| Identification |
|---|
| HMDB Protein ID
| HMDBP12306 |
| Secondary Accession Numbers
| None |
| Name
| 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT3 |
| Synonyms
|
- Alpha-3-fucosyltransferase FUT3
- Blood group Lewis alpha-4-fucosyltransferase
- FUTB
- Fucosyltransferase 3
- Fucosyltransferase III
- Lewis FT
- FucT-III
|
| Gene Name
| FUT3 |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Not Available |
| Specific Function
| Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to both the subterminal N-acetyl glucosamine (GlcNAc) of type 1 chain (beta-D-Gal-(1->3)-beta-D-GlcNAc) glycolipids and oligosaccharides via an alpha(1,4) linkage, and the subterminal glucose (Glc) or GlcNAc of type 2 chain (beta-D-Gal-(1->4)-beta-D-GlcNAc) oligosaccharides via an alpha(1,3) linkage, independently of the presence of terminal alpha-L-fucosyl-(1,2) moieties on the terminal galactose of these acceptors and participates in the blood groups Lewis determination and expression of Lewis a (Le(a)), lewis b (Le(b)), Lewis x/SSEA-1 (Le(x)) and lewis y (Le(y)) antigens. Also catalyzes the transfer of L-fucose to subterminal GlcNAc of sialyl- and disialyl-lactotetraosylceramide to produce sialyl Lewis a (sLe(a)) and disialyl Lewis a via an alpha(1,4) linkage and therefore may regulate cell surface sialyl Lewis a expression and consequently regulates adhesive properties to E-selectin, cell proliferation and migration. Catalyzes the transfer of an L-fucose to 3'-sialyl-N-acetyllactosamine by an alpha(1,3) linkage, which allows the formation of sialyl-Lewis x structure and therefore may regulate the sialyl-Lewis x surface antigen expression and consequently adhesive properties to E-selectin. Prefers type 1 chain over type 2 acceptors. Type 1 tetrasaccharide is a better acceptor than type 1 disaccharide suggesting that a beta anomeric configuration of GlcNAc in the substrate is preferred. Lewis-positive (Le(+)) individuals have an active enzyme while Lewis-negative (Le(-)) individuals have an inactive enzyme. |
| Pathways
|
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| protein glycosylation |
| regulation of cell proliferation |
| oligosaccharide metabolic process |
| regulation of cell migration |
| fucosylation |
| positive regulation of cell-cell adhesion |
| Cellular Component |
| integral to membrane |
| Golgi cisterna membrane |
| Molecular Function |
| 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity |
| alpha-(1->3)-fucosyltransferase activity |
| 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity |
|
| Cellular Location
|
Not Available
|
| Gene Properties |
|---|
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| Not Available |
| Gene Sequence
|
Not Available
|
| Protein Properties |
|---|
| Number of Residues
| Not Available |
| Molecular Weight
| 42654.04 |
| Theoretical pI
| Not Available |
| Pfam Domain Function
|
|
| Signals
|
Not Available
|
|
Transmembrane Regions
|
|
| Protein Sequence
|
Not Available
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| Q11126 |
| UniProtKB/Swiss-Prot Entry Name
| FUT3_BOVIN |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Oulmouden A, Wierinckx A, Petit JM, Costache M, Palcic MM, Mollicone R, Oriol R, Julien R: Molecular cloning and expression of a bovine alpha(1,3)-fucosyltransferase gene homologous to a putative ancestor gene of the human FUT3-FUT5-FUT6 cluster. J Biol Chem. 1997 Mar 28;272(13):8764-73. doi: 10.1074/jbc.272.13.8764. [PubMed:9079712 ]
- Wierinckx A, Mercier D, Oulmouden A, Petit JM, Julien R: Complete genomic organization of futb encoding a bovine alpha 3-fucosyltransferase: exons in human orthologous genes emerged from ancestral intronic sequences. Mol Biol Evol. 1999 Nov;16(11):1535-47. doi: 10.1093/oxfordjournals.molbev.a026066. [PubMed:10555285 ]
|
