FURIN
Description
The FURIN (furin, paired basic amino acid cleaving enzyme) is a protein-coding gene located on chromosome 15.
Furin is a protease, a proteolytic enzyme activated by substrate presentation, encoded by the FURIN gene in humans and other animals. It activates proteins by cleaving inactive sections. Named after its location upstream of the FES oncogene, Furin is also known as PACE (Paired basic Amino acid Cleaving Enzyme). As a member of family S8, it's a subtilisin-like peptidase. Furin is a calcium-dependent serine endoprotease that efficiently cleaves precursor proteins at their paired basic amino acid processing sites. Its substrates include proparathyroid hormone, transforming growth factor beta 1 precursor, proalbumin, pro-beta-secretase, membrane type-1 matrix metalloproteinase, beta subunit of pro-nerve growth factor, and von Willebrand factor.
Furin is a ubiquitous endoprotease found within constitutive secretory pathways. It cleaves proteins at the RX(K/R)R consensus motif, playing a crucial role in the activation of various proteins, including TGF-beta-1, brain natriuretic factor (BNP), and the accessory subunit ATP6AP1/Ac45 of the V-ATPase, which regulates acidification of secretory granules.
FURIN is also known as FUR, PACE, PCSK3, SPC1.
