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dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
GDP-alpha-D-mannose + Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)(Manalpha(1-6))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-PP-dolichol
GDP + Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)(Manalpha(1-3)Manalpha(1-6))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-PP-dolichol
additional information
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dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
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dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
the core oligosaccharide Glc3Man9GlcNAc2 is assembled by a series of membrane-bound glycosyltransferases as the lipid carrier dolichylpyrophosphate-linked glycan in the endoplasmic reticulum (ER). The first step of this assembly pathway on the ER luminal side is mediated by ALG3. AtALG3 is a critical factor for mature N-glycosylation of proteins, but not essential for cell viability and growth in Arabidopsis
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dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
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dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
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dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
regulatory role for the Alg3p-dependent alpha1,3-linked Man in subsequent oligosaccharide-lipid and glycoprotein glycan maturation. The presence of this Man appears to provide structural information potentiating the downstream action of the endoplasmic reticulum glucosyltransferases Alg6p, Alg8p and Alg10p, glucosidases Gls1p and Gls2p, and the Golgi Och1p outerchain alpha1,6-Man branch-initiating mannosyltransferase
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dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
the formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl beta-D-mannosyl phosphate. Alg3p is not required for elongation of D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
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dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
extension does not occur when the acceptor was added as a free Man5GlcNAc2 oligosaccharide or when GDP-Man is used as mannosyl donor
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GDP-alpha-D-mannose + Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)(Manalpha(1-6))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-PP-dolichol
GDP + Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)(Manalpha(1-3)Manalpha(1-6))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-PP-dolichol
alg3 Man5GlcNAc2 precursor
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GDP-alpha-D-mannose + Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)(Manalpha(1-6))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-PP-dolichol
GDP + Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)(Manalpha(1-3)Manalpha(1-6))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-PP-dolichol
cytosolic alg3 Man5GlcNAc2 precursor
product of the Alg3p step
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GDP-alpha-D-mannose + Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)(Manalpha(1-6))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-PP-dolichol
GDP + Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)(Manalpha(1-3)Manalpha(1-6))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-PP-dolichol
cytosolic alg3 Man5GlcNAc2 precursor
product of the Alg3p step
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GDP-alpha-D-mannose + Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)(Manalpha(1-6))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-PP-dolichol
GDP + Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)(Manalpha(1-3)Manalpha(1-6))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-PP-dolichol
alg3 Man5GlcNAc2 precursor
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additional information
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Alg3-mediated N-glycosylation of the effector, Secreted LysM Protein1 (Slp1), is essential for its activity. Slp1 has three N-glycosylation sites and simultaneous Alg3-mediated N-glycosylation of each site is required to maintain protein stability and the chitin binding activity of Slp1
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additional information
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MNN1 encoded enzyme adds at least the penultimate alpha-1,3-linked Man of the terminal Manalpha(1-3)Manalpha(1-3)-disaccharide on O-linked glycans
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additional information
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MNN1 encoded enzyme adds at least the penultimate alpha-1,3-linked Man of the terminal Manalpha(1-3)Manalpha(1-3)-disaccharide on O-linked glycans
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additional information
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regulatory role for the Alg3p-dependent alpha-1,3-linked Man in subsequent oligosaccharide-lipid and glycoprotein glycan maturation, it provides structural information that potentiates the Alg6p, Alg8p and Alg10p ER glucosyltransferases and Gls1p and Gls2p trimming glucosidases
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additional information
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regulatory role for the Alg3p-dependent alpha-1,3-linked Man in subsequent oligosaccharide-lipid and glycoprotein glycan maturation, it provides structural information that potentiates the Alg6p, Alg8p and Alg10p ER glucosyltransferases and Gls1p and Gls2p trimming glucosidases
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additional information
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involved in oligosaccharide-lipid synthesis
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additional information
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MNN1 encoded enzyme adds at least the penultimate alpha-1,3-linked Man of the terminal Manalpha(1-3)Manalpha(1-3)-disaccharide on O-linked glycans
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additional information
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regulatory role for the Alg3p-dependent alpha-1,3-linked Man in subsequent oligosaccharide-lipid and glycoprotein glycan maturation, it provides structural information that potentiates the Alg6p, Alg8p and Alg10p ER glucosyltransferases and Gls1p and Gls2p trimming glucosidases
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additional information
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involved in oligosaccharide-lipid synthesis
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dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
additional information
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dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
the core oligosaccharide Glc3Man9GlcNAc2 is assembled by a series of membrane-bound glycosyltransferases as the lipid carrier dolichylpyrophosphate-linked glycan in the endoplasmic reticulum (ER). The first step of this assembly pathway on the ER luminal side is mediated by ALG3. AtALG3 is a critical factor for mature N-glycosylation of proteins, but not essential for cell viability and growth in Arabidopsis
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dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
regulatory role for the Alg3p-dependent alpha1,3-linked Man in subsequent oligosaccharide-lipid and glycoprotein glycan maturation. The presence of this Man appears to provide structural information potentiating the downstream action of the endoplasmic reticulum glucosyltransferases Alg6p, Alg8p and Alg10p, glucosidases Gls1p and Gls2p, and the Golgi Och1p outerchain alpha1,6-Man branch-initiating mannosyltransferase
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dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
the formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl beta-D-mannosyl phosphate. Alg3p is not required for elongation of D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
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additional information
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regulatory role for the Alg3p-dependent alpha-1,3-linked Man in subsequent oligosaccharide-lipid and glycoprotein glycan maturation, it provides structural information that potentiates the Alg6p, Alg8p and Alg10p ER glucosyltransferases and Gls1p and Gls2p trimming glucosidases
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additional information
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regulatory role for the Alg3p-dependent alpha-1,3-linked Man in subsequent oligosaccharide-lipid and glycoprotein glycan maturation, it provides structural information that potentiates the Alg6p, Alg8p and Alg10p ER glucosyltransferases and Gls1p and Gls2p trimming glucosidases
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additional information
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involved in oligosaccharide-lipid synthesis
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additional information
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regulatory role for the Alg3p-dependent alpha-1,3-linked Man in subsequent oligosaccharide-lipid and glycoprotein glycan maturation, it provides structural information that potentiates the Alg6p, Alg8p and Alg10p ER glucosyltransferases and Gls1p and Gls2p trimming glucosidases
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additional information
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involved in oligosaccharide-lipid synthesis
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malfunction
alg3 yeast accumulates Man5GlcNAc2-P-P-dolichol due to a defective alphal,3-mannosyltransferase required for the next step in oligosaccharide-lipid elongation
malfunction
Arabidopsis thaliana ALG3 mutant synthesizes immature oligosaccharides in the ER and accumulates unique N-glycans. Most of the proteins in alg3-T are not modified as high-mannose-type N-glycoproteins
malfunction
deletion of this gene in an och1 mutant background results in the secretion of glycoproteins with a Man5GlcNAc2 structure
malfunction
procyclic and bloodstream form null mutants of TbALG3 grow with normal kinetics, remain infectious to mice and tsetse flies, respectively, and have normal morphology. Both forms display aberrant N-glycosylation of their major surface glycoproteins, procylcin, and variant surface glycoprotein, respectively. The largest Dol-PP-linked oligosaccharide made by the TbALG3 null mutant is a biantennary Man5GlcNAc2 species
malfunction
the alg3 mutant accumulates D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
malfunction
the inactivation of the nonessential ALG3 gene results in the accumulation of lipid-linked Man5GlcNAc2 and protein-bound carbohydrates which are completely Endo H resistant
malfunction
type IV of the carbohydrate deficient glycoprotein syndromes (CDGS) is characterized by microcephaly, severe epilepsy, minimal psychomotor development and partial deficiency of sialic acids in serum glycoproteins. The molecular defect in the index patient is a missense mutation in the gene encoding the mannosyltransferase that transfers mannose from dolichyl-phosphate mannose on to the lipid-linked oligosaccharide (LLO) intermediate Man(5)GlcNAc(2)-PP-dolichol. The defect results in the accumulation of the LLO intermediate and, due to its leaky nature, a residual formation of full-length LLOs. N-glycosylation is abnormal because of the transfer of truncated oligosaccharides in addition to that of full-length oligosaccharides and because of the incomplete utilization of N-glycosylation sites
malfunction
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alg3 yeast accumulates Man5GlcNAc2-P-P-dolichol due to a defective alphal,3-mannosyltransferase required for the next step in oligosaccharide-lipid elongation
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physiological function
regulatory role for the Alg3p-dependent alpha1,3-linked Man in subsequent oligosaccharide-lipid and glycoprotein glycan maturation. The presence of this Man appears to provide structural information potentiating the downstream action of the endoplasmic reticulum glucosyltransferases Alg6p, Alg8p and Alg10p, glucosidases Gls1p and Gls2p, and the Golgi Och1p outerchain alpha1,6-Man branch-initiating mannosyltransferase
physiological function
the formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl beta-D-mannosyl phosphate
physiological function
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an the alg3 knockout strain displays decreased site-specific N-glycosylation occupancy preferentially at Asn-Xaa-Ser sequences located in secondary structural elements. Glycosylation sites are not uniformly affected in DELTAalg3 cells, with the subset of sites with lower affinity for oligosaccharyltransferase most strongly affected. 13 specific glycosylation sites are found which are underglycosylated in the DELTAalg3 strain compared to wild type cells. The features of these glycosylation sites suggest that they are the subset of normally modified sites that are more difficult for oligosaccharyltransferase to glycosylate. Under-glycosylated sites in the DELTAalg3 strain are likely to be present in secondary structural elements such as helices or sheets, whereas efficiently glycosylated sites are more likely present in flexible loops
physiological function
deletion of the alg3+ gene in the och1 deletion mutant lacking alpha-1,6mannosyltransferase activity. Analysis of the detailed oligosaccharide structures in alg3och1 double mutant reveals that the N-linked oligosaccharides of Schizosaccharomyces pombe alg3och1 cells mainly consist of two or three alpha-galactose-capped M5B structures. Western blot analysis of recombinant human transferrin in alg3och1 cells suggests that heterologously expressed glycoproteins in this mutant have Endo H-resistant N-linked oligosaccharide structures similar to those of alg3och1 cell-surface glycoproteins
physiological function
inactivation of alg3 gene results in the production of predominantly Man3GlcNAc2 protein-linked N-glycans. No impact on growth nor a developmental phenotype due to the deletion is observed
physiological function
deletion of Alg3 results in the arrest of secondary infection hyphae and a significant reduction in virulence. Alg3 deletion mutants induce massive production of reactive oxygen species in host cells. Alg3-mediated N-glycosylation of the effector, Secreted LysM Protein1 (Slp1), is essential for its activity. Alg3 deletion mutants accumulate reactive oxygen species in a similar manner to Slp1 deletion mutants, which is a key factor responsible for arresting infection hyphae of the mutants
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Cipollo, J.F.; Trimble, R.B.
The accumulation of Man6GlcNAc2-PP-dolichol in the Saccharomyces cerevisiae deltaalg9 mutant reveals a regulatory role for the Alg3p alpha1,3-Man middle-arm addition in downstream oligosaccharide-lipid and glycoprotein glycan processing
J. Biol. Chem.
275
4267-4277
2000
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P38179), Saccharomyces cerevisiae A (P38179)
brenda
Verostek, M.F.; Atkinson, P.H.; Trimble, R.B.
Structure of Saccharomyces cerevisiae alg3,sec18 mutant oligosaccharides
J. Biol. Chem.
266
5547-5551
1991
Saccharomyces cerevisiae (P38179), Saccharomyces cerevisiae A (P38179)
brenda
Sharma, C.B.; Knauer, R.; Lehle, L.
Biosynthesis of lipid-linked oligosaccharides in yeast: the ALG3 gene encodes the Dol-P-Man:Man5GlcNAc2-PP-Dol mannosyltransferase
Biol. Chem.
382
321-328
2001
Saccharomyces cerevisiae (P38179), Saccharomyces cerevisiae
brenda
Krner, C.; Knauer, R.; Stephani, U.; Marquardt, T.; Lehle, L.; von Figura, K.
Carbohydrate deficient glycoprotein syndrome type IV: deficiency of dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase
EMBO J.
18
6816-6822
1999
Homo sapiens (Q92685)
brenda
Davidson, R.C.; Nett, J.H.; Renfer, E.; Li, H.; Stadheim, T.A.; Miller, B.J.; Miele, R.G.; Hamilton, S.R.; Choi, B.K.; Mitchell, T.I., Wildt, S.
Functional analysis of the ALG3 gene encoding the Dol-P-Man:Man5GlcNAc2-PP-Dol mannosyltransferase enzyme of P. pastoris
Glycobiology
14
399-407
2004
Komagataella pastoris (Q6DNA2)
brenda
Manthri, S.; Gther, M.L.; Izquierdo, L.; Acosta-Serrano, A.; Ferguson, M.A.
Deletion of the TbALG3 gene demonstrates site-specific N-glycosylation and N-glycan processing in Trypanosoma brucei
Glycobiology
18
367-383
2008
Trypanosoma brucei (A8E112), Trypanosoma brucei
brenda
Kajiura, H.; Seki, T.; Fujiyama, K.
Arabidopsis thaliana ALG3 mutant synthesizes immature oligosaccharides in the ER and accumulates unique N-glycans
Glycobiology
20
736-751
2010
Arabidopsis thaliana (O82244), Arabidopsis thaliana
brenda
Aebi, M.; Gassenhuber, J.; Domdey, H.; te Heesen, S.
Cloning and characterization of the ALG3 gene of Saccharomyces cerevisiae
Glycobiology
6
439-444
1996
Saccharomyces cerevisiae (P38179)
brenda
Henquet, M.; Lehle, L.; Schreuder, M.; Rouwendal, G.; Molthoff, J.; Helsper, J.; van der Krol, S.; Bosch, D.
Identification of the gene encoding the alpha1,3-mannosyltransferase (ALG3) in Arabidopsis and characterization of downstream N-glycan processing
Plant Cell
20
1652-1664
2008
Arabidopsis thaliana (O82244)
brenda
Berends, E.; Lehle, L.; Henquet, M.; Hesselink, T.; Woesten, H.A.; Lugones, L.G.; Bosch, D.
Identification of alg3 in the mushroom-forming fungus Schizophyllum commune and analysis of the Deltaalg3 knockout mutant
Glycobiology
23
147-154
2013
Schizophyllum commune (D8PWW0)
brenda
Ohashi, T.; Nakakita, S.; Sumiyoshi, W.; Takegawa, K.
Production of heterologous glycoproteins by a glycosylation-defective alg3och1 mutant of Schizosaccharomyces pombe
J. Biotechnol.
150
348-356
2010
Schizosaccharomyces pombe (Q9Y7I4)
brenda
Bailey, U.M.; Jamaluddin, M.F.; Schulz, B.L.
Analysis of congenital disorder of glycosylation-Id in a yeast model system shows diverse site-specific under-glycosylation of glycoproteins
J. Proteome Res.
11
5376-5383
2012
Saccharomyces cerevisiae
brenda
De Pourcq, K.; Tiels, P.; Van Hecke, A.; Geysens, S.; Vervecken, W.; Callewaert, N.
Engineering Yarrowia lipolytica to produce glycoproteins homogeneously modified with the universal Man3GlcNAc2 N-glycan core
PLoS ONE
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Yarrowia lipolytica
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Riess, S.; Reddihough, D.S.; Howell, K.B.; Dagia, C.; Jaeken, J.; Matthijs, G.; Yaplito-Lee, J.
ALG3-CDG (CDG-Id): clinical, biochemical and molecular findings in two siblings
Mol. Genet. Metab.
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2013
Homo sapiens
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Chen, X.L.; Shi, T.; Yang, J.; Shi, W.; Gao, X.; Chen, D.; Xu, X.; Xu, J.R.; Talbot, N.J.; Peng, Y.L.
N-glycosylation of effector proteins by an alpha-1,3-mannosyltransferase is required for the rice blast fungus to evade host innate immunity
Plant Cell
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Pyricularia oryzae (M1RXP4)
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Himmelreich, N.; Dimitrov, B.; Geiger, V.; Zielonka, M.; Hutter, A.-M.; Beedgen, L.; Hllen, A.; Breuer, M.; Peters, V.; Thiemann, K.-C.; Hoffmann, G. F.; Sinning, I.; Dupre, T.; Vuillaumier-Barrot, S.; Barrey, C.; Denecke, J.; Klfen, W.; Dker, G.; Ganschow, R.; Lentze, M.J.; Moore, S.; Seta, N.; Ziegler, A.; Thiel, C.
Novel variants and clinical symptoms in four new ALG3-CDG patients, review of the literature, and identification of AAGRP-ALG3 as a novel ALG3 variant with alanine and glycine-rich N-terminus
Hum. Mutat.
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2019
Homo sapiens (Q92685)
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