Detail Information for IndEnz0002016214
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