Primary structure, functional characteristics and tissue expression pattern of human ATA2, a subtype of amino acid transport system A.

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Citation

Hatanaka T, Huang W, Wang H, Sugawara M, Prasad PD, Leibach FH, Ganapathy V

Primary structure, functional characteristics and tissue expression pattern of human ATA2, a subtype of amino acid transport system A.

Biochim Biophys Acta. 2000 Jul 31;1467(1):1-6. doi: 10.1016/s0005-2736(00)00252-2.

PubMed ID
10930503 [ View in PubMed
]
Abstract

We report here on the primary structure and functional characteristics of the protein responsible for the system A amino acid transport activity that is known to be expressed in most human tissues. This transporter, designated ATA2 for amino acid transporter A2, was cloned from the human hepatoma cell line HepG2. Human ATA2 (hATA2) consists of 506 amino acids and exhibits a high degree of homology to rat ATA2. hATA2-specific mRNA is ubiquitously expressed in human tissues. When expressed in mammalian cells, hATA2 mediates Na+-dependent transport of alpha-(methylamino)isobutyric acid, a specific model substrate for system A. The transporter is specific for neutral amino acids. It is pH-sensitive and Li+-intolerant. The Na+:amino acid stoichiometry is 1:1.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Sodium-coupled neutral amino acid transporter 2Q96QD8Details