Serine endoprotease which cleaves substrates at the RX(K/R)R consensus motif. Release of mature proteins from their proproteins by cleavage of -Arg-Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors. Binds 3 calcium ions per subunit. Inhibited by the propeptide before the second cleavage. Inhibited by ethylenediaminetetraacetic acid (EDTA), ZnSO(4) and chloroketone DEC-RVKR-CMK. Optimum pH is 7.0. Active from pH 7.0 to 8.5. N-glycosylated. The inhibition peptide, which plays the role of an intramolecular chaperone, is probably autocatalytically removed in the endoplasmic reticulum (ER) and remains non-covalently bound as a potent autoinhibitor. Probably following transport to the trans Golgi, a second cleavage within the inhibition propeptide results in propeptide dissociation and bli activation. Belongs to the peptidase S8 family. Furin subfamily.