FURIN Human Recombinant Protein

The protein encoded by this gene belongs to the subtilisin-like proprotein convertase family. The members of this family are proprotein convertases that process latent precursor proteins into their biologically active products. This encoded protein is a calcium-dependent serine endoprotease that can efficiently cleave precursor proteins at their paired basic amino acid processing sites. Some of its substrates are: 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. It is also thought to be one of the proteases responsible for the activation of HIV envelope glycoproteins gp160 and gp140. This gene is thought to play a role in tumor progression. The use of alternate polyadenylation sites has been found for this gene. [provided by RefSeq, Jul 2008]

FURIN: Furin is likely to represent the ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RX(K/R)R consensus motif. Belongs to the peptidase S8 family. Furin subfamily.

Protein type: Protease; Vesicle; EC 3.4.21.75; Cell surface; Membrane protein, integral

Chromosomal Location of Human Ortholog: 15q26.1

Cellular Component: Golgi membrane; extracellular space; trans-Golgi network transport vesicle; cell surface; membrane; Golgi lumen; plasma membrane; integral to membrane; trans-Golgi network; lipid raft

Molecular Function: peptidase activity; serine-type endopeptidase inhibitor activity; protease binding; metal ion binding; serine-type endopeptidase activity; endopeptidase activity; nerve growth factor binding; peptide binding

Biological Process: extracellular matrix organization and biogenesis; nerve growth factor receptor signaling pathway; viral reproduction; peptide hormone processing; regulation of signal transduction; pathogenesis; viral infectious cycle; proteolysis; positive regulation of membrane protein ectodomain proteolysis; peptide biosynthetic process; nerve growth factor processing; extracellular matrix disassembly; transforming growth factor beta receptor signaling pathway; regulation of endopeptidase activity; negative regulation of nerve growth factor production; secretion by cell; Notch signaling pathway; signal peptide processing; virus assembly; post-translational protein modification; peptidyl-glutamic acid carboxylation; nerve growth factor production; negative regulation of transforming growth factor-beta1 production; collagen catabolic process; cell proliferation; cellular protein metabolic process; viral protein processing; protein processing; regulation of protein catabolic process; negative regulation of low-density lipoprotein receptor catabolic process