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Protein O-fucosyltransferase 4 (POFUT4) is an enzyme located in the endoplasmic reticulum that catalyzes the addition of fucose to serine or threonine residues within EMI (elastin microfibril interface) domains of target proteins including MMRN1, MMRN2, and EMID1 through an O-glycosidic linkage[1][5]. This O-fucosylation process is essential for proper folding and secretion of EMI domain-containing proteins and participates in a non-canonical quality control pathway in the endoplasmic reticulum[1][5]. POFUT4 was previously annotated as alpha-(1,3)-fucosyltransferase 11 (FUT11), but recent research clarified its role as a novel protein O-fucosyltransferase[1]. Aberrant function or expression of POFUT4 has been implicated in diseases such as stomach cancer, where it may serve as a biomarker[5]. Experimental evidence for its role in drug interaction, mechanisms of action, or specific safety concerns is presently lacking.
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