| 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. |
| Protein Name | Alpha-2-MacroglobulinAlpha-2-MC3 And Pzp-Like Alpha-2-Macroglobulin Domain-Containing Protein 5 |
| Database Links | Reactome: R-HSA-114608Reactome: R-HSA-140837Reactome: R-HSA-1474228Reactome: R-HSA-8963896 |
| Cellular Localisation | Secreted |
| Alternative Protein Names | Alpha-2-Macroglobulin proteinAlpha-2-M proteinC3 And Pzp-Like Alpha-2-Macroglobulin Domain-Containing Protein 5 proteinA2M proteinCPAMD5 proteinFWP007 protein |
Information sourced from Uniprot.org
