title: Structure and activity of a new form of the glutamate transporter of the nematode Caenorhabditis elegans.
abstract: A Caenorhabditis elegans cDNA for a glutamate transporter was cloned and examined in this study. The predicted protein is 11 residues shorter at the N-terminus than Ceglut-1, which we previously reported. The protein, when expressed in Xenopus laevis oocytes, showed much higher glutamate transport activity than Ceglut-1, suggesting that the N-terminal sequence is critical in glutamate transport.
authors.affiliation: Suntory Institute for Bioorganic Research, Osaka, Japan. LDF01673@niftyserve.or.jp
authors.forename: T
authors.initials: T
authors.lastname: Kawano
authors.forename: K
authors.initials: K
authors.lastname: Takuwa
authors.forename: T
authors.initials: T
authors.lastname: Nakajima
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000737:chemistry* / Q000502:physiology; D000595:Amino Acid Sequence; D027322:Amino Acid Transport System X-AG; D000818:Animals; D001483:Base Sequence; D001692:Biological Transport / Q000502:physiology; D017173:Caenorhabditis elegans / Q000378:metabolism*; D003001:Cloning, Molecular; D008969:Molecular Sequence Data; D009865:Oocytes / Q000378:metabolism; D011994:Recombinant Proteins / Q000096:biosynthesis; D013329:Structure-Activity Relationship; D014982:Xenopus laevis
chemical_list: D018528:ATP-Binding Cassette Transporters; D027322:Amino Acid Transport System X-AG; D011994:Recombinant Proteins