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Information on EC 2.4.1.258 - dolichyl-P-Man:Man5GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase and Organism(s) Homo sapiens and UniProt Accession Q92685

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IUBMB Comments
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-dolichol to Man9Glc-NAc2-PP-dolichol on the lumenal side use dolichyl beta-D-mannosyl phosphate. The first step of this assembly pathway on the luminal side of the endoplasmic reticulum is catalysed by ALG3.
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Homo sapiens
UNIPROT: Q92685
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
alg3p, atalg3, tbalg3, dol-p-man:man5glcnac2-pp-dol mannosyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Dol-P-Man:Man5GlcNAc2-PP-Dol mannosyltransferase
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dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase
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Not56-like protein
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SYSTEMATIC NAME
IUBMB Comments
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 alpha-1,3-mannosyltransferase
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-dolichol to Man9Glc-NAc2-PP-dolichol on the lumenal side use dolichyl beta-D-mannosyl phosphate. The first step of this assembly pathway on the luminal side of the endoplasmic reticulum is catalysed by ALG3.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ALG3_HUMAN
438
7
50126
Swiss-Prot
Mitochondrion (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G118D
missense mutation in patients with type IV of the carbohydrate deficient glycoprotein syndromes, characterized by microcephaly, severe epilepsy, minimal psychomotor development and partial deficiency of sialic acids in serum glycoproteins
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
identification of an additional open-reading frame of 141 bp (AAGRP) in the coding region of ALG3 in a patient with congenital disorder of glycosylation. Expression of this hybrid protein is significantly increased due to the homozygous variant c.160_196del. Patient shows secondary microcephaly, significantly decreased head control and axial muscular hypotonia associated with increased limb stiffness. Frequent episodes of hyperextension are observed
medicine
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two Vietnamese siblings with confirmed ALG3-Congenital disorders of glycosylation, 15 and 21 years old, show clinical features with previously reported patients including facial dysmorphism, severe psychomotor retardation, microcephaly, seizures, and gastrointestinal symptoms. Both patients show mutations c.206T > C (p.169 T) and c.626T > C (p.M209T)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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.
110
170-175
2013
Homo sapiens
Manually annotated by BRENDA team
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.
40
938-951
2019
Homo sapiens (Q92685)
Manually annotated by BRENDA team