Fibrinogen, the precursor of fibrin, is the coagulable protein in the blood plasma of vertebrates. Following vascular injury, fibrinogen is cleaved by thrombin to form fibrin which is the most abundant component of blood clots. Fibrinogen consists as a dimer of 3 pairs of non-identical chains FGA, FGB, and FGG that are cross-linked by disulfide bonds in their N-terminal segments. The molecule has 2 terminal D domains and one central E domain, all three domains are separated when fibrinogen is degradated by plasmin. Mutations in this gene lead to several disorders, including dysfibrinogenemia, afibrinogenemia, and renal amyloidosis.
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Protein Aliases: epididymis secretory sperm binding protein Li 78p; fibg; Fibrinogen alpha chain; Fibrinogen beta chain; Fibrinogen gamma chain; fibrinogen, A alpha polypeptide; fibrinogen, alpha polypeptide; fibrinogen, B beta polypeptide; fibrinogen, beta polypeptide; fibrinogen, gamma polypeptide; Fibrinopeptide A; Fibrinopeptide B; Liver regeneration-related protein LRRG036/LRRG043/LRRG189; MGC119422; MGC119423; MGC119425; testicular tissue protein Li 70
Gene Aliases: Ab1-181; Ab1-216; Ac1-581; Ac1873; Fba5e; FGA; FGB; FGG; Fib2; HEL-S-78p; PRO2061
Molecular Function: intercellular signal molecule