InterPro domain: IPR004856

N-linked (asparagine-linked) glycosylation of proteins is mediated by a highly conserved pathway in eukaryotes, in which a lipid (dolicholphosphate)-linked oligosaccharide is assembled at the endoplasmic reticulum membrane prior to the transfer of the oligosaccharidemoiety to the target asparagine residues. This oligosaccharide is composed of Glc(3)Man(9)GlcNAc(2). The addition of the threeglucose residues is the final series of steps in the synthesis of the oligosaccharide precursor. Alg6 transfers the first glucose residue,and Alg8 transfers the second one [ 1 ]. In the human alg6 gene, a C-T transition, which causes Ala333 to be replaced with Val, hasbeen identified as the cause of a congenital disorder of glycosylation, designated as type Ic OMIM:603147 [ 2 ].

1. New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: cloning of the ALG8 locus. Proc. Natl. Acad. Sci. U.S.A. 91, 5977-81
2. A mutation in the human ortholog of the Saccharomyces cerevisiae ALG6 gene causes carbohydrate-deficient glycoprotein syndrome type-Ic. Proc. Natl. Acad. Sci. U.S.A. 96, 6982-7