Protein O-fucosyltransferase 2 (POFUT2)

Protein O-fucosyltransferase 2 (POFUT2) is an endoplasmic reticulum-localized enzyme in the glycosyltransferase family that catalyzes the addition of O-linked fucose to specific serine or threonine residues within thrombospondin type 1 repeats (TSRs) of more than 40 human proteins[1][2][3]. POFUT2 is highly selective for properly folded TSR domains, relying on recognition of a distinct three-dimensional fold rather than sequence motifs[1][2]. This modification is critical for proper folding, function, and quality control of TSR-containing proteins in the secretory pathway, making POFUT2 essential for the stability and trafficking of these substrates[3][4]. In pathogens like Plasmodium falciparum, loss of POFUT2 disrupts trafficking and function of key surface proteins, impairing infectiousness[4]. While not currently a direct therapeutic target, impairment of its enzymatic activity could affect processes involving TSR-containing proteins.

Other names

GDP-fucose protein O-fucosyltransferase 2C21orf80FUT13KIAA0958O-FucT-2Peptide-O-fucosyltransferase 2peptide-O-fucosyltransferase

Not applicable (no known drugs targeting POFUT2)