A2ML1 - Alpha-2-macroglobulin-like protein 1 - human protein (Function)
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A2ML1 »  Alpha-2-macroglobulin-like protein 1
Protein also known as:  C3 and PZP-like alpha-2-macroglobulin domain-containing protein 9.
Gene name:  A2ML1
Entry whose protein(s) existence is based on evidence at protein level
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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 (By similarity). 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.  
  • CuratedUniProtKB
GO molecular function 
Peptidase inhibitor activitydefinition[GO:0030414]  
  • IDAUniProtKB
Serine-type endopeptidase inhibitor activitydefinition[GO:0004867]  
  • IEAUniProtKB KW
GO biological process 
Negative regulation of endopeptidase activitydefinition[GO:0010951]  
  • IEAUniProtKB KW
  • IEAInterPro 2 GO
Regulation of endopeptidase activitydefinition[GO:0052548]  
  • IDAUniProtKB
Enzymatic activity 
More information is available from:


Molecular function 
Protease inhibitor  definition   [KW-0646]
Serine protease inhibitor  definition   [KW-0722]
Technical term 
Reference proteome  definition   [KW-1185]

Further external links