Human, Mouse.

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This gene encodes a member of the glycosyltransferase O-Fuc family. This enzyme adds O-fucose through an O-glycosidic linkage to conserved serine or threonine residues in the epidermal growth factor-like repeats of a number of cell surface and secreted proteins. O-fucose glycans are involved in ligand-induced receptor signaling. Alternative splicing of this gene results in two transcript variants encoding different isoforms. [provided by RefSeq]

POFUT1, an endoplasmic reticulum-residing member of the glycosyltransferase O-Fuc family, adds O-fucose through an O-glycosidic linkage to conserved serine or threonines in epidermal growth factor-like repeats of several cell surface and secreted proteins. Unlike its homolog POFUT2, POFUT1 can also catalyze the transfer of fucose to thrombospondin type 1 repeats. Many of the substrates of POFUT1 are involved in ligand-induced receptor signaling. One such protein is Notch; mouse ES cells lacking POFUT have normal levels of Notch receptors at the cell surface, but these receptors do not bind Notch ligands or exhibit Notch signaling. At least two isoforms of POFUT1 are known to exist. This antibody is predicted to not cross-react with POFUT2.