Fibroblast activation protein (FAP; FAP-α; seprase) is a type II 170 kDa post-proline cleaving atypical serine protease, closely related to the dipeptidyl peptidases (DPP) DPP-4, DPP-8, and DPP-9 in the prolyl oligopeptidase gene and enzyme family. FAP is conserved throughout chordate evolution, with homologs in human (hFAP), mouse (mFAP), and Xenopus laevis (89% and 50% protein sequence identity to hFAP, respectively). FAP expression correlates with tissue remodeling events (Hamson et al. 2014; Liu et al. 2015; Jiang et al. 2016). FAP is also phylogenetically linked to the prototype prolyl oligopeptidase and prolyl endopeptidase (PEP; PREP). FAP has both an endopeptidase activity that is similar to but distinct from that of PEP and a DPP activity that is similar to those of DPP4, DPP8, and DPP9 as well as the unrelated peptidase DPP7 (DPP-II).
FAP was originally discovered in...
MDG is supported by project grants 1105238 and 1113842 from the Australian National Health and Medical Research Council.