Protein O-fucosyltransferase 3 (POFUT3)

Protein O-fucosyltransferase 3 (POFUT3) is an enzyme localized predominantly to the endoplasmic reticulum, where it catalyzes the *O*-fucosylation of serine or threonine residues in the elastin microfibril interface (EMI) domains of target proteins, including Multimerin-1 (MMRN1), Multimerin-2 (MMRN2), and EMID1[1][5]. This modification requires the target protein to be properly folded and is important for protein quality control, folding, and secretion, particularly for EMI domain-containing proteins[1][3][5]. POFUT3 and the related POFUT4 are distinct from other fucosyltransferases because they transfer fucose directly to protein substrates rather than to glycan precursors[1][3]. The identification of POFUT3 expands the known spectrum of enzymes mediating protein *O*-fucosylation and highlights its specialized biological function, distinct from other fucosyltransferases involved in cell surface glycan synthesis or blood group antigen formation[1][3].

Other names

FUT10Fuc-TXFucT-XFucosyltransferase 10Fucosyltransferase XGalactoside 3-L-fucosyltransferase 10Alpha-(1,3)-fucosyltransferase 10FUCTXGDP-fucose protein O-fucosyltransferase 3