A2M 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. Belongs to the protease inhibitor I39 (alpha-2-macroglobulin) family. Secreted in plasma. Note: This description may include information from UniProtKB.
Protein type: Inhibitor; Secreted; Secreted, signal peptide
Chromosomal Location of Human Ortholog: 6 F1|6 57.49 cM
Cellular Component:  extracellular region; extracellular space
Molecular Function:  brain-derived neurotrophic factor binding; calcium-dependent protein binding; endopeptidase inhibitor activity; enzyme binding; growth factor binding; interleukin-1 binding; interleukin-8 binding; nerve growth factor binding; peptidase inhibitor activity; protease binding; protein binding; protein homodimerization activity; serine-type endopeptidase inhibitor activity; signaling receptor binding; tumor necrosis factor binding
Biological Process:  female pregnancy; negative regulation of complement activation, lectin pathway; negative regulation of peptidase activity; stem cell differentiation
Reference #:  Q6GQT1 (UniProtKB)
Alt. Names/Synonyms: A2m; A2mp; Alpha-2-macroglobulin; Alpha-2-macroglobulin-P
Gene Symbols: A2mp
Molecular weight: 164,353 Da
Basal Isoelectric point: 6.18  Predict pI for various phosphorylation states
Select Structure to View Below


Protein Structure Not Found.

Cross-references to other databases:  STRING  |  Reactome  |  BioGPS  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene