Sialyltransferase 7B (SIAT7B)

ST6GALNAC2 belongs to a family of sialyltransferases that add sialic acids to the nonreducing ends of glycoconjugates. At the cell surface, these modifications have roles in cell-cell and cell-substrate interactions, bacterial adhesion, and protein targeting . The deduced protein contains 374 amino acids and shares 74.6% amino acid identity with the mouse protein. ST6GAlNAC2 is a type II transmembrane glycoprotein with an N-terminal cytoplasmic tail, a short transmembrane segment, a stem region, and a 347-amino acid catalytic domain containing sialyl motifs L, S, and VS. It has 3 potential N-glycosylation sites. Northern blot analysis detected 2.0- and 1.9-kb ST6GALNAC2 mRNAs abundantly expressed in skeletal muscle. Expression was weaker in heart and very weak or undetectable in all other tissues examined.