| Tissue Specificity | Expressed in the inner limiting membrane and around blood vessels in the retina (at protein level). Plasma FN (soluble dimeric form) is secreted by hepatocytes. Cellular FN (dimeric or cross-linked multimeric forms), made by fibroblasts, epithelial and other cell types, is deposited as fibrils in the extracellular matrix. |
| Post Translational Modifications | Sulfated. Forms covalent cross-links mediated by a transglutaminase, such as F13A or TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers (e.g. fibrinogen-fibronectin, collagen-fibronectin heteropolymers). Phosphorylated by FAM20C in the extracellular medium. Proteolytic processing produces the C-terminal NC1 peptide, anastellin. Some lysine residues are oxidized to allysine by LOXL3, promoting fibronectin activation and matrix formation. Serotonylated on Gln residues by TGM2 in response to hypoxia. |
| Function | Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts. Acts as a ligand for the Lilrb4a receptor, inhibiting Fcgr1/CD64-mediated monocyte activation. Secreted by contracting muscle, induces liver autophagy, a degradative pathway for nutrient mobilization and damage removal, and systemic insulin sensitization via hepatic ITGA5:ITGB1 integrin receptor signaling. Anastellin: Binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling. |
| Protein Name | FibronectinFn Cleaved Into - Anastellin |
| Database Links | Reactome: R-MMU-114608Reactome: -MMU-1474228Reactome: -MMU-1474244Reactome: -MMU-1566977Reactome: -MMU-202733Reactome: -MMU-2129379Reactome: -MMU-216083Reactome: -MMU-3000170Reactome: -MMU-3000178Reactome: -MMU-354192Reactome: -MMU-354194Reactome: -MMU-372708Reactome: -MMU-381426Reactome: -MMU-5674135Reactome: -MMU-8874081Reactome: -MMU-8957275Reactome: -MMU-9634597 |
| Cellular Localisation | SecretedExtracellular SpaceExtracellular Matrix |
| Alternative Antibody Names | Anti-Fibronectin antibodyAnti-Fn Cleaved Into - Anastellin antibodyAnti-Fn1 antibody |
Information sourced from Uniprot.org
