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InterPro: IPR015827 Alpha-(1,6)-fucosyltransferase, eukaryotic type

Protein matchesHelp
UniProtKB
Matches:
40 proteins
AccessionHelp IPR015827 Alpha1_6FUT_euk
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR001452 Src homology-3 domain
GO Term annotationHelp
Process GO:0033578 protein amino acid glycosylation in Golgi
Function GO:0008424 glycoprotein 6-alpha-L-fucosyltransferase activity
Component GO:0016021 integral to membrane
GO:0032580 Golgi cisterna membrane
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Members of this group have enzymatic activity EC:2.4.1.68. They transfer fucose on glycoproteins to the innermost asparagine-linked N-acetylglucosamine of the chitobiose disaccharide-core unit [1]. Core alpha 1,6-fucosylation is a conserved feature of animal N-linked oligosaccharides, being present in both invertebrates and vertebrates [2].

All known fucosyltransferases are type II transmembrane proteins with four distinct domains: cytoplasmic, transmembrane, hypervariable, and catalytic. The catalytic domain resides in the luminal side of the trans-Golgi compartment [3]. Members of this group share the conserved three alpha-6-motifs that are also present in the bacterial 6-alpha fucosyltransferases (IPR008716) [4].

Disruption of the 6-alpha fucosyltransferase gene from a Chinese hamster ovary cell line has been shown to produce completely defucosylated recombinant antibodies [5].

All members contain an SH3 domain (IPR001452) near the carboxyl end, but its function is unknown.

Database linksHelp
Enzyme: EC:2.4.1.68

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR015827 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P79282 Alpha-(1,6)-fucosyltransferase

Q9BYC5 Alpha-(1,6)-fucosyltransferase

Q9VYV5 Alpha-(1,6)-fucosyltransferase

Q9WTS2 Alpha-(1,6)-fucosyltransferase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR001452 Src homology-3 domain
IPR015827 Alpha-(1,6)-fucosyltransferase, eukaryotic type
SWISS-MODEL
PDB Chain
ModBase

PublicationsHelp
1. Oriol R, Mollicone R, Cailleau A, Balanzino L, Breton C.
Divergent evolution of fucosyltransferase genes from vertebrates, invertebrates, and bacteria.
Glycobiology 9 323-34 1999 [PubMed: 10089206]
http://dx.doi.org/10.1093/glycob/9.4.323
2. Paschinger K, Staudacher E, Stemmer U, Fabini G, Wilson IB.
Fucosyltransferase substrate specificity and the order of fucosylation in invertebrates.
Glycobiology 15 463-74 2005 [PubMed: 15604090]
http://dx.doi.org/10.1093/glycob/cwi028
3. Paulson JC, Colley KJ.
Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation.
J. Biol. Chem. 264 17615-8 1989 [PubMed: 2681181]
http://intl.jbc.org/cgi/content/abstract/264/30/17615
4. Breton C, Oriol R, Imberty A.
Conserved structural features in eukaryotic and prokaryotic fucosyltransferases.
Glycobiology 8 87-94 1998 [PubMed: 9451017]
http://dx.doi.org/10.1093/glycob/8.1.87
5. Yamane-Ohnuki N, Kinoshita S, Inoue-Urakubo M, Kusunoki M, Iida S, Nakano R, Wakitani M, Niwa R, Sakurada M, Uchida K, Shitara K, Satoh M.
Establishment of FUT8 knockout Chinese hamster ovary cells: an ideal host cell line for producing completely defucosylated antibodies with enhanced antibody-dependent cellular cytotoxicity.
Biotechnol. Bioeng. 87 614-22 2004 [PubMed: 15352059]
http://dx.doi.org/10.1002/bit.20151

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InterPro 23.1