IED ID | IndEnz0002016214 |
Enzyme Type ID | protease016214 |
Protein Name |
Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe EC 2.4.1.222 O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase |
Gene Name | Lfng |
Organism | Rattus norvegicus (Rat) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
Enzyme Sequence | MLQRCGRRLLLALVGALLACLLVLTADPPPTPVPAERGRRALRSLAGSSGAAPGPGSRAAVDPGVLVREVHSLSEYFSLLTRARRDADPPPGVASRQGDGHPRPPAEVLSPRDVFIAVKTTRKFHRARLDLLFETWISRHKEMTFIFTDGEDEALAKHTGNVVLTNCSAAHSRQALSCKMAVEYDRFIESGKKWFCHVDDDNYVNLRALLRLLASYPHTQDVYIGKPSLDRPIQATERISEHRVRPVHFWFATGGAGFCISRGLALKMGPWASGGHFMSTAERIRLPDDCTIGYIVEALLGVPLIRSGLFHSHLENLQQVPTTELHEQVTLSYGMFENKRNAVHIKGPFSVEADPSRFRSIHCHLYPDTPWCPRTAIL |
Enzyme Length | 378 |
Uniprot Accession Number | Q924T4 |
Absorption | |
Active Site | ACT_SITE 289; /evidence=ECO:0000250 |
Activity Regulation | |
Binding Site | BINDING 128; /note=Substrate; /evidence=ECO:0000250; BINDING 200; /note=Substrate; /evidence=ECO:0000250 |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor.; EC=2.4.1.222; |
DNA Binding | |
EC Number | 2.4.1.222 |
Enzyme Function | FUNCTION: 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. Decreases the binding of JAG1 to NOTCH2 but not that of DLL1. Essential mediator of somite segmentation and patterning. {ECO:0000250|UniProtKB:O09010, ECO:0000250|UniProtKB:Q8NES3}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Binding site (2); Chain (1); Disulfide bond (3); Glycosylation (1); Metal binding (2); Region (1); Site (1); Topological domain (2); Transmembrane (1) |
Keywords | Developmental protein;Disulfide bond;Glycoprotein;Glycosyltransferase;Golgi apparatus;Manganese;Membrane;Metal-binding;Reference proteome;Signal-anchor;Transferase;Transmembrane;Transmembrane helix |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | PTM: A soluble form may be derived from the membrane form by proteolytic processing. {ECO:0000305}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 41,958 |
Kinetics | |
Metal Binding | METAL 201; /note=Manganese; /evidence=ECO:0000250; METAL 313; /note=Manganese; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |