Dipeptidyl peptidase 8 is member of the peptidase S9B family, a small family of dipeptidyl peptidases that are able to cleave peptide substrates at a prolyl bond.
The encoded protein shares similarity with dipeptidyl peptidase IV in that it is ubiquitously expressed, and hydrolyzes the same substrates. These similarities suggest that, like dipeptidyl peptidase IV, this protein may play a role in T-cell activation and immune function. Alternatively spliced transcript variants encoding different isoforms have been described.The deduced 882-amino acid DPP8 protein shares about 27% sequence identity with DPP4 and FAP; unlike these proteins, however, DPP8 has no transmembrane domain and no N- or O-linked glycosylation sites.