FGB (P02675) - Overview - Molecular Target Synopsis
FGB, Fibrinogen beta chain
Also Known as FIBB_HUMAN, FGB
Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways. Heterohexamer; disulfide linked. Contains 2 sets of 3 non-identical chains (alpha, beta and gamma). The 2 heterotrimers are in head to head conformation with the N-termini in a small central domain.
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UniProt: FGB is active in the following subcellular-locations: secreted.
GO terms: FGB is active in the following subcellular-locations: blood microparticle, cell cortex, cell surface, collagen-containing extracellular matrix, endoplasmic reticulum, external side of plasma membrane, extracellular exosome, extracellular region, extracellular space, extracellular vesicle, fibrinogen complex, plasma membrane, platelet alpha granule, platelet alpha granule lumen, synapse.