Mannose (or mannan)-binding lectin (MBL), also known as serum mannosebinding protein (MBP), initiates the lectin branch of the innate immune response by binding to the surface of potentially pathogenic microorganisms and initiating complement fixation through an N-terminal collagen-like domain. MBL is a key component in immune response in that it can directly trigger neutralization of invading microorganisms by an Ab-independent mechanism. Mutations of human MBL are associated with immunodeficiency resulting from a reduction in the ability of the mutant MBL to initiate complement fixation. In human, three types of MBL-associated serine proteases, MASP-1, MASP-2 and MASP-3, and a truncated form of MASP-2 (small MBL-associated protein; sMAP or MAp19) complex with MBL to activate the lectin pathway of the complement system. Activated MASPs subsequently cleave and activate downstream components of the complement pathway. MASP-3 is an alternatively spliced product from the MASP-1 gene and may function to inhibit MASP-2 by competing for MBL binding and inhibiting the activation of MBLassociated MASP-2.
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Protein Aliases: mannan-binding; mannan-binding lectin serine peptidase 1 pseudogene 1; mannan-binding lectin serine protease 1 pseudogene 1; Mannan-binding lectin serine protease 2; Mannan-binding lectin serine protease 2 A chain; Mannan-binding lectin serine protease 2 B chain; Mannose-binding protein-associated serine protease 2; MASP-2; MBL-associated plasma protein of 19 kD; MBL-associated serine protease 2; small MBL-associated protein
Gene Aliases: MAP19; MASP-2; MASP1P1; MASP2; sMAP
UniProt ID: (Human) O00187
Entrez Gene ID: (Human) 10747
Molecular Function: serine protease