Tripeptidyl-peptidase II domain (IPR034051)

Short name: TPP_II_domain

Overlapping homologous superfamilies

Domain relationships


Tripeptidyl-peptidase II (MEROPS identifier S08.090) is a member of the peptidase S8 or subtilase family. Tripeptidyl-peptidase II removes tripeptides from the free N terminus of oligopeptides as well as having endoproteolytic activity. Some tripeptidyl-peptidases have been shown to cleave tripeptides and small peptides, e.g. angiotensin II and glucagon, while others are believed to be involved in MHC I processing [PMID: 16125107].

Peptidases S8 (or subtilases serine endo- and exo-peptidase clan) have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values [PMID: 1798697, PMID: 8420571, PMID: 8439290, PMID: 9070434].

GO terms

Biological Process

GO:0006508 proteolysis

Molecular Function

GO:0008240 tripeptidyl-peptidase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
  • cd04857 (Peptidases_S8_Tripeptidyl_Aminopeptidase_II)