Sialyltransferase 10 (SIAT10)

Sialyltransferases, such as ST3GAL6, catalyze the transfer of sialic acid from cytidine 5-prime monophospho-N-acetylneuraminic acid (CMP-NeuAc) to terminal positions of glycoprotein and glycolipid carbohydrate groups. Terminal NeuAc residues are key determinants of carbohydrate structures, such as the sialyl-Lewis X determinants, and are widely distributed in many cell types.The deduced 331-amino acid protein has a calculated molecular mass of about 38 kD. It contains an N-terminal type II transmembrane domain, 2 sialylmotifs, a C-terminal motif conserved among ST3GAL subfamily members, and 6 potential N-linked glycosylation sites. The ST3GALVI protein shares 38%, 34%, and 33% identity with ST3GALIV, ST3GALIII, and mouse St3galv, respectively.