UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1 is an
enzyme that in humans is encoded by the B3GALNT1gene.[4][5][6]
This gene is a member of the beta-1,3-
galactosyltransferase (beta3GalT) gene family. This family encodes type II membrane-bound
glycoproteins with diverse enzymatic functions using different donor substrates (
UDP-galactose and UDP-N-acetylgalactosamine) and different acceptor sugars (
N-acetylglucosamine,
galactose,
N-acetylgalactosamine). The beta3GalT genes are distantly related to the Drosophila Brainiac gene and have the protein coding sequence contained in a single
exon. The beta3GalT proteins also contain
conserved sequences not found in the beta4GalT or alpha3GalT proteins. The carbohydrate chains synthesized by these enzymes are designated as type 1, whereas beta4GalT enzymes synthesize type 2 carbohydrate chains. The ratio of type 1:type 2 chains changes during
embryogenesis. By
sequence similarity, the beta3GalT genes fall into at least two groups: beta3GalT4 and 4 other beta3GalT genes (beta3GalT1-3, beta3GalT5). The encoded protein of this gene does not use N-acetylglucosamine as an acceptor sugar at all. Multiple
transcript variants that are alternatively spliced in the
5' UTR have been described; they all encode the same protein.[6]
Amado M, Almeida R, Schwientek T, Clausen H (2000). "Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions". Biochim. Biophys. Acta. 1473 (1): 35–53.
doi:
10.1016/S0304-4165(99)00168-3.
PMID10580128.
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.
PMID2649653.
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.
PMID2829950.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4.
doi:
10.1016/0378-1119(94)90802-8.
PMID8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56.
doi:
10.1016/S0378-1119(97)00411-3.
PMID9373149.
UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1 is an
enzyme that in humans is encoded by the B3GALNT1gene.[4][5][6]
This gene is a member of the beta-1,3-
galactosyltransferase (beta3GalT) gene family. This family encodes type II membrane-bound
glycoproteins with diverse enzymatic functions using different donor substrates (
UDP-galactose and UDP-N-acetylgalactosamine) and different acceptor sugars (
N-acetylglucosamine,
galactose,
N-acetylgalactosamine). The beta3GalT genes are distantly related to the Drosophila Brainiac gene and have the protein coding sequence contained in a single
exon. The beta3GalT proteins also contain
conserved sequences not found in the beta4GalT or alpha3GalT proteins. The carbohydrate chains synthesized by these enzymes are designated as type 1, whereas beta4GalT enzymes synthesize type 2 carbohydrate chains. The ratio of type 1:type 2 chains changes during
embryogenesis. By
sequence similarity, the beta3GalT genes fall into at least two groups: beta3GalT4 and 4 other beta3GalT genes (beta3GalT1-3, beta3GalT5). The encoded protein of this gene does not use N-acetylglucosamine as an acceptor sugar at all. Multiple
transcript variants that are alternatively spliced in the
5' UTR have been described; they all encode the same protein.[6]
Amado M, Almeida R, Schwientek T, Clausen H (2000). "Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions". Biochim. Biophys. Acta. 1473 (1): 35–53.
doi:
10.1016/S0304-4165(99)00168-3.
PMID10580128.
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.
PMID2649653.
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.
PMID2829950.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4.
doi:
10.1016/0378-1119(94)90802-8.
PMID8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56.
doi:
10.1016/S0378-1119(97)00411-3.
PMID9373149.