H
IPR036943

Fibronectin type II domain superfamily

InterPro entry
Short nameFN_type2_sf
Overlapping entries
 
Kringle-like fold (IPR013806)

Description

Fibronectin is a multi-domain glycoprotein, found in a soluble form in plasma, and in an insoluble form in loose connective tissue and basement membranes, that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in a number of important functions e.g., wound healing; cell adhesion; blood coagulation; cell differentiation and migration; maintenance of the cellular cytoskeleton; and tumour metastasis
[9]
.

The major part of the sequence of fibronectin consists of the repetition of three types of domains, which are called type I, II, and III (also called FN1, FN2 and FN3 respectively)
[2]
. In fibronectin the type II domain is duplicated. Type II domain is approximately forty residues long, contains four conserved cysteines involved in disulphide bonds and is part of the collagen-binding region of fibronectin. Type II domains have also been found in a range of proteins including blood coagulation factor XII; bovine seminal plasma proteins PDC-109 (BSP-A1/A2) and BSP-A3
[3]
; cation-independent mannose-6-phosphate receptor
[6]
; mannose receptor of macrophages
[4]
; 180 Kd secretory phospholipase A2 receptor
[8]
. DEC-205 receptor
[7]
; 72 Kd and 92 Kd type IV collagenase (
3.4.24.24
)
[5]
; and hepatocyte growth factor activator
[1]
.

References

1.Molecular cloning and sequence analysis of the cDNA for a human serine protease reponsible for activation of hepatocyte growth factor. Structural similarity of the protease precursor to blood coagulation factor XII. Miyazawa K, Shimomura T, Kitamura A, Kondo J, Morimoto Y, Kitamura N. J. Biol. Chem. 268, 10024-8, (1993). View articlePMID: 7683665

2.Complete primary structure of bovine plasma fibronectin. Skorstengaard K, Jensen MS, Sahl P, Petersen TE, Magnusson S. Eur. J. Biochem. 161, 441-53, (1986). View articlePMID: 3780752

3.Complete amino acid sequence of BSP-A3 from bovine seminal plasma. Homology to PDC-109 and to the collagen-binding domain of fibronectin. Seidah NG, Manjunath P, Rochemont J, Sairam MR, Chretien M. Biochem. J. 243, 195-203, (1987). View articlePMID: 3606570

4.Primary structure of the mannose receptor contains multiple motifs resembling carbohydrate-recognition domains. Taylor ME, Conary JT, Lennartz MR, Stahl PD, Drickamer K. J. Biol. Chem. 265, 12156-62, (1990). View articlePMID: 2373685

5.H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen. Collier IE, Wilhelm SM, Eisen AZ, Marmer BL, Grant GA, Seltzer JL, Kronberger A, He CS, Bauer EA, Goldberg GI. J. Biol. Chem. 263, 6579-87, (1988). View articlePMID: 2834383

6.Structure and function of the mannose 6-phosphate/insulinlike growth factor II receptors. Kornfeld S. Annu. Rev. Biochem. 61, 307-30, (1992). View articlePMID: 1323236

7.The receptor DEC-205 expressed by dendritic cells and thymic epithelial cells is involved in antigen processing. Jiang W, Swiggard WJ, Heufler C, Peng M, Mirza A, Steinman RM, Nussenzweig MC. Nature 375, 151-5, (1995). View articlePMID: 7753172

8.Cloning and expression of a membrane receptor for secretory phospholipases A2. Lambeau G, Ancian P, Barhanin J, Lazdunski M. J. Biol. Chem. 269, 1575-8, (1994). View articlePMID: 8294398

9.Cloning and analysis of the promotor region of the human fibronectin gene. Dean DC, Bowlus CL, Bourgeois S. Proc. Natl. Acad. Sci. U.S.A. 84, 1876-80, (1987). View articlePMID: 3031656

Cross References

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