HGNC Approved Gene Symbol:VTN
Cytogenetic location:17q11.2 Genomic coordinates(GRCh38) :17:28,367,284-28,370,307 (from NCBI)
Vitronectin, also called serum spreading factor or complement S-protein, is a 75-kD glycoprotein in plasma and tissue. It is a multifunctional protein that mediates cell-to-substrate adhesion, inhibits the cytolytic action of the terminal complement cascade in vitro, and binds to several serine protease inhibitors of the serpin family, e.g., antithrombin III (AT3;107300), plasminogen activator inhibitors I and II (PAI1,173360; PAI2,173390), heparin cofactor II (HCF2;142360), and protease nexin (PN1;177010) (summary byFink et al., 1992).
The primary structure of vitronectin has been deduced from the sequence of its cloned cDNA (Jenne and Stanley, 1985;Preissner et al., 1986). The deduced protein contains 459 amino acides preceded by a cleaved leader peptide of 19 residues.
By use of high resolution fluorescence in situ hybridization (FISH),Fink et al. (1992) mapped the VTN gene to chromosome 17q11. The localization was confirmed by cohybridization with a centromere-specific alphoid probe.
Polymorphism of vitronectin of plasma has been demonstrated (Conlan et al., 1988;Kubota et al., 1988).Sun and Mosher (1989) demonstrated that the frequencies are different in Caucasian and East Asian populations.
S-protein is not to be confused with protein S (176880).
Conlan, M. G., Tomasini, B. R., Schultz, R. L., Mosher, D. F.Plasma vitronectin polymorphism in normal subjects and patients with disseminated intravascular coagulation. Blood 72: 185-190, 1988. [PubMed:2455567,related citations]
Fink, T. M., Jenne, D. E., Lichter, P.The human vitronectin (complement S-protein) gene maps to the centromeric region of 17q. Hum. Genet. 88: 569-572, 1992. [PubMed:1372588,related citations] [Full Text]
Jenne, D., Stanley, K. K.Molecular cloning of S-protein, a link between complement, coagulation and cell-substrate adhesion. EMBO J. 4: 3153-3157, 1985. [PubMed:3004934,related citations] [Full Text]
Kubota, K., Katayama, S., Matsuda, M., Hayashi, M.Three types of vitronectin in human blood. Cell Struct. Funct. 13: 123-128, 1988. [PubMed:2454751,related citations] [Full Text]
Preissner, K. T., Heimburger, N., Anders, E., Muller-Berghaus, G.Physicochemical, immunological and functional comparison of human S-protein and vitronectin: evidence for the identity of both plasma proteins. Biochem. Biophys. Res. Commun. 134: 951-956, 1986. [PubMed:2418831,related citations] [Full Text]
Sun, W. H., Mosher, D. F.Polymorphism of vitronectin. (Letter) Blood 73: 353-354, 1989. [PubMed:2462942,related citations]
Alternative titles; symbols
HGNC Approved Gene Symbol: VTN
Cytogenetic location: 17q11.2 Genomic coordinates(GRCh38) : 17:28,367,284-28,370,307(from NCBI)
Vitronectin, also called serum spreading factor or complement S-protein, is a 75-kD glycoprotein in plasma and tissue. It is a multifunctional protein that mediates cell-to-substrate adhesion, inhibits the cytolytic action of the terminal complement cascade in vitro, and binds to several serine protease inhibitors of the serpin family, e.g., antithrombin III (AT3; 107300), plasminogen activator inhibitors I and II (PAI1, 173360; PAI2, 173390), heparin cofactor II (HCF2; 142360), and protease nexin (PN1; 177010) (summary by Fink et al., 1992).
The primary structure of vitronectin has been deduced from the sequence of its cloned cDNA (Jenne and Stanley, 1985; Preissner et al., 1986). The deduced protein contains 459 amino acides preceded by a cleaved leader peptide of 19 residues.
By use of high resolution fluorescence in situ hybridization (FISH), Fink et al. (1992) mapped the VTN gene to chromosome 17q11. The localization was confirmed by cohybridization with a centromere-specific alphoid probe.
Polymorphism of vitronectin of plasma has been demonstrated (Conlan et al., 1988; Kubota et al., 1988). Sun and Mosher (1989) demonstrated that the frequencies are different in Caucasian and East Asian populations.
S-protein is not to be confused with protein S (176880).
Conlan, M. G., Tomasini, B. R., Schultz, R. L., Mosher, D. F.Plasma vitronectin polymorphism in normal subjects and patients with disseminated intravascular coagulation. Blood 72: 185-190, 1988. [PubMed: 2455567]
Fink, T. M., Jenne, D. E., Lichter, P.The human vitronectin (complement S-protein) gene maps to the centromeric region of 17q. Hum. Genet. 88: 569-572, 1992. [PubMed: 1372588] [Full Text: https://doi.org/10.1007/BF00219346]
Jenne, D., Stanley, K. K.Molecular cloning of S-protein, a link between complement, coagulation and cell-substrate adhesion. EMBO J. 4: 3153-3157, 1985. [PubMed: 3004934] [Full Text: https://doi.org/10.1002/j.1460-2075.1985.tb04058.x]
Kubota, K., Katayama, S., Matsuda, M., Hayashi, M.Three types of vitronectin in human blood. Cell Struct. Funct. 13: 123-128, 1988. [PubMed: 2454751] [Full Text: https://doi.org/10.1247/csf.13.123]
Preissner, K. T., Heimburger, N., Anders, E., Muller-Berghaus, G.Physicochemical, immunological and functional comparison of human S-protein and vitronectin: evidence for the identity of both plasma proteins. Biochem. Biophys. Res. Commun. 134: 951-956, 1986. [PubMed: 2418831] [Full Text: https://doi.org/10.1016/s0006-291x(86)80512-5]
Sun, W. H., Mosher, D. F.Polymorphism of vitronectin. (Letter) Blood 73: 353-354, 1989. [PubMed: 2462942]
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