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Information on EC 2.4.1.132 - GDP-Man:Man1GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase and Organism(s) Mus musculus and UniProt Accession Q9DBE8

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IUBMB Comments
The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an alpha1,3-mannosylation of D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation (cf. EC 2.4.1.257), to form the first branched pentasaccharide intermediate of the dolichol pathway [1,2].
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Mus musculus
UNIPROT: Q9DBE8
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
alpha-1,3-mannosyltransferase, mannosyltransferase ii, halg2, gdp-man:dol-pp-glcnac2man2 alpha-1,3-mannosyltransferase, gdp-man:man1glcnac2-pp-dolichol mannosyltransferase, asparagine-linked glycosylation 2, scalg2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
asparagine-linked glycosylation 2
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alpha-1,3-mannosyltransferase
-
-
-
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GDP-mannose-oligosaccharide-lipid mannosyltransferase II
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-
-
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mannosyltransferase II
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-
-
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mannosyltransferase, guanosine diphosphomannose-oligosaccharide-lipid II
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
GDP-D-mannose:D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol 3-alpha-mannosyltransferase
The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an alpha1,3-mannosylation of D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation (cf. EC 2.4.1.257), to form the first branched pentasaccharide intermediate of the dolichol pathway [1,2].
CAS REGISTRY NUMBER
COMMENTARY hide
81181-76-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene ALG2
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
a calvarial bone-derived osteoblast cell line
Manually annotated by BRENDA team
distribution of ALG2 in mouse muscle sections by immunohistochemic analysis, Alg2 is enriched at endplate regions of the muscle sections, the region of the alpha-bungarotoxin binding
Manually annotated by BRENDA team
additional information
asparagine-linked glycosylation 2 (Alg2) is commonly downregulated in BMP-2-induced osteoblast differentiation in both MC3T3-E1 and ST-2 cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
loss of Alg2 promotes osteoblast differentiation in ST-2 cells without affecting the protein level of Runx2. Alg2 knockdown does not affect endoplasmic reticulum stress or bone morphogenetic protein, BMP, signaling in ST-2 cells. Atf4,also known as CCAAT/enhancer-binding protein homologous protein (Chop), is mildly upregulated by sAlg2, but only in BMP-2-treated cells. The expression of a target of the Atf6 pathway, heat shock protein 5 (Hspa5), is not altered by loss of Alg2
metabolism
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ALG2_MOUSE
415
0
47405
Swiss-Prot
Mitochondrion (Reliability: 3)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
V68G
site-directed mutagenesis, the mutant shows reduced expression in muscle
additional information
ALG2 downregulation in ST-2 cells by siRNA transfection
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ALG2, expression analysis by quantitative RT-PCR, coexpression of Alg2 and Runx2 in COS-7 cells, both localizing to different compartments
gene ALG2, recombinant expression of wild-type and mutat V68G enzymes in HEK-293 cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
knockdown of human immunodeficiency virus type 1 enhancer-binding protein 3, Hivep3, downregulates Alg2 expression. Expression of the Alg2 gene is reduced upon knockdown of Hivep3 in osteoblastic cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cossins, J.; Belaya, K.; Hicks, D.; Salih, M.A.; Finlayson, S.; Carboni, N.; Liu, W.W.; Maxwell, S.; Zoltowska, K.; Farsani, G.T.; Laval, S.; Seidhamed, M.Z.; Seidhamed, M.Z.; Donnelly, P.; Bentley, D.; McGowan, S.J.; Mueller, J.; Palace, J.; Lochmueller, H.; Beeson, D.
Congenital myasthenic syndromes due to mutations in ALG2 and ALG14
Brain
136
944-956
2013
Homo sapiens (Q9H553), Homo sapiens, Mus musculus (Q9DBE8)
Manually annotated by BRENDA team
Imamura, K.; Maeda, S.; Kawamura, I.; Matsuyama, K.; Shinohara, N.; Yahiro, Y.; Nagano, S.; Setoguchi, T.; Yokouchi, M.; Ishidou, Y.; Komiya, S.
Human immunodeficiency virus type 1 enhancer-binding protein 3 is essential for the expression of asparagine-linked glycosylation 2 in the regulation of osteoblast and chondrocyte differentiation
J. Biol. Chem.
289
9865-9879
2014
Mus musculus (Q9DBE8), Mus musculus C57/BL6J (Q9DBE8)
Manually annotated by BRENDA team