Aliases for FUT9 Gene
External Ids for FUT9 Gene
Previous GeneCards Identifiers for FUT9 Gene
The protein encoded by this gene belongs to the glycosyltransferase family. It is localized to the golgi, and catalyzes the last step in the biosynthesis of Lewis X (LeX) antigen, the addition of a fucose to precursor polysaccharides. This protein is one of the few fucosyltransferases that synthesizes the LeX oligosaccharide (CD15) expressed in the organ buds progressing in mesenchyma during embryogenesis. It is also responsible for the expression of CD15 in mature granulocytes. A common haplotype of this gene has also been associated with susceptibility to placental malaria infection. [provided by RefSeq, Nov 2011]
GeneCards Summary for FUT9 Gene
FUT9 (Fucosyltransferase 9) is a Protein Coding gene. Diseases associated with FUT9 include Malaria. Among its related pathways are Globo Sphingolipid Metabolism and Glycosphingolipid biosynthesis - lacto and neolacto series. Gene Ontology (GO) annotations related to this gene include fucosyltransferase activity and alpha-(1->3)-fucosyltransferase activity. An important paralog of this gene is FUT3.
UniProtKB/Swiss-Prot Summary for FUT9 Gene
Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a distal lactosamine unit of a glycoprotein or a glycolipid-linked polylactosamine chains through an alpha-1,3 glycosidic linkage and participates in particular to the Lewis x (Lex)/CD15 epitope biosynthesis in neurons which allows cell differentiation, cell adhesion, and initiation of neurite outgrowth (PubMed:23263199, PubMed:23192350, PubMed:10386598, PubMed:17335083, PubMed:23000574, PubMed:11278338, PubMed:10622713, PubMed:18395013, PubMed:12107078, PubMed:16282604). Also fucosylates di-, tri- and tetraantennary N-glycans linked to glycoproteins and the inner lactosamine unit of the alpha2,3-sialylated polylactosamine resulting in sLex (CD15s) epitope synthesis (PubMed:11278338, PubMed:12107078, PubMed:18395013). Furthermore, it is capable to synthesizes Lewis a (Lea), although to a lesser extent than Lex and Lewis y (Ley) and to confer SELE-dependent, but not SELL- and SELP-selectin-dependent, cell rolling and adhesion by enhancing Lex and sLex synthesis (PubMed:18395013, PubMed:23192350).