F7

F7 Full Name

coagulation factor VII (serum prothrombin conversion accelerator)

F7 Introduction

Coagulation Factor VII (Factor VII, FVII) is a crucial vitamin K-dependent serine protease within the blood coagulation system, encoded by the F7 gene. The structure of the F7 gene is relatively compact, spanning approximately 12 to 14 kilobase pairs (kb), and consists of nine exons (1a, 1b, 2, 3, 4, 5, 6, 7, 8) and eight introns. The protein precursor synthesized from the F7 gene undergoes a series of post-translational modifications, ultimately forming the mature FVII protein composed of 406 amino acids. Its protein structure is highly modular, featuring several well-defined functional domains: an N-terminal γ-carboxyglutamic acid (Gla) domain essential for calcium ion and phospholipid membrane binding, followed by two epidermal growth factor-like (EGF-like) domains (EGF-1 and EGF-2), and finally a C-terminal serine protease catalytic domain. During activation, the protein is cleaved at specific sites to form activated coagulation factor VII (FVIIa), consisting of a light chain (containing the Gla and two EGF domains) and a heavy chain (containing the catalytic domain), linked by a disulfide bond.

The core physiological function of FVII is to initiate the extrinsic coagulation cascade. In normal circulation, FVII exists in its zymogen (inactive) form. When vascular injury exposes tissue factor (TF)—expressed by subendothelial cells—to blood, FVII rapidly binds to TF, forming the FVII-TF complex. This binding not only localizes FVII to the site of injury but also greatly enhances its activation efficiency by trace amounts of thrombin or other proteases into FVIIa. The resulting FVIIa-TF complex possesses potent proteolytic activity; it efficiently activates coagulation Factor X (FX) and Factor IX (FIX), thereby triggering the downstream coagulation cascade. This ultimately leads to the conversion of fibrinogen to fibrin, forming a stable blood clot that seals the wound and prevents blood loss.

Figure 1. AT reacts with FVIIa only if FVIIa is bound to functionally active TF, thereby forming a FVIIa–AT complex. (Source: Moruzzi S, et al. 2024)

Functional defects or abnormalities in the F7 gene are directly linked to an autosomal recessive bleeding disorder known as Hereditary Factor VII Deficiency. This condition results from mutations in the F7 gene that lead to reduced synthesis, structural abnormalities, or functional loss of the FVII protein. Numerous mutation types have been identified to date, including missense, nonsense, splice-site mutations, and gene deletions, which are distributed across various functional regions of the gene.

Alternate Names for F7

F7; coagulation factor VII (serum prothrombin conversion accelerator); SPCA; coagulation factor VII; eptacog alfa; proconvertin; FVII coagulation protein;

• 1. Sevenet PO, et al. Factor VII Deficiency: From Basics to Clinical Laboratory Diagnosis and Patient Management. Clin Appl Thromb Hemost. 2017 Oct;23(7):703-710.
  2. Moruzzi S, et al. Activated Factor VII-Antithrombin Complex, a Biomarker of Tissue Factor-Related Pathways in Different Clinical Settings: A Narrative Review from Cardiovascular Diseases to Cancer. Diagnostics (Basel). 2024 Aug 6;14(16):1711.