CAC86915.1
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UniProt Primary Accession #
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UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
262,625 Da
NCBI Official Full Name
fibronectin
NCBI Official Synonym Full Names
fibronectin 1
NCBI Official Synonym Symbols
FN; CIG; FNZ; MSF; ED-B; FINC; GFND; LETS; GFND2 [Similar Products]
NCBI Protein Information
fibronectin; cold-insoluble globulin; migration-stimulating factor
UniProt Protein Name
Fibronectin
UniProt Synonym Protein Names
Cold-insoluble globulin
UniProt Synonym Gene Names
UniProt Entry Name
FINC_HUMAN
NCBI Summary for FN
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. 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. However, the full-length nature of some variants has not been determined. [provided by RefSeq, Jul 2008]
UniProt Comments for FN
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. 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. Ref.38 Ref.40 Ref.44 Ref.50Anastellin 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. Ref.38 Ref.40 Ref.44 Ref.50
Subunit structure: Mostly heterodimers or multimers of alternatively spliced variants, connected by 2 disulfide bonds near the carboxyl ends; to a lesser extent homodimers. Interacts with FBLN1, AMBP, TNR, LGALS3BP and COL13A1. Interacts with FBLN7
By similarity. Interacts with COMP. Interacts with S.aureus fnbA. Interacts with TNR; the interaction inhibits cell adhesion and neurite outgrowth
By similarity. Interacts with FST3. Ref.36 Ref.38 Ref.39 Ref.41 Ref.42 Ref.47
Subcellular location: Secreted › extracellular space › extracellular matrix.
Tissue specificity: 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. Ugl-Y1, Ugl-Y2 and Ugl-Y3 are found in urine. Ref.16 Ref.35
Developmental stage: Ugl-Y1, Ugl-Y2 and Ugl-Y3 are present in the urine from 0 to 17 years of age. Ref.16 Ref.35
Post-translational modification: Sulfated.It is not known whether both or only one of Thr-2064 and Thr-2065 are/is glycosylated. Ref.16 Ref.26 Ref.35 Ref.58Forms 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).Phosphorylation sites are present in the extracellular medium.Proteolytic processing produces the C-terminal NC1 peptide, anastellin.
Involvement in disease: Glomerulopathy with fibronectin deposits 2 (GFND2) [MIM:601894]: 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.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.72
Sequence similarities: Contains 12 fibronectin type-I domains.Contains 2 fibronectin type-II domains.Contains 16 fibronectin type-III domains.
Sequence caution: The sequence AAX76513.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAD93077.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.The sequence CAD91166.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.The sequence CAD97964.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.The sequence CAD97965.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.The sequence CAH18136.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
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Pathways associated with FN elisa kit
Diseases associated with FN elisa kit
Organs/Tissues associated with FN elisa kit
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