Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which is an essential interface for biological recognition processes. Fucosyltransferases catalyze the covalent association of fucose to different positional linkages in sugar acceptor molecules. POFUT1 (protein O-fucosyltransferase 1), also known as FUT12, O-FUT or O-FucT-1, is a 388 amino acid protein that localizes to the endoplasmic reticulum and belongs to the fucosyltransferase subfamily of glycosyltransferases. Highly expressed in pancreas, kidney, lung, heart, brain, liver, placenta and skeletal muscle, POFUT1 uses manganese to catalyze the attachment (specifically the O-glycosidic linkage) of fucose to a conserved serine or threonine residue on a protein acceptor. Via its cataytic activity, POFUT1 plays an important role in Notch signaling, as Notch ligands can serve as POFUT1 substrates. Two isoforms of POFUT1 exist due to alternative splicing events.
Function:
Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in EGF domains. Plays a crucial role in Notch signaling.
Subcellular Location:
Endoplasmic reticulum.
Tissue Specificity:
Highly expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.
Post-translational modifications:
N-glycosylated.
Similarity:
Belongs to the glycosyltransferase 68 family.
SWISS:
Q9H488
Gene ID:
23509
Database links:
Entrez Gene: 23509 Human
Entrez Gene: 140484 Mouse
Entrez Gene: 311551 Rat
Omim: 607491 Human
SwissProt: Q9H488 Human
SwissProt: Q91ZW2 Mouse
SwissProt: Q6EV70 Rat
Unigene: 47489 Human
Unigene: 293761 Mouse
Unigene: 214685 Rat
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