Expression cloning of a Na(+)-independent neutral amino acid transporter from rat kidney.
Uptake of long-chain and aromatic neutral amino acids into cells is known to be catalyzed by the Na(+)-independent system L transporter, which is ubiquitous in animal cells and tissues. We have used a Xenopus oocyte expression system to clone the cDNA of a system L transporter from a rat kidney cDNA library. The 2.3-kilobase cDNA codes for a protein of 683 amino acids. The transporter has four putative membrane-spanning domains and bears no sequence or structural homology to any known animal or bacterial transporter. When transcribed and expressed in Xenopus oocytes, the transporter exhibits many, but not all, of the characteristics of L-system transporters, suggesting that this represents one of several related L-system transporters.
Tate
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Department of Biochemistry, Cornell University Medical College, New York, NY 10021.
Yan
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Udenfriend
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D000595:Amino Acid Sequence; D026905:Amino Acid Transport Systems; D000596:Amino Acids / Q000378:metabolism; D000818:Animals; D001483:Base Sequence; D001692:Biological Transport; D015152:Blotting, Northern; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics*; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D015870:Gene Expression; D007668:Kidney / Q000502:physiology; D008565:Membrane Proteins / Q000235:genetics; D008969:Molecular Sequence Data; D012333:RNA, Messenger / Q000235:genetics; D051381:Rats; D012995:Solubility; D014018:Tissue Distribution; D014982:Xenopus laevis / Q000235:genetics
D026905:Amino Acid Transport Systems; D000596:Amino Acids; D002352:Carrier Proteins; D008565:Membrane Proteins; D012333:RNA, Messenger; D004247:DNA