| Function | Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase. Displays inhibitory activity against chymotrypsin, papain, thermolysin, subtilisin A and, to a lesser extent, elastase but not trypsin. May play an important role during desquamation by inhibiting extracellular proteases. |
| Protein Name | Alpha-2-Macroglobulin-Like Protein 1C3 And Pzp-Like Alpha-2-Macroglobulin Domain-Containing Protein 9 |
| Cellular Localisation | Secreted |
| Alternative Protein Names | Alpha-2-Macroglobulin-Like Protein 1 proteinC3 And Pzp-Like Alpha-2-Macroglobulin Domain-Containing Protein 9 proteinA2ML1 proteinCPAMD9 protein |
Information sourced from Uniprot.org
