Entrez 5648 | Ensembl ENSG00000127241 | |
Aliases MASP1, 3MC1, CRARF, CRARF1, MAP1, MASP, MASP3, MAp44, PRSS5, RaRF, mannan binding lectin serine peptidase 1 External IDs OMIM: 600521 HomoloGene: 89143 GeneCards: MASP1 |
Mannan-binding lectin serine protease 1 also known as mannose-associated serine protease 1 (MASP-1) is an enzyme that in humans is encoded by the MASP1 gene.
MASP-1 is involved in the lectin pathway of the complement system and is responsible for cleaving C4 and C2 to form C4b2a, a C3-convertase.
Function
MASP-1 is a serine protease that functions as a component of the lectin pathway of complement activation. The complement pathway plays an essential role in the innate and adaptive immune response. MASP-1 is synthesized as a zymogen and is activated when it complexes with the pathogen recognition molecules of lectin pathway, the mannose-binding lectin and the ficolins. This protein is not directly involved in complement activation but may play a role as an amplifier of complement activation by cleaving complement C2 or by activating another complement serine protease, MASP-2. MASP-1 is also able to cleave fibrinogen and factor XIII and may be involved in coagulation. A splice variant of this gene which lacks the serine protease domain functions as an inhibitor of the complement pathway.