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Description

Furin (UniProt: P09958, also known as EC: 3.4.2.75, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme, PACE) is encoded by the FURIN (also known as FUR, PACE, PCSK3) gene (Gene ID: 5045) in human. Furin is an ubiquitously expressed enzyme with endoprotease activity within constitutive secretory pathways and is capable of cleavage at the RX(K/R)R consensus motif. It is single-pass type I membrane protein that shuttles between the trans-Golgi network and the cell surface. It is synthesized with a signal peptide of 26 amino acids and a propeptide region (aa 27-107) that inhibits its activity. The inhibition peptide plays the role of an intramolecular chaperone. It is autocatalytically removed in the endoplasmic reticulum (ER) and remains non-covalently bound to furin as a potent autoinhibitor. Propeptide cleavage is a prerequisite for exit of Furin molecules out of the endoplasmic reticulum. A second cleavage within the propeptide region occurs in the trans-Golgi network, followed by the release of the propeptide and the activation of Furin. Mature Furin has a luminal region (aa 108-705), a helical domain (aa 716-738), and a cytoplasmic region (aa 739-794). The cytoplasmic domain responsible for its trans-Golgi network localization and recycling from the cell surface.