Furin is an endopeptidase localized to the Golgi membrane that cleaves many proteins on the carboxyterminal side of the sequence motif Arg-[any residue]-(Lys or Arg)-Arg (Jones et al. 1995; Leduc et al. 1992). In the case of gamma-carboxylated proteins, if this cleavage does not occur, the proteins are still secreted but do not function properly (Bristol et al. 1993; Lind et al. 1997). The aminoterminal fragments, "propeptides", generated in this reaction have no known function; the carboxylated, cleaved proteins are delivered to the cell membrane or secreted from the cell via pathways to be annotated in a future release of Reactome.
|BioModels Database||BIOMD0000000340, BIOMD0000000338, BIOMD0000000339|
|1629222||Activation of human furin precursor processing endoprotease occurs by an intramolecular autoproteolytic cleavage||J Biol Chem||1992|
|8846780||Intracellular trafficking of furin is modulated by the phosphorylation state of a casein kinase II site in its cytoplasmic tail||EMBO J||1995|
|9108399||Naturally occurring Arg(-1) to His mutation in human protein C leads to aberrant propeptide processing and secretion of dysfunctional protein C||Blood||1997|
|8463288||Propeptide processing during factor IX biosynthesis. Effect of point mutations adjacent to the propeptide cleavage site.||J Biol Chem||1993|