| Primary Identifier | IPR033190 | Type | Family |
| Short Name | F7 |
| description | Factor VII (F7) initiates the extrinsic pathway of blood coagulation. It contains an N-terminal Gla domain followed by two epidermal growth factor-like domains (EGF1 and EGF2) and a C-terminal trypsin-like serine protease domain. It can be transformed into active forms (FVIIa) by proteolytic cleavage of the activation peptide located in the connecting region between the EGF2 and the protease domain; this results in the formation of a two-chain FVIIa molecule and a heavy chain held together by a single disulfide bond []. Its first EGF domain (EGF1) binds a calcium ion at its N terminus [].At an injury site, initiation of coagulation begins by exposure of blood to tissue factor (TF) in the extravascular space and formation of the Ca2+-dependent complex between TF and plasma FVIIa. The Ca2+/FVIIa/TF complex formed on the cell surfaces then activates both FX and FIX leading to thrombin generation and fibrin formation []. Mutations in the F7 gene cause Factor VII deficiency (FA7D), the most frequent among rare congenital bleeding disorders []. |
