FN1

This gene encodes fibronectin, a glycoprotein present in a soluble dimeric form in plasma, and in a dimeric or multimeric form at the cell surface and in extracellular matrix. The encoded preproprotein is proteolytically processed to generate the mature protein. Fibronectin is involved in cell adhesion and migration processes including embryogenesis, wound healing, blood coagulation, host defense, and metastasis. The gene has three regions subject to alternative splicing, with the potential to produce 20 different transcript variants, at least one of which encodes an isoform that undergoes proteolytic processing. The full-length nature of some variants has not been determined.

Full Name

Fibronectin 1

Alternative Names

FN; CIG; FNZ; MSF; ED-B; FINC; GFND; LETS; GFND2; SMDCF

Function

Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin (PubMed:3024962, PubMed:3900070, PubMed:3593230, PubMed:7989369).

Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape (PubMed:3024962, PubMed:3900070, PubMed:3593230, PubMed:7989369).

Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (By similarity).

Participates in the regulation of type I collagen deposition by osteoblasts (By similarity).

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.

Biological Process

Acute-phase response Source: UniProtKB-KW
Angiogenesis Source: UniProtKB-KW
Biological process involved in interaction with symbiont Source: CAFA
Blood coagulation, fibrin clot formation Source: GO_Central
Calcium-independent cell-matrix adhesion Source: Ensembl
Cell adhesion Source: UniProtKB
Cell-matrix adhesion Source: GO_Central
Cell-substrate junction assembly Source: GO_Central
Endodermal cell differentiation Source: UniProtKB
Heart development Source: GO_Central
Integrin activation Source: UniProtKB
Integrin-mediated signaling pathway Source: BHF-UCL
Negative regulation of transforming growth factor beta production Source: UniProtKB
Nervous system development Source: GO_Central
Neural crest cell migration involved in autonomic nervous system development Source: MGI
Peptide cross-linking Source: BHF-UCL
Platelet aggregation Source: GO_Central
Positive regulation of axon extension Source: Ensembl
Positive regulation of cell population proliferation Source: UniProtKB
Positive regulation of fibroblast proliferation Source: UniProtKB
Positive regulation of gene expression Source: UniProtKB
Positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
Positive regulation of substrate-dependent cell migration, cell attachment to substrate Source: UniProtKB
Regulation of cell shape Source: UniProtKB-KW
Regulation of ERK1 and ERK2 cascade Source: UniProtKB
Regulation of protein phosphorylation Source: UniProtKB
Response to wounding Source: UniProtKB
Substrate adhesion-dependent cell spreading Source: BHF-UCL

Cellular Location

Extracellular matrix

Involvement in disease

Glomerulopathy with fibronectin deposits 2 (GFND2):
Genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life.
Spondylometaphyseal dysplasia, corner fracture type (SMDCF):
An autosomal dominant form of spondylometaphyseal dysplasia, a group of short stature disorders distinguished by abnormalities in the vertebrae and the metaphyses of the tubular bones. SMDCF is characterized by flake-like, triangular, or curvilinear ossification centers at the edges of irregular metaphyses that simulate fractures. These corner fractures involve the distal tibia, the ulnar aspect of the distal radius, the proximal humerus, and the proximal femur. They represent irregular ossification at the growth plates and secondary ossification centers.

PTM

Sulfated.
It is not known whether both or only one of Thr-2155 and Thr-2156 are/is glycosylated.
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.

Anti-FN1 antibodies

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Mouse Anti-FN1 Monoclonal Antibody (71) (CBMAB-1241CQ)

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Target: FN1

Host: Mouse

Antibody Isotype: IgG1

Specificity: Human

Clone: 71

Application*: E, B, IF, WB

Functional Assay

FN1

Anti-FN1 antibodies

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