FUT8

FUT8
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2DE0
Identifiers
Aliases	FUT8, fucosyltransferase 8, CDGF, CDGF1
External IDs	OMIM: 602589; MGI: 1858901; HomoloGene: 9650; GeneCards: FUT8; OMA:FUT8 - orthologs
Gene location (Human)
Chr.	Chromosome 14 (human)
End	65,744,121 bp
Gene location (Mouse)
Chr.	Chromosome 12 (mouse)
End	77,523,112 bp
RNA expression pattern
	Top expressed in
	corpus callosum; ; olfactory bulb; ; testicle; ; trigeminal ganglion; ; inferior ganglion of vagus nerve; ; pylorus; ; ventricular zone; ; C1 segment; ; subthalamic nucleus; ; Achilles tendon;
	Top expressed in
	seminal vesicula; ; sciatic nerve; ; olfactory epithelium; ; left colon; ; epithelium of stomach; ; crypt of lieberkuhn of small intestine; ; optic nerve; ; lobe of cerebellum; ; olfactory tubercle; ; cerebellar vermis;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transferase activity; glycosyltransferase activity; SH3 domain binding; glycoprotein 6-alpha-L-fucosyltransferase activity; alpha-(1->6)-fucosyltransferase activity;
Cellular component	integral component of membrane; Golgi apparatus; membrane; Golgi membrane; Golgi cisterna membrane; extracellular exosome; cytosol;
Biological process	GDP-L-fucose metabolic process; regulation of cellular response to oxidative stress; N-glycan fucosylation; N-glycan processing; in utero embryonic development; respiratory gaseous exchange by respiratory system; protein glycosylation; oligosaccharide biosynthetic process; regulation of gene expression; integrin-mediated signaling pathway; protein N-linked glycosylation; transforming growth factor beta receptor signaling pathway; cell migration; L-fucose catabolic process; receptor metabolic process; protein N-linked glycosylation via asparagine;
	Sources:Amigo / QuickGO
Orthologs
	2530
	53618
	ENSG00000033170
	ENSMUSG00000021065
	Q9BYC5
	Q9WTS2
NM_004480; NM_178154; NM_178155; NM_178156; NM_178157;
	NM_001371533; NM_001371534; NM_001371536
	NM_001252614; NM_001252615; NM_001252616; NM_016893
NP_004471; NP_835368; NP_835369; NP_001358462; NP_001358463;
	NP_001358465
	NP_001239543; NP_001239544; NP_001239545; NP_058589
	Wikidata
View/Edit Human	View/Edit Mouse

Alpha-(1,6)-fucosyltransferase is an enzyme that in humans is encoded by the FUT8 gene.^[5]^[6]

This enzyme belongs to the family of fucosyltransferases. The product of this gene catalyzes the transfer of fucose from GDP-fucose to N-linked type complex glycopeptides. This enzyme is distinct from other fucosyltransferases which catalyze alpha1-2, alpha1-3, and alpha1-4 fucose addition. The expression of this gene may contribute to the malignancy of cancer cells and to their invasive and metastatic capabilities. Alternatively spliced variants encoding different isoforms have been identified.^[6]

Kyowa Hakko Kirin's "Potelligent" platform uses a CHO cell line in which FUT8 has been knocked out to make afucosylated monoclonal antibodies.^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000033170 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000021065 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Costache M, Apoil PA, Cailleau A, Elmgren A, Larson G, Henry S, Blancher A, Iordachescu D, Oriol R, Mollicone R (Dec 1997). "Evolution of fucosyltransferase genes in vertebrates". J Biol Chem. 272 (47): 29721–8. doi:10.1074/jbc.272.47.29721. PMID 9368041.
^ ^a ^b "Entrez Gene: FUT8 fucosyltransferase 8 (alpha (1,6) fucosyltransferase)".
^ Yu, X; Marshall, MJE; Cragg, MS; Crispin, M (June 2017). "Improving Antibody-Based Cancer Therapeutics Through Glycan Engineering". BioDrugs : Clinical Immunotherapeutics, Biopharmaceuticals and Gene Therapy. 31 (3): 151–166. doi:10.1007/s40259-017-0223-8. PMID 28466278.

Miyoshi E, Noda K, Yamaguchi Y, et al. (2000). "The alpha1-6-fucosyltransferase gene and its biological significance". Biochim. Biophys. Acta. 1473 (1): 9–20. doi:10.1016/s0304-4165(99)00166-x. PMID 10580126.
Kalyanaraman VS, Rodriguez V, Veronese F, et al. (1990). "Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1" (PDF). AIDS Res. Hum. Retroviruses. 6 (3): 371–80. doi:10.1089/aid.1990.6.371. PMID 2187500.
Pal R, Hoke GM, Sarngadharan MG (1989). "Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1". Proc. Natl. Acad. Sci. U.S.A. 86 (9): 3384–8. doi:10.1073/pnas.86.9.3384. PMC 287137. PMID 2541446.
Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP (1989). "Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport". J. Virol. 63 (6): 2452–6. PMC 250699. PMID 2542563.
Kozarsky K, Penman M, Basiripour L, et al. (1989). "Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein". J. Acquir. Immune Defic. Syndr. 2 (2): 163–9. PMID 2649653.
Robinson WE, Montefiori DC, Mitchell WM (1988). "Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis". AIDS Res. Hum. Retroviruses. 3 (3): 265–82. doi:10.1089/aid.1987.3.265. PMID 2829950.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
Yanagidani S, Uozumi N, Ihara Y, et al. (1997). "Purification and cDNA cloning of GDP-L-Fuc:N-acetyl-beta-D-glucosaminide:alpha1-6 fucosyltransferase (alpha1-6 FucT) from human gastric cancer MKN45 cells". J. Biochem. 121 (3): 626–32. doi:10.1093/oxfordjournals.jbchem.a021631. PMID 9133635.
Yamaguchi Y, Fujii J, Inoue S, et al. (1999). "Mapping of the alpha-1,6-fucosyltransferase gene, FUT8, to human chromosome 14q24.3". Cytogenet. Cell Genet. 84 (1–2): 58–60. doi:10.1159/000015215. PMID 10343104.
Takahashi T, Ikeda Y, Tateishi A, et al. (2000). "A sequence motif involved in the donor substrate binding by alpha1,6-fucosyltransferase: the role of the conserved arginine residues". Glycobiology. 10 (5): 503–10. doi:10.1093/glycob/10.5.503. PMID 10764839.
Yamaguchi Y, Ikeda Y, Takahashi T, et al. (2000). "Genomic structure and promoter analysis of the human alpha1, 6-fucosyltransferase gene (FUT8)". Glycobiology. 10 (6): 637–43. doi:10.1093/glycob/10.6.637. PMID 10814706.
Takahashi T, Ikeda Y, Miyoshi E, et al. (2000). "alpha1,6fucosyltransferase is highly and specifically expressed in human ovarian serous adenocarcinomas". Int. J. Cancer. 88 (6): 914–9. doi:10.1002/1097-0215(20001215)88:6<914::AID-IJC12>3.0.CO;2-1. PMID 11093814.
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.
Coullin P, Crooijmans RP, Groenen MA, et al. (2003). "Assignment of FUT8 to chicken chromosome band 5q1.4 and to human chromosome 14q23.2→q24.1 by in situ hybridization. Conserved and compared synteny between human and chicken". Cytogenet. Genome Res. 97 (3–4): 234–8. doi:10.1159/000066611. PMID 12438718.
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.
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.
Ito Y, Miyauchi A, Yoshida H, et al. (2003). "Expression of alpha1,6-fucosyltransferase (FUT8) in papillary carcinoma of the thyroid: its linkage to biological aggressiveness and anaplastic transformation". Cancer Lett. 200 (2): 167–72. doi:10.1016/S0304-3835(03)00383-5. PMID 14568171.

External links

Overview of all the structural information available in the PDB for UniProt: Q9BYC5 (Human FUT8) at the PDBe-KB.

This article on a gene on human chromosome 14 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000033170 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000021065 – 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.

[pmid9368041-5] Costache M, Apoil PA, Cailleau A, Elmgren A, Larson G, Henry S, Blancher A, Iordachescu D, Oriol R, Mollicone R (Dec 1997). "Evolution of fucosyltransferase genes in vertebrates". J Biol Chem. 272 (47): 29721–8. doi:10.1074/jbc.272.47.29721. PMID 9368041.

[entrez-6] "Entrez Gene: FUT8 fucosyltransferase 8 (alpha (1,6) fucosyltransferase)".

[Yu2017-7] Yu, X; Marshall, MJE; Cragg, MS; Crispin, M (June 2017). "Improving Antibody-Based Cancer Therapeutics Through Glycan Engineering". BioDrugs : Clinical Immunotherapeutics, Biopharmaceuticals and Gene Therapy. 31 (3): 151–166. doi:10.1007/s40259-017-0223-8. PMID 28466278.

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References

Further reading

External links