C1r, C1s, MBL-associated serine protease (MASP)-1, MASP-2 and MASP-3 are mosaic serine proteases of the classical and lectin pathways of complement. They form a family of enzymes with identical domain organization and similar overall structure, but with different enzymatic properties. MASP-2 of the lectin pathway can autoactivate and cleave C4 and C2 components. In the classical pathway two enzymes mediate these functions: C1r autoactivates and activates C1s, while C1s cleaves C4 and C2. The substrate specificity and the biological function of MASP-1 and MASP-3 have not yet been completely resolved. MASP-1 can autoactivate and the activated MASP-1 has more relaxed substrate specificity than the other members of the family. It was demonstrated that MASP-1 can specifically cleave C2, C3 and fibrinogen, but the physiological relevance of these findings has to be proved. We do not know how MASP-3 becomes activated and its biological function is also not clear. In this review, we will summarize current knowledge about the structure and function of these proteases. Special emphasis will be laid on the specificity, autoactivation and evolution of these enzymes.