Carbohydrate Sulfotransferase 9 (CHST9)

Sulfate groups in carbohydrates confer highly specific functions on glycoproteins, glycolipids, and proteoglycans and are critical for cell-cell interaction, signal transduction, and embryonic development. Sulfotransferases, such as CHST9, carry out sulfation of carbohydrates. The full-length protein contains 443 amino acids and has a calculated molecular mass of 52.1 kD. It has a membrane-spanning domain with a type II topology, a stem region, putative 5-prime-phosphosulfonate- and 3-prime-phosphate-binding sites, and 4 potential N-glycosylation sites. GalNAc4ST2 shares 46% amino acid identity with GalNAc4ST1 (CHST8). Synthesis of this protein is initiated from an alternative start codon (met86), and, consequently, it lacks the N-terminal transmembrane domain.