MGAT1 explained
Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase is an enzyme that in humans is encoded by the MGAT1 gene.[1] [2]
There are over 100 different glycosyltransferases involved in the synthesis of protein-bound and lipid-bound oligosaccharides. UDP-N-acetylglucosamine:alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I is a medial-Golgi enzyme essential for the synthesis of hybrid and complex N-glycans. The protein, encoded by a single exon, shows typical features of a type II transmembrane protein. The protein is believed to be essential for normal embryogenesis.
Further reading
- Kumar R, Yang J, Eddy RL, etal . Cloning and expression of the murine gene and chromosomal location of the human gene encoding N-acetylglucosaminyltransferase I . Glycobiology . 2 . 4 . 383–93 . 1992 . 1421759 . 10.1093/glycob/2.4.383 .
- Kumar R, Yang J, Larsen RD, Stanley P . Cloning and expression of N-acetylglucosaminyltransferase I, the medial Golgi transferase that initiates complex N-linked carbohydrate formation . Proc. Natl. Acad. Sci. U.S.A. . 87 . 24 . 9948–52 . 1991 . 1702225 . 10.1073/pnas.87.24.9948 . 55291 . free .
- Tan J, D'Agostaro AF, Bendiak B, etal . 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 . 1995 . 7635144 . 10.1111/j.1432-1033.1995.tb20703.x .
- Yip B, Chen SH, Mulder H, etal . Organization of the human beta-1,2-N-acetylglucosaminyltransferase I gene (MGAT1), which controls complex and hybrid N-glycan synthesis . Biochem. J. . 321 . 2. 465–74 . 1997 . 9020882 . 10.1042/bj3210465. 1218092 .
- Yen CL, Stone SJ, Cases S, etal . Identification of a gene encoding MGAT1, a monoacylglycerol acyltransferase . Proc. Natl. Acad. Sci. U.S.A. . 99 . 13 . 8512–7 . 2002 . 12077311 . 10.1073/pnas.132274899 . 124292 . 2002PNAS...99.8512Y . free .
- Strausberg RL, Feingold EA, Grouse LH, etal . Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences . Proc. Natl. Acad. Sci. U.S.A. . 99 . 26 . 16899–903 . 2003 . 12477932 . 10.1073/pnas.242603899 . 139241 . 2002PNAS...9916899M . free .
- Ota T, Suzuki Y, Nishikawa T, etal . Complete sequencing and characterization of 21,243 full-length human cDNAs . Nat. Genet. . 36 . 1 . 40–5 . 2004 . 14702039 . 10.1038/ng1285 . free .
- Colland F, Jacq X, Trouplin V, etal . Functional proteomics mapping of a human signaling pathway . Genome Res. . 14 . 7 . 1324–32 . 2004 . 15231748 . 10.1101/gr.2334104 . 442148 .
- Gerhard DS, Wagner L, Feingold EA, etal . The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) . Genome Res. . 14 . 10B . 2121–7 . 2004 . 15489334 . 10.1101/gr.2596504 . 528928 .
- Rual JF, Venkatesan K, Hao T, etal . Towards a proteome-scale map of the human protein-protein interaction network . Nature . 437 . 7062 . 1173–8 . 2005 . 16189514 . 10.1038/nature04209 . 2005Natur.437.1173R . 4427026 .
- Otsuki T, Ota T, Nishikawa T, etal . Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries . DNA Res. . 12 . 2 . 117–26 . 2007 . 16303743 . 10.1093/dnares/12.2.117 . free .
- Saribas AS, Johnson K, Liu L, etal . Refolding of human beta-1-2 GlcNAc transferase (GnT1) and the role of its unpaired Cys 121 . Biochem. Biophys. Res. Commun. . 362 . 2 . 381–6 . 2007 . 17716624 . 10.1016/j.bbrc.2007.07.199 .
Notes and References
- Hull E, Sarkar M, Spruijt MP, Hoppener JW, Dunn R, Schachter H . Organization and localization to chromosome 5 of the human UDP-N-acetylglucosamine:alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I gene . Biochem Biophys Res Commun . 176 . 2 . 608–15 . Jun 1991 . 1827260 . 10.1016/S0006-291X(05)80227-X .
- Web site: Entrez Gene: MGAT1 mannosyl (alpha-1,3-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase.