Literature summary for 2.4.1.265 extracted from

Chantret, I.; Dancourt, J.; Dupre, T.; Delenda, C.; Bucher, S.; Vuillaumier-Barrot, S.; Ogier de Baulny, H.; Peletan, C.; Danos, O.; Seta, N.; Durand, G.; Oriol, R.; Codogno, P.; Moore, S.E.
A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl alpha3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation (2003), J. Biol. Chem., 278, 9962-9971.

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9BVK2	-	-

Synonyms

Synonyms	Comment	Organism
dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl alpha3-glucosyltransferase	-	Homo sapiens
hALG8p	-	Homo sapiens

General Information

General Information	Comment	Organism
malfunction	patient with inefficient addition of the second glucose residue onto lipid-linked oligosaccharide. The patient possesses only 1020% normal amounts of mRNA encoding the enzyme, dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl alpha3-glucosyltransferase (hALG8p), which catalyzes this reaction. Sequencing of hALG8 genomic DNA reveals exon 4 to contain a base deletion in one allele and a base insertion in the other. Both mutations give rise to premature stop codons predicted to generate severely truncated proteins. Because the translation inhibitor emetine is shown to stabilize the hALG8 mRNA from the patient to normal levels, it is likely that both transcripts undergo nonsensemediated mRNA decay. As the cells from the patient are successfully complemented with wild type hALG8 cDNA, it is concluded that these mutations are the underlying cause of this new CDG I subtype that we propose be called CDG Ih	Homo sapiens

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Release 2023.1 (January 2023)