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FUT8 (fucosyltransferase 8 (alpha (1,6) fucosyltransferase))

Written2010-08Hideyuki Ihara, Cong-xiao Gao, Yoshitaka Ikeda, Naoyuki Taniguchi
Division of Molecular Cell Biology, Department of Biomolecular Sciences, Saga University Faculty of Medicine, Saga, Japan (HI, YI); Department of Disease Glycomics, Institute of Scientific, Industrial Research, Osaka University, Osaka, Japan (CXG, NT); Disease Glycomics Team, Systems Glycobiology Research Group, Chemical Biology Department, Japan (NT)

(Note : for Links provided by Atlas : click)

Identity

Alias_names6) fucosyltransferase
Other aliasMGC26465
HGNC (Hugo) FUT8
LocusID (NCBI) 2530
Atlas_Id 40649
Location 14q23.3  [Link to chromosome band 14q23]
Location_base_pair Starts at 65877310 and ends at 66210839 bp from pter ( according to hg19-Feb_2009)  [Mapping FUT8.png]
Fusion genes
(updated 2016)
ATG14 (14q22.3) / FUT8 (14q23.3)FUT8 (14q23.3) / AGBL4 (1p33)FUT8 (14q23.3) / AL139022.1 ()
FUT8 (14q23.3) / CCDC85C (14q32.2)FUT8 (14q23.3) / CTNNA1 (5q31.2)FUT8 (14q23.3) / FNTB (14q23.3)
FUT8 (14q23.3) / IFT52 (20q13.12)FUT8 (14q23.3) / NUMB (14q24.2)FUT8 (14q23.3) / SIPA1L1 (14q24.2)
IFRD1 (7q31.1) / FUT8 (14q23.3)

DNA/RNA

 
  Figure 1. Genomic organization of human FUT8 gene. Exons are represented by vertical bars. Exons denoted by ATG or TAA contain start and stop codons, respectively. These exons also have a part of the noncoding region.
Description Human FUT8 gene is located on chromosome 14q23.3 (Yamaguchi et al., 1999). This gene encompasses approximately 333 kb and contains nine exons with coding regions and three 5'-untranslated exons (Yamaguchi et al., 2000; Martinez-Duncker et al., 2004).
Transcription Some splicing variants of the 5'-untranslated region arise in a developmental stage-specific and tissue-specific manner (Martinez-Duncker et al., 2004). At least three different promoters appear to be functional in regulating the expression of the FUT8 gene. Three transcripts with different 5'-untranslated regions have been identified. With respect to coding region, four variants were reported to encode polypeptides containing 575, 446, 308 and 169 amino acid residues. The 575 residue protein is a fully active alpha1,6-fucosyltransferase, which was first of the variants to be identified. The other variants have not yet been examined for enzymatic activity and biological function. The 308 amino acid variant is known to be expressed in the retina (Yamaguchi et al., 2000).

Protein

 
  Figure 2. Protein structure of FUT8. CT and TM denote the cytoplasmic tail and the transmembrane domain, respectively. I, II and III represent the conserved motifs in alpha1,2-, alpha1,6- and protein O-fucosyltransferases.
Description FUT8 was purified and cloned as a cDNA from porcine brain and a human gastric cancer cell line (Uozumi et al., 1996, Yanagidani et al., 1997). Human FUT8 is comprised of 575 amino acids, with a calculated molecular weight of 66516. FUT8 contains no N-glycosylation sites. This enzyme belongs to the GT23 family of the CaZY classification. The structual analysis of a transmembrane domain-truncated form of FUT8 showed that the enzyme consists of a catalytic domain, an N-terminal coiled-coil domain and a C-terminal SH3 domain (Ihara et al., 2007). The catalytic domain was structurally classfied as a member of the GT-B group of glycosylatransferases.
Expression FUT8 gene is widely expressed in human tissues (Martinez-Duncker et al., 2004). The FUT8 gene is expressed at relatively high levels in the brain, placenta, lung, stomach, small intestine and jejunum, while pancreas, uterus, kidney and urinary bladder exhibit moderate expression. The FUT8 gene is weakly expressed in the heart, ileum, colon and spleen. On the other hand, the expression is not detectable in the normal liver (Miyoshi et al., 1997).
Localisation FUT8 is a typical type II membrane protein and is localized in the Golgi apparatus.
 
  Figure 3. The reaction catalysed by FUT8.
Function FUT8 catalyzes the transfer of a fucose residue from GDP-fucose to the reducing terminal GlcNAc of Asn-linked oligosaccharide (N-glycan) via an alpha1.6-linkage (Figure 3). The resulting fucosyl residue is often refered to as a core fucose. The reaction does not require any divalent cations or cofactors. The deletion of the FUT8 gene in mice leads to severe phenotypes that exhibit growth retardation, lung emphysema and death during postnatal development (Wang et al., 2005). As has been clearly shown in studies using knockout mice, the lack of core fucosylation resulted in the biological activities of various proteins to be perturbed (Taniguchi et al., 2006; Takahashi et al., 2009). Examples of this include the TGF-beta1 receptor (Wang et al., 2005), EGF receptor (Wang et al., 2006), VEGF receptor-2 (Wang et al., 2009), LRP-1 (Lee et al., 2006), E-cadherin (Osumi et al., 2009), alpha3beta1 integrin (Zhao et al., 2006), VCAM and alpha4beta1 integrin (Li et al., 2008). The binding affinity of the core fucose-deleted TGF-beta receptor to TGF-beta 1 is diminished in fut8-null mice, resulting in the downregulation of TGF-beta 1 signaling (Wang et al., 2005). The unusual overexpression of matrix metalloproteinases such as MMP-12 and MMP-13 is associated with the impaired receptor function, and has been proposed to cause the lung-destructive phenotypes. The EGF receptor in fut8 null mice is also affected in terms of its binding affinity to EGF and EGF-induced phoshorylation (Wang et al., 2006). These studies strongly suggest that FUT8 and core fucose structures regulate the receptor function.
In addition, core fucosylation was reported to be involved in antibodydependent cellular cytotoxicity (ADCC) (Shields et al., 2002; Shinkawa et al., 2003). The lack of core fucose of N-glycan in the Fc region of the IgG1 molecule enhances ADCC activity up to 50-100-fold. This discorvery promises to be useful in the development of antibody therapy in cancer treatment.
Homology The sequence identities between human FUT8 and other organisms are as follows :
Chimpangee (100%), Dog (97.7%), Cow (97.5%), Pig (95.6%), Rat (96.6%), Mouse (96.5%), Chicken (93.9%), Clawed frog (90.3%), Zebrafish (79.5%), Takifugu (80.2%), Tetraodon (79.8%), Sea squirt (23.2%), Fruit fly (43.7%), C. elegans (34.8%).
Eight cysteine residues in the catalytic domain are conserved among these species, except for ciona (Ihara et al., 2007).
FUT8 contains three short regions that are highly conserved in FUT8, alpha1,2-, bacterial alpha1,6-, and protein O-fucosyltransferases (Oriol et al., 1999; Takahashi et al., 2000a; Chazalet et al., 2001; Martinez-Duncker et al., 2003). The structual analysis has shown that these regions are located adjacent to one another in the Rossmann fold of FUT8 (Ihara et al., 2007). In addition, the C-terminal SH3 domain of FUT8 is structually similar to the typical SH3 domain that is found in many proteins.

Mutations

Note One frame-shit mutation and 4 substitution mutants have been identified to date in various SNPs of the FUT8 gene. The frame shift mutant is due to the insertion of a T at position 2 of the codon for Val-85, resulting in 85-VLEEQLVK-92 being change to 85-VFRRAACter-92. The four substitution mutants are K101Q, L153V, E181G and T267K. These mutants are due to A being substituted by C at position 1 of codon 101, C to G at position 1 of codon 153, A to G at position 2 of codon 181, and C to A at posision 2 of codon 267, respectively. Effects of these substitutions on enzymatic activity are not currently known.

Implicated in

Note
  
Entity Hepatocellular carcinoma (HCC)
Note It is well known that the core fucosylation of alpha-fetoprotein (AFP) is implicated in the development of HCC. AFP is a major fetal plasma protein, and its expression is elevated in hepatic diseases such as HCC, hepatitis and liver cirrhosis (Alpert et al., 1968; Ruoslahti et al., 1974). The AFP-L3 fraction was identified as the core-fucosylated isoform of AFP. The elevation in serum and liver tissue was found to be specific to HCC, but was not observed in other liver diseases (Taketa, 1990; Aoyagi, 1995; Miyoshi et al., 1999).
Thus, it appears that AFP-L3 could be used as a marker for HCC. The FUT8 gene is not expressed in the normal adult liver, but is highly expressed in HCC tissue. Surprisingly, however, such an elevation was also observed in liver cirrhosis in spite of the absence of a concomitant increase in AFP-L3 levels (Noda et al., 1998). This discrepancy can be attributed to the difference in the synthesis of GDP-fucose, a glycosyl donor substrate for fucosyltransferases, including FUT8, and by the altered intracellular sorting of fucosylated glycoproteins in hepatic cells. Because the intracellular concentration of GDP-fucose is higher in HCC, as compared to a normal liver, chronic hepatitis and liver cirrhosis, this increase would be expected to facilitate core fucosyltion of AFP (Noda et al., 2003). Core fucosylation appears to serve as a sorting signal for a glycoprotein to be directed to the bile, as revealed by the predominant distribution of fucosylated glycoproteins in bile rather than serum (Nakagawa et al., 2006). In fact, the levels of alpha-antitrypsin and alpha1-acid glycoprotein, both of which are fucosylated glycoproteins, are quite low in the bile of Fut8-null mice. The loss of polarity in cancer cells is likely to impair the regulated sorting, thus allowing abnormal secretion into the serum.
Prognosis AFP-L3-positive HCC patients were reported to show a poor prognosis (Yamashita et al., 1996).
  
  
Entity Ovarian cancer
Note FUT8 activity and mRNA levels are highly and specifically elavated in cases of ovarian serous adenocarcinoma, as compared to nomal ovary and other types of epithelial ovarian carcinoma (Takahashi et al., 2000b). In addition, core fucosylation levels in glycoproteins is also significantlly increased in cases of serous adenocarcinoma tissues.
  
  
Entity Thyroid cancer
Note The overexpression of FUT8 occurs in 33.3% of cases of papillary carcinoma of the thyroid (Ito et al., 2003), although FUT8 was not expressed in normal follicular cells. This overexpression was also shown to be correlated with tumor size and lymph node metastasis. These phenomena were not observed in cases of follicular carcinoma and anaplastic carcinoma.
  
  
Entity Pancreatic cancer
Note Haptoglobin was identified as a highly fucosylated glycoprotein in the serum of patients with pancreatic cancer (Okuyama et al., 2006). The increment of fucosylated haptoglobin was observed in pancreatic cancer rather than other diseases such as HCC, liver cirrhosis, gastric cancer and colon cancer, and also appeared to be correlated with the clinical stage. Structural analyses using lectin blotting and mass spectrometry showed that core fucosylation as well as alpha1,3/4-fucosylation is increased in haptoglobin from the serum of such patients. In addition, it was shown that interleukin 6 expressed in pancreatic cancer is a possible inducing factor for increasing the production of fucosylated haptoglobin in the liver (Narisada et al., 2008).
  
  
Entity Colorectal cancer
Note The enzymatic activity and protein expression of FUT8 were increased in tumor tissues of human colorectal carcinoma, but not in healthy tissues (Muinelo-Romay et al., 2008). This increment was well observed in cases of male, polypoid growth, no regional lymph node metastasis and early clinical stage. In addition, immunohistochemical examination has demonstrated that FUT8 is expressed at higher levels in tumor tissues of colorectal carcinoma than in healthy and transitional tissues.
  
  
Entity Cystic fibrosis
Note Fucosylation is known to be increased in cystic fibrosis. The alpha1,6-fucosylation of a membrane glycoprotein is elevated in cystic fibrosis fibroblast (Wang et al., 1990).
  

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Citation

This paper should be referenced as such :
Ihara, H ; Gao, CX ; Ikeda, Y ; Taniguchi, N
FUT8 (fucosyltransferase 8 (alpha (1,6) fucosyltransferase))
Atlas Genet Cytogenet Oncol Haematol. 2011;15(5):410-414.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/FUT8ID40649ch14q23.html


External links

Nomenclature
HGNC (Hugo)FUT8   4019
Cards
AtlasFUT8ID40649ch14q23
Entrez_Gene (NCBI)FUT8  2530  fucosyltransferase 8
Aliases
GeneCards (Weizmann)FUT8
Ensembl hg19 (Hinxton)ENSG00000033170 [Gene_View]  chr14:65877310-66210839 [Contig_View]  FUT8 [Vega]
Ensembl hg38 (Hinxton)ENSG00000033170 [Gene_View]  chr14:65877310-66210839 [Contig_View]  FUT8 [Vega]
ICGC DataPortalENSG00000033170
TCGA cBioPortalFUT8
AceView (NCBI)FUT8
Genatlas (Paris)FUT8
WikiGenes2530
SOURCE (Princeton)FUT8
Genetics Home Reference (NIH)FUT8
Genomic and cartography
GoldenPath hg19 (UCSC)FUT8  -     chr14:65877310-66210839 +  14q24.3   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)FUT8  -     14q24.3   [Description]    (hg38-Dec_2013)
EnsemblFUT8 - 14q24.3 [CytoView hg19]  FUT8 - 14q24.3 [CytoView hg38]
Mapping of homologs : NCBIFUT8 [Mapview hg19]  FUT8 [Mapview hg38]
OMIM602589   
Gene and transcription
Genbank (Entrez)AB049740 AF052088 AJ514324 AJ514325 AJ536053
RefSeq transcript (Entrez)NM_004480 NM_178154 NM_178155 NM_178156 NM_178157
RefSeq genomic (Entrez)NC_000014 NC_018925 NT_026437 NW_004929393
Consensus coding sequences : CCDS (NCBI)FUT8
Cluster EST : UnigeneHs.654961 [ NCBI ]
CGAP (NCI)Hs.654961
Alternative Splicing GalleryENSG00000033170
Gene ExpressionFUT8 [ NCBI-GEO ]   FUT8 [ EBI - ARRAY_EXPRESS ]   FUT8 [ SEEK ]   FUT8 [ MEM ]
Gene Expression Viewer (FireBrowse)FUT8 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)2530
GTEX Portal (Tissue expression)FUT8
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ9BYC5   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ9BYC5  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ9BYC5
Splice isoforms : SwissVarQ9BYC5
Catalytic activity : Enzyme2.4.1.68 [ Enzyme-Expasy ]   2.4.1.682.4.1.68 [ IntEnz-EBI ]   2.4.1.68 [ BRENDA ]   2.4.1.68 [ KEGG ]   
PhosPhoSitePlusQ9BYC5
Domaine pattern : Prosite (Expaxy)GT23 (PS51659)   
Domains : Interpro (EBI)Alpha1_6FUT_euk    GT23_dom    SH3_domain   
Domain families : Pfam (Sanger)SH3_9 (PF14604)   
Domain families : Pfam (NCBI)pfam14604   
Domain families : Smart (EMBL)SH3 (SM00326)  
Conserved Domain (NCBI)FUT8
DMDM Disease mutations2530
Blocks (Seattle)FUT8
PDB (SRS)2DE0   
PDB (PDBSum)2DE0   
PDB (IMB)2DE0   
PDB (RSDB)2DE0   
Structural Biology KnowledgeBase2DE0   
SCOP (Structural Classification of Proteins)2DE0   
CATH (Classification of proteins structures)2DE0   
SuperfamilyQ9BYC5
Human Protein AtlasENSG00000033170
Peptide AtlasQ9BYC5
HPRD03994
IPIIPI00004668   IPI00215828   IPI00216701   IPI01025399   IPI01025061   IPI01025652   IPI01025284   IPI01025815   IPI01025453   IPI01025924   IPI00302523   
Protein Interaction databases
DIP (DOE-UCLA)Q9BYC5
IntAct (EBI)Q9BYC5
FunCoupENSG00000033170
BioGRIDFUT8
STRING (EMBL)FUT8
ZODIACFUT8
Ontologies - Pathways
QuickGOQ9BYC5
Ontology : AmiGOGolgi membrane  in utero embryonic development  cytoplasm  Golgi apparatus  protein N-linked glycosylation  N-glycan processing  transforming growth factor beta receptor signaling pathway  integrin-mediated signaling pathway  respiratory gaseous exchange  glycoprotein 6-alpha-L-fucosyltransferase activity  glycoprotein 6-alpha-L-fucosyltransferase activity  oligosaccharide biosynthetic process  regulation of gene expression  membrane  integral component of membrane  cell migration  SH3 domain binding  protein N-linked glycosylation via asparagine  Golgi cisterna membrane  protein glycosylation in Golgi  N-glycan fucosylation  L-fucose catabolic process  receptor metabolic process  GDP-L-fucose metabolic process  extracellular exosome  regulation of cellular response to oxidative stress  
Ontology : EGO-EBIGolgi membrane  in utero embryonic development  cytoplasm  Golgi apparatus  protein N-linked glycosylation  N-glycan processing  transforming growth factor beta receptor signaling pathway  integrin-mediated signaling pathway  respiratory gaseous exchange  glycoprotein 6-alpha-L-fucosyltransferase activity  glycoprotein 6-alpha-L-fucosyltransferase activity  oligosaccharide biosynthetic process  regulation of gene expression  membrane  integral component of membrane  cell migration  SH3 domain binding  protein N-linked glycosylation via asparagine  Golgi cisterna membrane  protein glycosylation in Golgi  N-glycan fucosylation  L-fucose catabolic process  receptor metabolic process  GDP-L-fucose metabolic process  extracellular exosome  regulation of cellular response to oxidative stress  
Pathways : KEGGN-Glycan biosynthesis    Glycosaminoglycan biosynthesis - keratan sulfate    Transcriptional misregulation in cancer   
REACTOMEQ9BYC5 [protein]
REACTOME Pathways975578 [pathway]   
NDEx NetworkFUT8
Atlas of Cancer Signalling NetworkFUT8
Wikipedia pathwaysFUT8
Orthology - Evolution
OrthoDB2530
GeneTree (enSembl)ENSG00000033170
Phylogenetic Trees/Animal Genes : TreeFamFUT8
HOVERGENQ9BYC5
HOGENOMQ9BYC5
Homologs : HomoloGeneFUT8
Homology/Alignments : Family Browser (UCSC)FUT8
Gene fusions - Rearrangements
Fusion : MitelmanATG14/FUT8 [14q22.3/14q23.3]  [t(14;14)(q22;q23)]  
Fusion : MitelmanFUT8/AGBL4 [14q23.3/1p33]  [t(1;14)(p33;q23)]  
Fusion : MitelmanFUT8/CCDC85C [14q23.3/14q32.2]  [t(14;14)(q23;q32)]  
Fusion : MitelmanFUT8/FNTB [14q23.3/14q23.3]  [t(14;14)(q23;q23)]  
Fusion : MitelmanFUT8/SIPA1L1 [14q23.3/14q24.2]  [t(14;14)(q23;q24)]  
Fusion: TCGAATG14 14q22.3 FUT8 14q23.3 GBM
Fusion: TCGAFUT8 14q23.3 AGBL4 1p33 BRCA
Fusion: TCGAFUT8 14q23.3 AL139022.1 OV
Fusion: TCGAFUT8 14q23.3 CCDC85C 14q32.2 OV
Fusion: TCGAFUT8 14q23.3 FNTB 14q23.3 BRCA
Fusion: TCGAFUT8 14q23.3 SIPA1L1 14q24.2 LGG
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerFUT8 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)FUT8
dbVarFUT8
ClinVarFUT8
1000_GenomesFUT8 
Exome Variant ServerFUT8
ExAC (Exome Aggregation Consortium)FUT8 (select the gene name)
Genetic variants : HAPMAP2530
Genomic Variants (DGV)FUT8 [DGVbeta]
DECIPHER (Syndromes)14:65877310-66210839  ENSG00000033170
CONAN: Copy Number AnalysisFUT8 
Mutations
ICGC Data PortalFUT8 
TCGA Data PortalFUT8 
Broad Tumor PortalFUT8
OASIS PortalFUT8 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICFUT8  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDFUT8
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch FUT8
DgiDB (Drug Gene Interaction Database)FUT8
DoCM (Curated mutations)FUT8 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)FUT8 (select a term)
intoGenFUT8
NCG5 (London)FUT8
Cancer3DFUT8(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM602589   
Orphanet
MedgenFUT8
Genetic Testing Registry FUT8
NextProtQ9BYC5 [Medical]
TSGene2530
GENETestsFUT8
Huge Navigator FUT8 [HugePedia]
snp3D : Map Gene to Disease2530
BioCentury BCIQFUT8
ClinGenFUT8
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD2530
Chemical/Pharm GKB GenePA28435
Clinical trialFUT8
Miscellaneous
canSAR (ICR)FUT8 (select the gene name)
Probes
Litterature
PubMed57 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineFUT8
EVEXFUT8
GoPubMedFUT8
iHOPFUT8
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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