Dipeptidyl peptidase (DPP) 9 is a member of the DPP4 (DPP-IV) family, which are all members of clan SC of serine proteases, family S9, subfamily S9B. S9B proteases have a unique ability to remove Xaa-Pro dipeptides from the N-terminus of substrates. Fibroblast activation protein (FAP) and DPP8 are the other S9B peptidases.
DPP9 has been localized to human chromosome 19p13.3 (Olsen and Wagtmann 2002). The human DPP9 gene spans 48.6 kb and comprises 22 exons that are 53 bp to 1431 bp in length (Ajami et al. 2004). A predominant DPP9 mRNA transcript of 4.4 kb (AY374518; encoding 863 amino acids, the short form) is ubiquitous, with the highest levels in liver, heart, and skeletal muscle (Olsen and Wagtmann 2002; Ajami et al. 2004). A less abundant 5 kb transcript (AF542510; encoding 971 amino acids) that is abundant in skeletal muscle contains a second ATG translation start site...
MDG is supported by grants 1105238 and 1113842 from the Australian National Health and Medical Research Council.
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