FUT9

FUT9
Identifiers
Aliases	FUT9 , Fuc-TIX, fucosyltransferase 9
External IDs	OMIM: 606865; MGI: 1330859; HomoloGene: 4800; GeneCards: FUT9; OMA:FUT9 - orthologs
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 Bgee Human Mouse (ortholog) Top expressed in pylorus cerebellar vermis Brodmann area 46 endothelial cell orbitofrontal cortex postcentral gyrus Brodmann area 23 middle temporal gyrus entorhinal cortex pars reticulata Top expressed in lobe of cerebellum cerebellar vermis lateral geniculate nucleus medial geniculate nucleus dorsal tegmental nucleus medial dorsal nucleus lateral hypothalamus medial vestibular nucleus deep cerebellar nuclei globus pallidus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function glycosyltransferase activity 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

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

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. S2CID   21861521.
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. S2CID   85080516.
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. S2CID   37842289.
• 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2003Natur.425..805M. 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.