FN1

Fibronectin is a major extracellular matrix (ECM) glycoprotein and one of the most important adhesion molecules in vertebrates. This large 2477 amino acid multidomain protein exists as a dimer and contains three types of repeating modules (FN-I, FN-II, and FN-III repeats) that create distinct binding sites for cells and other ECM components. The core functions of fibronectin center on organizing the ECM architecture and mediating cell-ECM interactions. Through its RGD motif in the FN-III10 domain, fibronectin directly binds integrin receptors (particularly alpha5beta1, alpha4beta1, alphaVbeta3) to mediate cell adhesion, migration, and signaling. Fibronectin serves as a key structural organizer by binding collagen types I-V and VII, assembling into fibrillar networks, and coordinating ECM assembly. It also binds fibrin through N-terminal and C-terminal sites, playing critical roles in provisional matrix formation during wound healing and hemostasis. Additional functions include binding heparin/heparan sulfate proteoglycans and serving as a ligand for various cell surface receptors. Fibronectin is essential for embryonic development, particularly in mesoderm formation, neural crest cell migration, heart development, and vascular morphogenesis. While the protein participates in numerous biological contexts including wound healing, angiogenesis, and platelet function, its fundamental role is as an ECM structural constituent and cell adhesion scaffold that integrates mechanical and biochemical signals at the cell-matrix interface.

Disorders

Relationship is the entry's genetic[].relationship_type. untyped means the entry has a genetic record for the gene but does not type it; its free-text association is shown instead.

An entry matches when ClinGen's MONDO disease is the entry's own disease term, a subtype term, or an exact-match mapping. An amber status marks an entry ClinGen supports the gene for (Definitive, Strong or Moderate) whose own record does not type it. A Limited, Disputed or Refuted tier on such an entry is not a gap.