Polypeptide-N-Acetylgalactosaminyltransferase 10 (GALNT10)

Polypeptide GalNAc transferases (GalNAcTs; EC 2.4.1.41), such as GALNT10, initiate the synthesis of mucin-type oligosaccharides by transferring GalNAc from UDP-GalNAc to the hydroxyl group of either a serine or threonine residue on the polypeptide acceptor. The deduced type II membrane protein contains 603 amino acids. Its catalytic domain has conserved motifs for the binding of a UDP-sugar and an acceptor, and its C terminus has a lectin-like domain characteristic of GalNAcTs. GALNT10 shares 94% homology with rat GalNAcT9. Real-time PCR detected expression in all tissues tested, with highest levels in small intestine and intermediate levels in stomach, pancreas, ovary, thyroid gland, and spleen. Little to no expression was observed in other normal tissues and in most tumor cell lines examined.