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33  structures 414  species 3  interactions 2520  sequences 56  architectures

Family: Propep_M14 (PF02244)

Summary: Carboxypeptidase activation peptide

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Carboxypeptidase activation peptide Provide feedback

Carboxypeptidases are found in abundance in pancreatic secretions. The pro-segment moiety (activation peptide) accounts for up to a quarter of the total length of the peptidase, and is responsible for modulation of folding and activity of the pro-enzyme.

Literature references

  1. Aloy P, Catasus L, Villegas V, Reverter D, Vendrell J, Aviles FX; , Biol Chem 1998;379:149-155.: Comparative analysis of the sequences and three-dimensional models of human procarboxypeptidases A1, A2 and B. PUBMED:9524066 EPMC:9524066


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR003146

The peptidases are synthesised as inactive molecules, zymogens, with propeptides that must be removed by proteolytic cleavage to activate the enzyme. Structural studies of carboxypeptidases A and B reveal the propeptide to exist as a globular domain, followed by an extended alpha-helix; this shields the catalytic site, without specifically binding to it, while the substrate-binding site is blocked by making specific contacts [PUBMED:7674922, PUBMED:1548696].

This entry represents a propeptide associated with peptidases belonging to MEROPS peptidase family M14A. It is found in the carboxypeptidases A [PUBMED:9384570] and B [PUBMED:12162965].

Carboxypeptidases are found in abundance in pancreatic secretions. The pro-segment moiety (propeptide or activation peptide) accounts for up to a quarter of the total length of the peptidase.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

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Pfam Clan

This family is a member of clan PPP-I (CL0570), which has the following description:

This superfamily is characterised by families of short N-terminal domains such as the pancreatic carboxypeptidase activation domain, the subtilase pr