Sialyltransferase 2 (SIAT2)

Sialyltransferases, such as ST6GAL2, are type II transmembrane proteins that catalyze the transfer of sialic acid from CMP-sialic acid to an acceptor carbohydrate, usually to the terminal ends of carbohydrate chains.The deduced 529-amino acid protein has a calculated molecular mass of 60.2 kD. ST6GalII contains an N-terminal hydrophobic sequence characteristic of type 2 transmembrane proteins followed by a stem region, and sialyl motifs L (long), S (short), and VS (very short). The VS motif contains the his and glu residues conserved among mammalian sialyltransferases. The protein also contains 4 potential N-glycosylation sites. The authors noted that the protein predicted by their clone lacks 5 N-terminal amino acids predicted by KIAA1877. They also found evidence for alternative splicing in some ST6GalII-related clones.