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9.B.9 The Urate Transporter (UAT) Family

A single report has described a putative urate transporter (UAT) which was reported to catalyze the electrogenic efflux of urate from mammalian cells following degradation of the purine bases, adenine and guanine, to uric acid. A cDN A was isolated which encodes a protein of 322 amino acids. It is largely hydrophilic and is homologous to a family of galactose binding lectins, the galectins. The selective urate transport activity of the recombinant UAT was reconstituted in planar lipid bilayers. The protein possibly exhibits a single transmembrane α-helical spanner (TMS). In view of its dubious topology, assignment of the transport function to this protein must be considered tentative.

The proposed transport reaction catalyzed by UAT is:

urate (in) urate (out)

References associated with 9.B.9 family:

Leal-Pinto, E., W. Tao, J. Rappaport, M. Richardson, B.A. Knorr, and R.G. Abramson. (1997). Molecular cloning and functional reconstitution of a urate transporter/channel. J. Biol. Chem. 272: 617-625. 8995305
Vollmer, W., M. von Rechenberg, and J.V. Höltje. (1999). Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli. J. Biol. Chem. 274: 6726-6734. 10037771