Domain

Proteinase inhibitor, carboxypeptidase propeptide (IPR003146)

Short name: Prot_inh_M14A

Domain relationships

Description

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 [PMID: 7674922, PMID: 1548696].

Members of this propeptide family are found in the metallocarboxypeptidases: A1, A2 [PMID: 9384570], A3, A4, A5, A6, U, insect gut carboxypeptidase and B [PMID: 12162965], and and are associated with peptidases belonging to MEROPS peptidase family M14A.

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.

GO terms

Biological Process

GO:0006508 proteolysis

Molecular Function

GO:0004180 carboxypeptidase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
GENE3D
Pfam