UDP Galactose Transporter (UGALT)

For glycosylation reactions to proceed in vivo, nucleotide sugars must be transported via a translocation mechanism from cytosol or nucleus into Golgi vesicles where glycosyltransferases function in an orderly fashion. Defects in glycosylation have been identified in Chinese hamster cells and mouse cells. The mutation in mouse cells was found to be complemented by the human X chromosome.

Ishida et al. (1996) identified an SLC35A2 splice variant, which they termed UGT2, that encodes a protein 3 amino acids longer than the 393-amino acid variant (UGT1) identified by Miura et al. (1996); the 2 proteins differ only over the last 8 residues. The UGT2 variant was able to complement the galactose transporter deficiency of the mouse Had-1 cell line.