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Literature summary extracted from

  • Matsumoto, K.; Ishio, A.; Matsuno, K.
    O-Fucose glycan in Drosophila Notch signaling (2015), Glycosci. Biol. Med., 2015, 841-847.
No PubMed abstract available

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.222 Golgi apparatus
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 Drosophila melanogaster 5794
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Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.222 additional information Drosophila melanogaster Drosophila Fringe glycosyltransferase adds GlcNAc specifically to the O-fucose residues of Notch transmembrane proteins ?
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 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.222 Drosophila melanogaster
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.222 additional information Drosophila Fringe glycosyltransferase adds GlcNAc specifically to the O-fucose residues of Notch transmembrane proteins Drosophila melanogaster ?
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 ?

General Information

EC Number General Information Comment Organism
2.4.1.222 malfunction Fringe-dependent Notch signaling is disrupted in a nac and Efr double mutant, reduction of Notch signaling may account for the developmental defects associated with CDG IIc Drosophila melanogaster
2.4.1.222 metabolism Fringe-dependent Notch signaling, overview Drosophila melanogaster
2.4.1.222 physiological function Drosophila Fringe is a glycosyltransferase, which adds GlcNAc specifically to the O-fucose residues on EGF-like repeats of Notch protein. The O-fucose is important as an acceptor for GlcNAc. The GlcNAc modification modulates the binding between Notch and two different ligands for Notch. This modulation of Notch-ligand interaction is required for region-specific activation of Notch signaling, which is essential for morphogenesis of various organs Drosophila melanogaster