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Publication : Molecular characterization of two novel transporters from human and mouse kidney and from LLC-PK1 cells reveals a novel conserved family that is homologous to bacterial and Aspergillus nucleobase transporters.

First Author  Faaland CA Year  1998
Journal  Biochim Biophys Acta Volume  1442
Issue  2-3 Pages  353-60
PubMed ID  9804989 Mgi Jnum  J:50857
Mgi Id  MGI:1312973 Doi  10.1016/s0167-4781(98)00151-1
Citation  Faaland CA, et al. (1998) Molecular characterization of two novel transporters from human and mouse kidney and from LLC-PK1 cells reveals a novel conserved family that is homologous to bacterial and Aspergillus nucleobase transporters. Biochim Biophys Acta 1442(2-3):353-60
abstractText  Nucleobase transport is important for the metabolism of nucleic acids and antiviral and antineoplastic drugs. This transport has been functionally described in several mammalian cells but has not been well characterized molecularly. We report the cloning of two novel transporters. YSPL2 encodes a 650-residue protein and has an ubiquitous 8 kb transcript. The human and pig homologs are 95% similar. YSPL3 encodes a 598-residue protein with a 3 kb transcript that is expressed only in kidney and liver. Human YSPL2 and YSPL3 are 60% similar at the amino acid level and both show 31% similarity to the first nucleobase permease gene described in vertebrates, YSPL1. These proteins appear to be members of a new family of possible nucleobase transporters with significant sequence similarities with bacterial and Aspergillus nucleobase transporters. Further functional studies will be needed to unveil the role of these transporters in nucleic acid metabolism in normal and in disease states.
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