Fibronectin

Fibronectin is a high-molecular weight (~500-~600 kDa) glycoprotein of the extracellular matrix that binds to membrane-spanning receptor proteins called integrins. Fibronectin also binds to other extracellular matrix proteins such as collagen, fibrin, and heparan sulfate proteoglycans (e.g. syndecans).

FN1
Available structures
PDBOrtholog search: H0Y7Z1%20or%20B7ZLE5 PDBe H0Y7Z1,B7ZLE5 RCSB
Identifiers
AliasesFN1, CIG, ED-B, FINC, FN, FNZ, GFND, GFND2, LETS, MSF, fibronectin 1, SMDCF
External IDsOMIM: 135600 MGI: 95566 HomoloGene: 1533 GeneCards: FN1
Orthologs
SpeciesHumanMouse
Entrez

2335

14268

Ensembl

ENSG00000115414

ENSMUSG00000026193

UniProt

P02751

P11276

RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)Chr 2: 215.36 – 215.44 MbChr 1: 71.62 – 71.69 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

Fibronectin exists as a protein dimer, consisting of two nearly identical monomers linked by a pair of disulfide bonds. The fibronectin protein is produced from a single gene, but alternative splicing of its pre-mRNA leads to the creation of several isoforms.

Two types of fibronectin are present in vertebrates:

  • soluble plasma fibronectin (formerly called "cold-insoluble globulin", or CIg) is a major protein component of blood plasma (300 μg/ml) and is produced in the liver by hepatocytes.
  • insoluble cellular fibronectin is a major component of the extracellular matrix. It is secreted by various cells, primarily fibroblasts, as a soluble protein dimer and is then assembled into an insoluble matrix in a complex cell-mediated process.

Fibronectin plays a major role in cell adhesion, growth, migration, and differentiation, and it is important for processes such as wound healing and embryonic development. Altered fibronectin expression, degradation, and organization has been associated with a number of pathologies, including cancer, arthritis, and fibrosis.

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