Beta-1,3-N-acetylglucosaminyltransferase 3

UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 3
Identifiers
Symbols	B3GNT3 ; B3GAL-T8; B3GN-T3; B3GNT-3; HP10328; TMEM3; beta3Gn-T3
External IDs	OMIM: 605863 MGI: 2152535 HomoloGene: 113516 GeneCards: B3GNT3 Gene
EC number	2.4.1.146, 2.4.1.149
Gene ontology Molecular function • galactosyltransferase activity • N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity • beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity Cellular component • Golgi membrane • integral component of plasma membrane Biological process • carbohydrate metabolic process • protein O-linked glycosylation • O-glycan processing • keratan sulfate biosynthetic process • glycosaminoglycan metabolic process • poly-N-acetyllactosamine biosynthetic process • keratan sulfate metabolic process • post-translational protein modification • cellular protein metabolic process • small molecule metabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	10331	72297
Ensembl	ENSG00000179913	ENSMUSG00000031803
UniProt	Q9Y2A9	Q5JCS9
RefSeq (mRNA)	NM_014256	NM_028189
RefSeq (protein)	NP_055071	NP_082465
Location (UCSC)	Chr 19: 17.79 – 17.81 Mb	Chr 8: 71.69 – 71.7 Mb
PubMed search

UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 3 is an enzyme that in humans is encoded by the B3GNT3 gene.^[1][2][3]

This gene encodes a member of the beta-1,3-N-acetylglucosaminyltransferase family. This enzyme is a type II transmembrane protein and contains a signal anchor that is not cleaved. It prefers the substrates of lacto-N-tetraose and lacto-N-neotetraose, and is involved in the biosynthesis of poly-N-acetyllactosamine chains and the biosynthesis of the backbone structure of dimeric sialyl Lewis a. It plays dominant roles in L-selectin ligand biosynthesis, lymphocyte homing and lymphocyte trafficking.^[3]

References

1. Yokoyama-Kobayashi M, Yamaguchi T, Sekine S, Kato S (Apr 1999). "Selection of cDNAs encoding putative type II membrane proteins on the cell surface from a human full-length cDNA bank". Gene 228 (1-2): 161–7. doi:10.1016/S0378-1119(99)00004-9. PMID 10072769.
2. Shiraishi N, Natsume A, Togayachi A, Endo T, Akashima T, Yamada Y, Imai N, Nakagawa S, Koizumi S, Sekine S, Narimatsu H, Sasaki K (May 2001). "Identification and characterization of three novel beta 1,3-N-acetylglucosaminyltransferases structurally related to the beta 1,3-galactosyltransferase family". J Biol Chem 276 (5): 3498–507. doi:10.1074/jbc.M004800200. PMID 11042166.
3. "Entrez Gene: B3GNT3 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 3".

Further reading

• 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. PMID 10580128.
• Kimura K, Wakamatsu A, Suzuki Y; et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Otsuki T, Ota T, Nishikawa T; et al. (2007). "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. doi:10.1093/dnares/12.2.117. PMID 16303743.
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Clark HF, Gurney AL, Abaya E; et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Yeh JC, Hiraoka N, Petryniak B; et al. (2001). "Novel sulfated lymphocyte homing receptors and their control by a Core1 extension beta 1,3-N-acetylglucosaminyltransferase.". Cell 105 (7): 957–69. doi:10.1016/S0092-8674(01)00394-4. PMID 11439191.
• Dias Neto E, Correa RG, Verjovski-Almeida S; et al. (2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags.". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491–6. doi:10.1073/pnas.97.7.3491. PMC 16267. PMID 10737800.
• 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. PMID 9373149.
• 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. PMID 8125298.

External links

• B3GNT3 human gene location in the UCSC Genome Browser.
• B3GNT3 human gene details in the UCSC Genome Browser.