Encyclopedia of Cancer

Living Edition
| Editors: Manfred Schwab


  • Robert DayEmail author
  • Alex Y. Strongin
Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-27841-9_2283-3



Furin (EC is a highly specialized proteinase that cleaves the unique sequence motifs in a variety of proteins. Normally, following furin cleavage, the target protein is activated, and therefore, it can exhibit its biological activity. Because furin has been discovered first, currently, it is the most studied enzyme of the proprotein convertase (PC) family of serine proteinases. Seven distinct proprotein convertases of this family (furin, PC2, PC1/PC3, PC4, PACE4, PC5/PC6, and PC7) have been identified in humans, some of which have isoforms generated as the result of alternative splicing. Structurally and functionally, furin resembles its evolutionary precursor: the prohormone-processing enzyme, kexin (EC, which is encoded by the KEX2 gene of yeast Saccharomyces cerevisiae. The polypeptide sequence of the furin catalytic domain is...


Tumorigenic Phenotype Cleavage Site Sequence Multiple Basic Amino Acid Constitutive Secretory Pathway Endoproteolytic Processing 
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© Springer-Verlag Berlin Heidelberg 2015

Authors and Affiliations

  1. 1.Department of Surgery/Division of Urology, Institut de Pharmacologie, Faculté de Médecine et des sciences de la santéUniversité de SherbrookeSherbrookeCanada
  2. 2.Burnham Institute for Medical ResearchLa JollaUSA