Sialyltransferase 7F (SIAT7F)

ST6GALNAC6 belongs to a family of sialyltransferases that modify proteins and ceramides on the cell surface to alter cell-cell or cell-extracellular matrix interactions.The deduced 333-amino acid protein has an N-terminal cytoplasmic tail, a transmembrane region, and a long extracellular catalytic domain containing the conserved sialyl motifs L and S. St6GalNAc VI has 3 potential N-glycosylation sites. Northern blot analysis detected a 2.5-kb transcript in all mouse tissues examined, with highest levels in colon, brain, liver, and heart. A 7.5-kb transcript was also detected in colon.Mouse St6GalNAc VI showed alpha-2,6-sialyltransferase activity against the gangliosides GM1b, GT1b, and GD1a, forming GD1-alpha, GQ1b-alpha, and GT1a-alpha, respectively. No glycoproteins examined were used as acceptor substrates.