FUT9

From Wikipedia, the free encyclopedia

Fucosyltransferase 9 (alpha (1,3) fucosyltransferase)

Identifiers

FUT9; Fuc-TIX

External IDs

OMIM: 606865 MGI: 1330859 HomoloGene: 4800

Gene ontology
Molecular Function:	• transferase activity, transferring glycosyl groups • alpha(1,3)-fucosyltransferase activity
Cellular Component:	• Golgi apparatus • membrane • integral to membrane
Biological Process:	• carbohydrate metabolic process • protein amino acid glycosylation • L-fucose catabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006581 (mRNA)
NP_006572 (protein)

NM_010243 (mRNA)
NP_034373 (protein)

Location

Chr 6: 96.57 - 96.76 Mb

Chr 4: 25.7 - 25.89 Mb

Pubmed search

[1]

[2]

Fucosyltransferase 9 (alpha (1,3) fucosyltransferase), also known as FUT9, is a human gene.^[1]

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]^[1]

[edit] References

^ ^a ^b Entrez Gene: FUT9 fucosyltransferase 9 (alpha (1,3) fucosyltransferase).

[edit] Further reading

Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548.
Kaneko M, Kudo T, Iwasaki H, et al. (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. PMID 10386598.
Kaneko M, Kudo T, Iwasaki H, et al. (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. PMID 10575236.
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. 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. 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. 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. 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. 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.