Coagulation factor X (F10) is a vitamin K-dependent glycoprotein that participates in the middle phase of the blood coagulation cascade (PMID: 1931959; 1313796). It is synthesized as a single-chain precursor in the liver where it undergoes a number of covalent processing steps before secretion into the blood as a two-chain molecule linked by a disulfide bond (PMID: 1313796). The light chain contains 2 EGF-like domains, while the heavy chain contains the catalytic domain which is structurally homologous to those of the other hemostatic serine proteases. Factor X is activated into factor Xa, by both the extrinsic and intrinsic pathway. The activated factor then converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.