Aliases for LFNG Gene
External Ids for LFNG Gene
Previous GeneCards Identifiers for LFNG Gene
This gene is a member of the fringe gene family which also includes radical and manic fringe genes. They all encode evolutionarily conserved glycosyltransferases that act in the Notch signaling pathway to define boundaries during embryonic development. While their genomic structure is distinct from other glycosyltransferases, fringe proteins have a fucose-specific beta-1,3-N-acetylglucosaminyltransferase activity that leads to elongation of O-linked fucose residues on Notch, which alters Notch signaling. This gene product is predicted to be a single-pass type II Golgi membrane protein but it may also be secreted and proteolytically processed like the related proteins in mouse and Drosophila (PMID: 9187150). Mutations in this gene have been associated with autosomal recessive spondylocostal dysostosis 3. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2009]
GeneCards Summary for LFNG Gene
LFNG (LFNG O-Fucosylpeptide 3-Beta-N-Acetylglucosaminyltransferase) is a Protein Coding gene. Diseases associated with LFNG include Spondylocostal Dysostosis 3, Autosomal Recessive and Spondylocostal Dysostosis 3. Among its related pathways are Development NOTCH1-mediated pathway for NF-KB activity modulation and PI3K-Akt signaling pathway. Gene Ontology (GO) annotations related to this gene include transferase activity, transferring glycosyl groups and O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase activity. An important paralog of this gene is RFNG.
UniProtKB/Swiss-Prot for LFNG Gene
Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1 via an increase in its binding to DLL1 (By similarity). Decreases the binding of JAG1 to NOTCH2 but not that of DLL1 (PubMed:11346656). Essential mediator of somite segmentation and patterning (By similarity).