FUT6

Protein-coding gene in the species Homo sapiens
FUT6
Identifiers
AliasesFUT6, FCT3A, FT1A, Fuc-TVI, FucT-VI, fucosyltransferase 6
External IDsOMIM: 136836; HomoloGene: 34780; GeneCards: FUT6; OMA:FUT6 - orthologs
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for FUT6
Genomic location for FUT6
Band19p13.3Start5,830,408 bp[1]
End5,839,722 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • mucosa of pharynx

  • olfactory bulb

  • buccal mucosa cell

  • pancreatic ductal cell

  • nasal epithelium

  • mucosa of ileum

  • amniotic fluid

  • trachea

  • oral cavity

  • mucosa of transverse colon
    n/a
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • alpha-(1->3)-fucosyltransferase activity
  • 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity
  • glycosyltransferase activity
  • 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
SpeciesHumanMouse
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 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

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

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. ^ a b c 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. ^ a b "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. doi:10.1016/S0021-9258(18)35803-4. 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. doi:10.1016/S0021-9258(18)99927-8. 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. Bibcode:2000PNAS...97.8369S. 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. Bibcode:2002PNAS...9916899M. 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. S2CID 9731951.
  • v
  • t
  • e
2.4.1: Hexosyl-
transferases
Glucosyl-
Galactosyl-
Glucuronosyl-
Fucosyl-
Mannosyl-
2.4.2: Pentosyl-
transferases
Ribose
ADP-ribosyltransferase
Phosphoribosyltransferase
Other
Other
2.4.99: Sialyl
transferases


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