ST3GAL1
Description
The ST3GAL1 (ST3 beta-galactoside alpha-2,3-sialyltransferase 1) is a protein-coding gene located on chromosome 8.
ST3GAL1 is a beta-galactoside alpha2-3 sialyltransferase that plays a crucial role in the terminal sialylation of glycoproteins and glycolipids. It catalyzes the transfer of sialic acid (N-acetylneuraminic acid; Neu5Ac) from the donor molecule CMP-Neu5Ac to acceptor Galbeta-(1->3)-GalNAc-terminated glycoconjugates, forming an alpha2-3 linkage. This enzyme adds sialic acid to the core 1 O-glycan, Galbeta-(1->3)-GalNAc-O-Ser/Thr, a major component of mucin-type O-glycans. ST3GAL1 is involved in a homeostatic mechanism that regulates CD8-positive T cell numbers by sialylating core 1 O-glycans of T cell glycoproteins SPN/CD43 and PTPRC/CD45. It prevents premature apoptosis of thymic CD8-positive T cells before they migrate to the periphery, and in secondary lymphoid organs, it controls the survival of CD8-positive memory T cells generated after an immune response. ST3GAL1 also transfers sialic acid to asialofetuin, likely onto Galbeta-(1->3)-GalNAc-O-Ser, and sialylates gangliosides GM1a, GA1, and GD1b to form GD1a, GM1b, and GT1b, respectively.
ST3GAL1 is also known as Gal-NAc6S, SIAT4A, SIATFL, ST3GalA, ST3GalA.1, ST3GalIA, ST3GalIA,1, ST3O.