FUT6

Alpha-(1,3)-fucosyltransferase is an enzyme that in humans is encoded by the FUT6 gene.[3][4][5]

FUT6
Identifiers
Aliases	FUT6, FCT3A, FT1A, Fuc-TVI, FucT-VI, fucosyltransferase 6
External IDs	OMIM: 136836 HomoloGene: 34780 GeneCards: FUT6
Gene location (Human) Chr. Chromosome 19 (human)[1] Band 19p13.3 Start 5,830,408 bp[1] End 5,839,722 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • alpha-(1->3)-fucosyltransferase activity • 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity • transferase activity, transferring glycosyl groups • fucosyltransferase activity Cellular component • integral component of membrane • Golgi cisterna membrane • Golgi apparatus • extracellular exosome • membrane • Golgi membrane Biological process • protein glycosylation • L-fucose catabolic process • fucosylation • ceramide metabolic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	2528	n/a
Ensembl	ENSG00000156413	n/a
UniProt	P51993	n/a
RefSeq (mRNA)	NM_000150 NM_001040701 NM_001369502 NM_001369504 NM_001369505 NM_001381955 NM_001381956 NM_001381957 NM_001381958 NM_001381959	n/a
RefSeq (protein)	NP_000141 NP_001035791 NP_001356431 NP_001356433 NP_001356434 NP_001368884 NP_001368885 NP_001368886 NP_001368887 NP_001368888	n/a
Location (UCSC)	Chr 19: 5.83 – 5.84 Mb	n/a
PubMed search	[2]	n/a
Wikidata
View/Edit Human

The alpha-1,3-fucosyltransferases constitute a large family of glycosyltransferases with a high degree of homology. The enzymes of this family comprise 3 main activity patterns called myeloid, plasma, and Lewis, based on their capacity to transfer alpha-L-fucose to distinct oligosaccharide acceptors, their sensitivity to N-ethylmaleimide inhibition, their cation requirements, and their tissue-specific expression patterns. The different categories of alpha-1,3-fucosyltransferases are sequentially expressed during embryo-fetal development.[supplied by OMIM][5]

References

1. GRCh38: Ensembl release 89: ENSG00000156413 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. Koszdin KL, Bowen BR (Oct 1992). "The cloning and expression of a human alpha-1,3 fucosyltransferase capable of forming the E-selectin ligand". Biochem Biophys Res Commun. 187 (1): 152–7. doi:10.1016/S0006-291X(05)81472-X. PMID 1520296.
4. McCurley RS, Recinos A III, Olsen AS, Gingrich JC, Szczepaniak D, Cameron HS, Krauss R, Weston BW (Jul 1995). "Physical maps of human alpha (1,3)fucosyltransferase genes FUT3-FUT6 on chromosomes 19p13.3 and 11q21". Genomics. 26 (1): 142–6. doi:10.1016/0888-7543(95)80094-3. PMID 7782074.
5. "Entrez Gene: FUT6 fucosyltransferase 6 (alpha (1,3) fucosyltransferase)".

Further reading

• Weston BW, Smith PL, Kelly RJ, Lowe JB (1992). "Molecular cloning of a fourth member of a human alpha (1,3)fucosyltransferase gene family. Multiple homologous sequences that determine expression of the Lewis x, sialyl Lewis x, and difucosyl sialyl Lewis x epitopes". J. Biol. Chem. 267 (34): 24575–84. PMID 1339443.
• Cameron HS, Szczepaniak D, Weston BW (1995). "Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms". J. Biol. Chem. 270 (34): 20112–22. doi:10.1074/jbc.270.34.20112. PMID 7650030.
• 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.
• Mollicone R, Reguigne I, Fletcher A, et al. (1994). "Molecular basis for plasma alpha(1,3)-fucosyltransferase gene deficiency (FUT6)". J. Biol. Chem. 269 (17): 12662–71. PMID 8175676.
• 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.
• Borsig L, Imbach T, Höchli M, Berger EG (2000). "alpha1,3Fucosyltransferase VI is expressed in HepG2 cells and codistributed with beta1,4galactosyltransferase I in the golgi apparatus and monensin-induced swollen vesicles". Glycobiology. 9 (11): 1273–80. doi:10.1093/glycob/9.11.1273. PMID 10536043.
• Schnyder-Candrian S, Borsig L, Moser R, Berger EG (2000). "Localization of alpha 1,3-fucosyltransferase VI in Weibel-Palade bodies of human endothelial cells". Proc. Natl. Acad. Sci. U.S.A. 97 (15): 8369–74. doi:10.1073/pnas.97.15.8369. PMC 26954. PMID 10900002.
• Kamińska J, Musielak M, Nowicka A, et al. (2001). "Neutrophils promote the release of alpha-6-fucosyltransferase from blood platelets through the action of cathepsin G and elastase". Biochimie. 83 (8): 739–42. doi:10.1016/S0300-9084(01)01306-2. PMID 11530205.
• Roos C, Kolmer M, Mattila P, Renkonen R (2002). "Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism". J. Biol. Chem. 277 (5): 3168–75. doi:10.1074/jbc.M107927200. PMID 11698403.
• 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.
• Kanoh A, Ota M, Narimatsu H, Irimura T (2003). "Expression levels of FUT6 gene transfected into human colon carcinoma cells switch two sialyl-Lewis X-related carbohydrate antigens with distinct properties in cell adhesion". Biochem. Biophys. Res. Commun. 303 (3): 896–901. doi:10.1016/S0006-291X(03)00420-0. PMID 12670495.
• Martinez-Duncker I, Michalski JC, Bauvy C, et al. (2004). "Activity and tissue distribution of splice variants of alpha6-fucosyltransferase in human embryogenesis". Glycobiology. 14 (1): 13–25. doi:10.1093/glycob/cwh006. PMID 14514715.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• 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.
• Higai K, Miyazaki N, Azuma Y, Matsumoto K (2007). "Interleukin-1beta induces sialyl Lewis X on hepatocellular carcinoma HuH-7 cells via enhanced expression of ST3Gal IV and FUT VI gene". FEBS Lett. 580 (26): 6069–75. doi:10.1016/j.febslet.2006.09.073. PMID 17054948.