Cloned (Comment) | Organism |
---|---|
coexpression of Flag-tagged DLL3 and HA-tagged LFNG in CHO cells, the two proteins coprecipitate | Mus musculus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
Golgi apparatus | - |
Mus musculus | 5794 | - |
trans-Golgi network | - |
Mus musculus | 5802 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Mus musculus | the enzyme interacts with Delta-like 3 (DLL3), a member of the DSL family of Notch ligands, epidermal growth factor like repeats 2 and 5 of DLL3 are O-fucosylated at consensus sites for peptide-O-fucosyltransferase POFUT1, EC 2.4.1.221 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | O09010 | gene lfng | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme interacts with Delta-like 3 (DLL3), a member of the DSL family of Notch ligands, epidermal growth factor like repeats 2 and 5 of DLL3 are O-fucosylated at consensus sites for peptide-O-fucosyltransferase POFUT1, EC 2.4.1.221 | Mus musculus | ? | - |
? | |
additional information | Delta-like 3 is O-fucosylated at epidermal growth factor repeats two and five, and the fucosylated protein is a substrate for FNG proteins in cultured cells, the O-fucose-linked residues in EGF 2 and/or 5 are elongated by fringe protein, enzyme LFNG. Recognition of DLL3 by LFNG also does not depend on the presence of O-linked fucose | Mus musculus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
LFNG | - |
Mus musculus |
Lunatic Fringe | - |
Mus musculus |
General Information | Comment | Organism |
---|---|---|
malfunction | loss of the DSL protein DLL3 in the mouse results in severe somite patterning defects, which are virtually indistinguishable from the defects in mice that lack the enzyme lunatic fringe. Embryos double homozygous for null mutations in Dll3 and Lfng are phenotypically indistinguishable from the single mutants supporting a potential common function. Mutation of the O-fucosylation sites in DLL3 does not disrupt the interaction of DLL3 with LFNG or full length Notch1or DLL1, and O-fucosylation-deficient DLL3 can still inhibit Notch in cis in vitro. In contrast to wild type DLL3, O-fucosylation-deficient DLL3 cannot compensate for the loss of endogenous DLL3 during somitogenesis in the embryo | Mus musculus |
physiological function | enzyme lunatic fringe is a glycosyltransferase involved in modifying Notch signaling. modification of DLL3 by O-linked fucose via the action of enzyme lunatic fringe is essential for its function during somitogenesis | Mus musculus |