FUT9

Alpha-(1,3)-fucosyltransferase is an enzyme that in humans is encoded by the FUT9 gene.[5][6][7]

FUT9
Identifiers
Aliases	FUT9, Fuc-TIX, fucosyltransferase 9
External IDs	OMIM: 606865 MGI: 1330859 HomoloGene: 4800 GeneCards: FUT9
Gene location (Human) Chr. Chromosome 6 (human)[1] Band 6q16.1 Start 96,015,974 bp[1] End 96,215,612 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4 A3|4 10.59 cM Start 25,609,332 bp[2] End 25,800,244 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity, transferring glycosyl groups • alpha-(1->3)-fucosyltransferase activity • fucosyltransferase activity • transferase activity Cellular component • integral component of membrane • Golgi apparatus • Golgi cisterna membrane • membrane • Golgi membrane Biological process • L-fucose catabolic process • fucosylation • nervous system development • protein glycosylation • carbohydrate metabolic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10690	14348
Ensembl	ENSG00000172461	ENSMUSG00000055373
UniProt	Q9Y231	O88819
RefSeq (mRNA)	NM_006581	NM_010243
RefSeq (protein)	NP_006572	NP_034373
Location (UCSC)	Chr 6: 96.02 – 96.22 Mb	Chr 4: 25.61 – 25.8 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

FUT9 is one of several alpha-3-fucosyltransferases that can catalyze the last step in the biosynthesis of Lewis antigen, the addition of a fucose to precursor polysaccharides. FUT9 synthesizes the LeX oligosaccharide (CD15), which is expressed in organ buds progressing in mesenchyma during human embryogenesis.[supplied by OMIM][7]

References

1. GRCh38: Ensembl release 89: ENSG00000172461 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000055373 - 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. Kaneko M, Kudo T, Iwasaki H, Ikehara Y, Nishihara S, Nakagawa S, Sasaki K, Shiina T, Inoko H, Saitou N, Narimatsu H (Jul 1999). "Alpha1,3-fucosyltransferase IX (Fuc-TIX) is very highly conserved between human and mouse; molecular cloning, characterization and tissue distribution of human Fuc-TIX". FEBS Lett. 452 (3): 237–42. doi:10.1016/S0014-5793(99)00640-7. PMID 10386598.
6. Kaneko M, Kudo T, Iwasaki H, Shiina T, Inoko H, Kozaki T, Saitou N, Narimatsu H (Jan 2000). "Assignment of the human alpha 1,3-fucosyltransferase IX gene (FUT9) to chromosome band 6q16 by in situ hybridization". Cytogenet Cell Genet. 86 (3–4): 329–30. doi:10.1159/000015329. PMID 10575236.
7. "Entrez Gene: FUT9 fucosyltransferase 9 (alpha (1,3) fucosyltransferase)".

Further reading

• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Nishihara S, Iwasaki H, Kaneko M, et al. (2000). "Alpha1,3-fucosyltransferase 9 (FUT9; Fuc-TIX) preferentially fucosylates the distal GlcNAc residue of polylactosamine chain while the other four alpha1,3FUT members preferentially fucosylate the inner GlcNAc residue". FEBS Lett. 462 (3): 289–94. doi:10.1016/S0014-5793(99)01549-5. PMID 10622713.
• Cailleau-Thomas A, Coullin P, Candelier JJ, et al. (2000). "FUT4 and FUT9 genes are expressed early in human embryogenesis". Glycobiology. 10 (8): 789–802. doi:10.1093/glycob/10.8.789. PMID 10929005.
• Nakayama F, Nishihara S, Iwasaki H, et al. (2001). "CD15 expression in mature granulocytes is determined by alpha 1,3-fucosyltransferase IX, but in promyelocytes and monocytes by alpha 1,3-fucosyltransferase IV". J. Biol. Chem. 276 (19): 16100–6. doi:10.1074/jbc.M007272200. PMID 11278338.
• 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.
• Toivonen S, Nishihara S, Narimatsu H, et al. (2003). "Fuc-TIX: a versatile alpha1,3-fucosyltransferase with a distinct acceptor- and site-specificity profile". Glycobiology. 12 (6): 361–8. doi:10.1093/glycob/12.6.361. PMID 12107078.
• Li H, Kong Y, Yan B (2003). "[Regulation by ovarian hormones of alpha 1,3-fucosyltransferase gene (FUT9) expression in human endometrium]". Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao. 34 (6): 775–9. PMID 12417923.
• 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.
• Nishihara S, Iwasaki H, Nakajima K, et al. (2004). "Alpha1,3-fucosyltransferase IX (Fut9) determines Lewis X expression in brain". Glycobiology. 13 (6): 445–55. doi:10.1093/glycob/cwg048. PMID 12626397.
• Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
• 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.
• Bogoevska V, Horst A, Klampe B, et al. (2006). "CEACAM1, an adhesion molecule of human granulocytes, is fucosylated by fucosyltransferase IX and interacts with DC-SIGN of dendritic cells via Lewis x residues". Glycobiology. 16 (3): 197–209. doi:10.1093/glycob/cwj057. PMID 16282604.