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http://purl.uniprot.org/citations/8618839http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8618839http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8618839http://www.w3.org/2000/01/rdf-schema#comment"In most plants amino acids represent the major transport form for organic nitrogen. A sensitive selection system in yeast mutants has allowed identification of a previously unidentified amino acid transporter in Arabidopsis. AAT1 encodes a hydrophobic membrane protein with 14 membrane-spanning regions and shares homologies with the ecotropic murine leukemia virus receptor, a bifunctional protein serving also as a cationic amino acid transporter in mammals. When expressed in yeast, AAT1 mediates high-affinity transport of basic amino acids, but to a lower extent also recognizes acidic and neutral amino acids. AAT1-mediated histidine transport is sensitive to protonophores and occurs against a concentration gradient, indicating that AAT1 may function as a proton symporter. AAT1 is specifically expressed in major veins of leaves and roots and in various floral tissues--i.e., and developing seeds."xsd:string
http://purl.uniprot.org/citations/8618839http://purl.org/dc/terms/identifier"doi:10.1073/pnas.92.26.12036"xsd:string
http://purl.uniprot.org/citations/8618839http://purl.org/dc/terms/identifier"doi:10.1073/pnas.92.26.12036"xsd:string
http://purl.uniprot.org/citations/8618839http://purl.uniprot.org/core/author"Frommer W.B."xsd:string
http://purl.uniprot.org/citations/8618839http://purl.uniprot.org/core/author"Frommer W.B."xsd:string
http://purl.uniprot.org/citations/8618839http://purl.uniprot.org/core/author"Hummel S."xsd:string
http://purl.uniprot.org/citations/8618839http://purl.uniprot.org/core/author"Hummel S."xsd:string
http://purl.uniprot.org/citations/8618839http://purl.uniprot.org/core/author"Ninnemann O."xsd:string
http://purl.uniprot.org/citations/8618839http://purl.uniprot.org/core/author"Ninnemann O."xsd:string
http://purl.uniprot.org/citations/8618839http://purl.uniprot.org/core/author"Unseld M."xsd:string
http://purl.uniprot.org/citations/8618839http://purl.uniprot.org/core/author"Unseld M."xsd:string
http://purl.uniprot.org/citations/8618839http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/8618839http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/8618839http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/8618839http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/8618839http://purl.uniprot.org/core/pages"12036-12040"xsd:string
http://purl.uniprot.org/citations/8618839http://purl.uniprot.org/core/pages"12036-12040"xsd:string
http://purl.uniprot.org/citations/8618839http://purl.uniprot.org/core/title"Seed and vascular expression of a high-affinity transporter for cationic amino acids in Arabidopsis."xsd:string
http://purl.uniprot.org/citations/8618839http://purl.uniprot.org/core/title"Seed and vascular expression of a high-affinity transporter for cationic amino acids in Arabidopsis."xsd:string
http://purl.uniprot.org/citations/8618839http://purl.uniprot.org/core/volume"92"xsd:string
http://purl.uniprot.org/citations/8618839http://purl.uniprot.org/core/volume"92"xsd:string
http://purl.uniprot.org/citations/8618839http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8618839
http://purl.uniprot.org/citations/8618839http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8618839