MGAT2

Mannosyl (alpha-1,6-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase

Identifiers

MGAT2; CDG2A; CDGS2; GLCNACTII; GNT-II; GNT2

External IDs

OMIM: 602616 MGI: 2384966 HomoloGene: 1806 GeneCards: MGAT2 Gene

2.4.1.143

Gene Ontology
Molecular function	• sugar binding • alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity • transferase activity, transferring glycosyl groups
Cellular component	• Golgi membrane • membrane fraction • Golgi apparatus • Golgi stack • membrane • integral to membrane
Biological process	• protein N-linked glycosylation • oligosaccharide metabolic process • oligosaccharide biosynthetic process • protein N-linked glycosylation via asparagine • post-translational protein modification • cellular protein metabolic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 14:
50.09 – 50.09 Mb

Chr 12:
70.29 – 70.29 Mb

PubMed search

[1]

[2]

Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase is an enzyme that in humans is encoded by the MGAT2 gene.^[1]^[2]

The product of this gene is a Golgi enzyme catalyzing an essential step in the conversion of oligomannose to complex N-glycans. The enzyme has the typical glycosyltransferase domains: a short N-terminal cytoplasmic domain, a hydrophobic non-cleavable signal-anchor domain, and a C-terminal catalytic domain. Mutations in this gene may lead to carbohydrate-deficient glycoprotein syndrome, type II. The coding region of this gene is intronless. Transcript variants with a spliced 5' UTR may exist, but their biological validity has not been determined.^[2]

References

^ Tan J, D'Agostaro AF, Bendiak B, Reck F, Sarkar M, Squire JA, Leong P, Schachter H (Sep 1995). "The human UDP-N-acetylglucosamine: alpha-6-D-mannoside-beta-1,2- N-acetylglucosaminyltransferase II gene (MGAT2). Cloning of genomic DNA, localization to chromosome 14q21, expression in insect cells and purification of the recombinant protein". Eur J Biochem 231 (2): 317–28. doi:10.1111/j.1432-1033.1995.tb20703.x. PMID 7635144.
^ ^a ^b "Entrez Gene: MGAT2 mannosyl (alpha-1,6-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4247.

Cormier-Daire V, Amiel J, Vuillaumier-Barrot S, et al. (2000). "Congenital disorders of glycosylation IIa cause growth retardation, mental retardation, and facial dysmorphism". J. Med. Genet. 37 (11): 875–7. doi:10.1136/jmg.37.11.875. PMC 1734478. PMID 11228641. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1734478.
Land A, Braakman I (2001). "Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum". Biochimie 83 (8): 783–90. doi:10.1016/S0300-9084(01)01314-1. PMID 11530211.
Dedera DA, Gu RL, Ratner L (1992). "Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function". Virology 187 (1): 377–82. doi:10.1016/0042-6822(92)90331-I. PMID 1736542.
Kalyanaraman VS, Rodriguez V, Veronese F, et al. (1990). "Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1". AIDS Res. Hum. Retroviruses 6 (3): 371–80. doi:10.1089/aid.1990.6.371. PMID 2187500.
Shimizu H, Tsuchie H, Honma H, et al. (1991). "Effect of N-(3-phenyl-2-propenyl)-1-deoxynojirimycin on the lectin binding to HIV-1 glycoproteins". Jpn. J. Med. Sci. Biol. 43 (3): 75–87. PMID 2283726.
Leonard CK, Spellman MW, Riddle L, et al. (1990). "Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells". J. Biol. Chem. 265 (18): 10373–82. PMID 2355006.
Pal R, Hoke GM, Sarngadharan MG (1989). "Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1". Proc. Natl. Acad. Sci. U.S.A. 86 (9): 3384–8. doi:10.1073/pnas.86.9.3384. PMC 287137. PMID 2541446. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=287137.
Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP (1989). "Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport". J. Virol. 63 (6): 2452–6. PMC 250699. PMID 2542563. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=250699.
Kozarsky K, Penman M, Basiripour L, et al. (1989). "Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein". J. Acquir. Immune Defic. Syndr. 2 (2): 163–9. PMID 2649653.
Robinson WE, Montefiori DC, Mitchell WM (1988). "Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis". AIDS Res. Hum. Retroviruses 3 (3): 265–82. doi:10.1089/aid.1987.3.265. PMID 2829950.
Blough HA, Pauwels R, De Clercq E, et al. (1987). "Glycosylation inhibitors block the expression of LAV/HTLV-III (HIV) glycoproteins". Biochem. Biophys. Res. Commun. 141 (1): 33–8. doi:10.1016/S0006-291X(86)80330-8. PMID 3099781.
Montefiori DC, Robinson WE, Mitchell WM (1988). "Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1". Proc. Natl. Acad. Sci. U.S.A. 85 (23): 9248–52. doi:10.1073/pnas.85.23.9248. PMC 282716. PMID 3264072. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=282716.
D'Agostaro GA, Zingoni A, Moritz RL, et al. (1995). "Molecular cloning and expression of cDNA encoding the rat UDP-N-acetylglucosamine:alpha-6-D-mannoside beta-1,2-N-acetylglucosaminyltransferase II". J. Biol. Chem. 270 (25): 15211–21. doi:10.1074/jbc.270.25.15211. PMID 7797505.
Fenouillet E, Jones I, Powell B, et al. (1993). "Functional role of the glycan cluster of the human immunodeficiency virus type 1 transmembrane glycoprotein (gp41) ectodomain". J. Virol. 67 (1): 150–60. PMC 237347. PMID 8093218. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=237347.
Yeh JC, Seals JR, Murphy CI, et al. (1993). "Site-specific N-glycosylation and oligosaccharide structures of recombinant HIV-1 gp120 derived from a baculovirus expression system". Biochemistry 32 (41): 11087–99. doi:10.1021/bi00092a019. PMID 8218172.
Bolmstedt A, Sjölander S, Hansen JE, et al. (1996). "Influence of N-linked glycans in V4-V5 region of human immunodeficiency virus type 1 glycoprotein gp160 on induction of a virus-neutralizing humoral response". J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. 12 (3): 213–20. doi:10.1097/00042560-199607000-00001. PMID 8673525.
Tan J, Dunn J, Jaeken J, Schachter H (1996). "Mutations in the MGAT2 gene controlling complex N-glycan synthesis cause carbohydrate-deficient glycoprotein syndrome type II, an autosomal recessive disease with defective brain development". Am. J. Hum. Genet. 59 (4): 810–7. PMC 1914797. PMID 8808595. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1914797.
Hu H, Shioda T, Moriya C, et al. (1996). "Infectivities of human and other primate lentiviruses are activated by desialylation of the virion surface". J. Virol. 70 (11): 7462–70. PMC 190813. PMID 8892864. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=190813.
Papandreou MJ, Fenouillet E (1997). "Effect of various glycosidase treatments on the resistance of the HIV-1 envelope to degradation". FEBS Lett. 406 (1–2): 191–5. doi:10.1016/S0014-5793(97)00273-1. PMID 9109416.

External links

GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview

MGAT2

References

Further reading

External links