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Literature summary extracted from

  • Rana, N.A.; Haltiwanger, R.S.
    Fringe benefits: functional and structural impacts of O-glycosylation on the extracellular domain of Notch receptors (2011), Curr. Opin. Struct. Biol., 21, 583-589.
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.221 endoplasmic reticulum lumen
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 Mus musculus 5788
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2.4.1.221 soluble
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 Mus musculus
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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 O-GlcNAc is added to Notch by an enzymatic activity distinct from the well-known nuclear/cytoplasmic O-GlcNAc transferase, OGT, EC 2.4.1.255 ?
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 ?
2.4.1.222 additional information Mus musculus O-GlcNAc is added to Notch by an enzymatic activity distinct from the well-known nuclear/cytoplasmic O-GlcNAc transferase, OGT, EC 2.4.1.255 ?
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 ?
2.4.1.222 [Notch]-fucose + UDP-alpha-D-N-acetylglucosamine Drosophila melanogaster
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 [Notch]-(3-O-beta-D-N-acetylglucosaminyl)fucose + UDP
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 ?
2.4.1.222 [Notch]-fucose + UDP-alpha-D-N-acetylglucosamine Mus musculus
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 [Notch]-(3-O-beta-D-N-acetylglucosaminyl)fucose + UDP
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.221 Drosophila melanogaster
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-
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2.4.1.221 Mus musculus
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-
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2.4.1.222 Drosophila melanogaster
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-
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2.4.1.222 Mus musculus
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-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.221 additional information Pofut1 adds fucose to Ser or Thr in the C2-x-x-x-x-(S/T)-C3 consensus sequence. Eliminating any of three highly conserved O-fucose sites at EGF 12, 26, or 27 within mouse Notch1 alters activity. Mus musculus ?
-
 ?
2.4.1.222 additional information O-GlcNAc is added to Notch by an enzymatic activity distinct from the well-known nuclear/cytoplasmic O-GlcNAc transferase, OGT, EC 2.4.1.255 Drosophila melanogaster ?
-
 ?
2.4.1.222 additional information O-GlcNAc is added to Notch by an enzymatic activity distinct from the well-known nuclear/cytoplasmic O-GlcNAc transferase, OGT, EC 2.4.1.255 Mus musculus ?
-
 ?
2.4.1.222 [Notch]-fucose + UDP-alpha-D-N-acetylglucosamine
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 Drosophila melanogaster [Notch]-(3-O-beta-D-N-acetylglucosaminyl)fucose + UDP
-
 ?
2.4.1.222 [Notch]-fucose + UDP-alpha-D-N-acetylglucosamine
-
 Mus musculus [Notch]-(3-O-beta-D-N-acetylglucosaminyl)fucose + UDP
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.221 O-fucosyltransferase 1
-
 Drosophila melanogaster
2.4.1.221 OFUT1
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 Drosophila melanogaster
2.4.1.221 Pofut1
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 Mus musculus
2.4.1.221 protein O-fucosyltransferase 1
-
 Mus musculus

General Information

EC Number General Information Comment Organism
2.4.1.221 malfunction elimination of Pofut1 in mice has a profound effect on ligand binding in both embryonic stem cells and lymphoid cells. A small decrease in cell surface expression of Notch proteins is seen in embryonic stem cells lacking Pofut1 and in somites from mice with a hypomorphic allele of Pofut1, cax Mus musculus
2.4.1.221 additional information O-glycome of Drosophila melanogaster by mass spectrometry, using beta-elimination to release the O-linked sugar modifications from total protein extracts of fly embryos, overview Drosophila melanogaster
2.4.1.221 physiological function O-fucosylation is universally required for all Notch signaling. O-Fucose and O-glucose glycans on Notch occur at specific consensus sequences within the context of EGF repeats, which make up the majority of the Notch extracellular domain. Molecular mechanisms by which O-fucose and O-glucose glycans affect Notch function Mus musculus
2.4.1.221 physiological function O-fucosylation is universally required for all Notch signaling. O-Fucose and O-glucose glycans on Notch occur at specific consensus sequences within the context of EGF repeats, which make up the majority of the Notch extracellular domain. Ofut1 might have a chaperone-like activity in Drosophila that is required for cell-surface expression of Notch in flies. Molecular mechanisms by which O-fucose and O-glucose glycans affect Notch function, overview Drosophila melanogaster
2.4.1.222 malfunction eliminating any of three highly conserved O-fucose sites at EGF 12, 26, or 27 within mouse Notch1 alters the activity in cell-based Notch signaling assays. EGF 12 is part of the ligand-binding region of Notch, a mouse line carrying a point mutation in the O-fucosylation site of EGF 12 in endogenous Notch1 shows loss of this site which results in a mild Notch phenotype with defects in T cell development Mus musculus
2.4.1.222 metabolism O-GlcNAc is added to Notch by an enzymatic activity distinct from the well-known nuclear/cytoplasmic O-GlcNAc transferase, OGT, EC 2.4.1.255. The structure GlcNAcbeta1-3Fucalpha1-OSer/Thr can be further elongated in mammals to the tetrasaccharide by sequential action of a beta1-4galactosyltransferase and an alpha2-3 or alpha2-6sialyltransferase Mus musculus
2.4.1.222 additional information Fringe elongation to the GlcNAc-beta1,3-fucose causes a significant conformational shift of several residues within the O-fucose consensus region. This may provide a mechanism for how Fringe modification indirectly exerts its effects on Notch activity at EGF 12 Mus musculus
2.4.1.222 physiological function the O-fucose and O-glucose glycans on Notch occur at specific consensus sequences within the context of EGF repeats, which make up the majority of the Notch extracellulr domain. O-GlcNAc modification, a third form of O-glycosylation, occurs on EGF repeats, on hydroxy amino acids between the fifth and sixth conserved Cys of an EGF repeat. Similar to O-fucosylation, the major effect of Fringe-mediated O-fucose elongation appears to be modulation of Notch-ligand binding, whereby Delta activation of Notch is potentiated, while signaling via Serrate is inhibited. GlcNAc is the terminal sugar added to O-fucose residues on Drosophila Notch, and the disaccharide is sufficient for observing a Fringe effect, In vitro extension to trisaccharide causes no change in in vitro ligand binding as assessed in vitro Drosophila melanogaster
2.4.1.222 physiological function the O-fucose and O-glucose glycans on Notch occur at specific consensus sequences within the context of EGF repeats, which make up the majority of the Notch extracellulr domain. O-GlcNAc modification, a third form of O-glycosylation, occurs on EGF repeats, on hydroxy amino acids between the fifth and sixth conserved Cys of an EGF repeat. Similar to O-fucosylation, the major effect of Fringe-mediated O-fucose elongation appears to be modulation of Notch-ligand binding, whereby Delta activation of Notch is potentiated, while signaling via Serrate is inhibited. Mammalian Fringe modification also alters ligand binding. Elongation beyond GlcNAc to the trisaccharide (Galbeta1-4GlcNAcbeta1-3-Fucosealpha1-O-Ser/Thr) is necessary to see a Fringe effect in a mammalian cell system Mus musculus