InterPro domain: IPR016900

Alg10 (asparagine-linked glycosylation) ( 2.4.1.256 ) is a dolichyl-phosphoglucose-dependent glucosyltransferase which adds the terminal alpha-1,2 glucose to the lipid-linked Glc2Man9GlcNAc2 oligosaccharide. The terminal alpha-1,2-linked glucose residue is important for substrate recognition by the oligosaccharyltransferase [ 1 ]. In Saccharomyces cerevisiae, Alg10 has a role in regulation of the expression of a myo-inositol transporter, Itr1 (hence the name Die2, standing for derepression of Itr1 expression) [ 2 ]. It also regulates the expression of Ino1, which is an inositol-3-phosphate synthase [ 3 ]. Alg10 is homologous to human and rat potassium channel regulatory protein KCR1, which diminishes the cardiac repolarising current I(Kr) drug response [ 3 , 4 ].

1. The ALG10 locus of Saccharomyces cerevisiae encodes the alpha-1,2 glucosyltransferase of the endoplasmic reticulum: the terminal glucose of the lipid-linked oligosaccharide is required for efficient N-linked glycosylation. Glycobiology 8, 455-62
2. Isolation and characterization of genes that promote the expression of inositol transporter gene ITR1 in Saccharomyces cerevisiae. Mol. Microbiol. 16, 301-8
3. HERG is protected from pharmacological block by alpha-1,2-glucosyltransferase function. J. Biol. Chem. 282, 5506-13
4. KCR1, a membrane protein that facilitates functional expression of non-inactivating K+ currents associates with rat EAG voltage-dependent K+ channels. J. Biol. Chem. 273, 23080-5