MGAT2

MGAT2
Identifiers
Aliases	MGAT2 , CDG2A, CDGS2, GLCNACTII, GNT-II, GNT2, mannosyl (alpha-1,6-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase, alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
External IDs	OMIM: 602616 MGI: 2384966 HomoloGene: 1806 GeneCards: MGAT2
Gene location (Human) Chr. Chromosome 14 (human) [1] Band 14q21.3 Start 49,620,799 bp [1] End 49,623,481 bp [1]
Gene location (Mouse) Chr. Chromosome 12 (mouse) [2] Band 12|12 C2 Start 69,230,931 bp [2] End 69,233,544 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in jejunal mucosa periodontal fiber corpus epididymis caput epididymis bronchial epithelial cell seminal vesicula superficial temporal artery pericardium duodenum monocyte Top expressed in parotid gland seminal vesicula epithelium of stomach calvaria medullary collecting duct pyloric antrum cervix renal corpuscle submandibular gland proximal tubule More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity carbohydrate binding glycosyltransferase activity manganese ion binding protein homodimerization activity metal ion binding Cellular component integral component of membrane Golgi membrane Golgi stack Golgi apparatus membrane Biological process protein glycosylation oligosaccharide biosynthetic process protein N-linked glycosylation oligosaccharide metabolic process protein N-linked glycosylation via asparagine Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4247 217664 Ensembl ENSG00000168282 ENSMUSG00000043998 UniProt Q10469 Q921V5 RefSeq (mRNA) NM_002408 NM_001015883 NM_146035 RefSeq (protein) NP_002399 NP_666147 Location (UCSC) Chr 14: 49.62 – 49.62 Mb Chr 12: 69.23 – 69.23 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase is an enzyme that in humans is encoded by the MGAT2 gene. ^{[5] [6]}

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. ^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000168282 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000043998 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. "Entrez Gene: MGAT2 mannosyl (alpha-1,6-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase".

Further reading

• 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.
• 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. hdl: 1874/5091 . PMID   11530211. S2CID   13576808.
• 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. doi: 10.7883/yoken1952.43.75 . 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. doi: 10.1016/S0021-9258(18)86956-3 . 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. Bibcode:1989PNAS...86.3384P. doi: 10.1073/pnas.86.9.3384 . PMC   287137 . PMID   2541446.
• 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. doi:10.1128/jvi.63.6.2452-2456.1989. PMC   250699 . PMID   2542563.
• 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. Bibcode:1988PNAS...85.9248M. doi: 10.1073/pnas.85.23.9248 . PMC   282716 . PMID   3264072.
• 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. doi:10.1128/jvi.67.1.150-160.1993. PMC   237347 . PMID   8093218.
• 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.
• 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. doi:10.1128/jvi.70.11.7462-7470.1996. PMC   190813 . PMID   8892864.
• 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. S2CID   17660.

External links

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