org/citations/10373490http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10373490
http://purl.uniprot.org/uniprot/P19145http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10373490
http://purl.uniprot.org/uniprot/P25621http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10373490