Primary Information |
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| BoMiProt ID | Bomi10462 |
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| Protein Name | Vascular endothelial growth factor B/VEGF-related factor |
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| Organism | Bos taurus |
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| Uniprot ID | Q9XS49 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_776912.1 |
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| Aminoacid Length | 207 |
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| Molecular Weight | 21655 |
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| FASTA Sequence |
Download |
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| Gene Name | VEGFB/VRF |
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| Gene ID | 282121 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | is expressed abundantly in cardiac and skeletal muscle .It acts as a growth factor for endothelial cells. |
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| Biochemical Properties | VEGF-B167 binds heparin and neuropilin-1 whereas the binding to neuropilin-1 of VEGF-B186 is regulated by proteolysis.VEGF are highly basic and bind to cellular or pericellular heparan sulfate proteoglycans, whereas the shorter isoforms are soluble in the extracellular fluid. |
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| Significance in milk | Involvement in immunosuppression and hypoxia stress and heat stress. |
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| PTMs | Disulphide bond, Glycosylation |
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| Significance of PTMs | VEGF-B186 is O-glycosylated presumably in its unique COOH-terminal domain.The addition of O-linked glycans may serve to compensate for the hydrophobic character of the VEGF-B186 COOH terminus and make the secreted protein more soluble in aqueous media. |
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| Linking IDs | Bomi10462 |
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| Bibliography | 1.Olofsson B, Pajusola K, von Euler G, Chilov D, Alitalo K, Eriksson U. Genomic organization of the mouse and human genes for vascular endothelial growth factor B (VEGF-B) and characterization of a second splice isoform. J Biol Chem. 1996 Aug 9;271(32):19310-7. doi: 10.1074/jbc.271.32.19310. PMID: 8702615. 2.Tsuchiya, N., Sato, K., Akao, T., Kakinuma, H., Sasaki, R., Shimoda, N., Satoh, S., Habuchi, T., Ogawa, O., & Kato, T. (2001). Quantitative analysis of gene expressions of vascular endothelial growth factor-related factors and their receptors in renal cell carcinoma. The Tohoku journal of experimental medicine, 195(2), 101–113. https://doi.org/10.1620/tjem.195.101 |
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| Protein Function | is expressed abundantly in cardiac and skeletal muscle .It acts as a growth factor for endothelial cells. |
|---|
| Biochemical Properties | VEGF-B167 binds heparin and neuropilin-1 whereas the binding to neuropilin-1 of VEGF-B186 is regulated by proteolysis.VEGF are highly basic and bind to cellular or pericellular heparan sulfate proteoglycans, whereas the shorter isoforms are soluble in the extracellular fluid. |
|---|
| Significance in milk | Involvement in immunosuppression and hypoxia stress and heat stress. |
|---|
| PTMs | Disulphide bond, Glycosylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| na |
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| Predicted Disorder Regions | (19-33), (119-207) |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | VEGF-B186 is O-glycosylated presumably in its unique COOH-terminal domain.The addition of O-linked glycans may serve to compensate for the hydrophobic character of the VEGF-B186 COOH terminus and make the secreted protein more soluble in aqueous media. |
|---|
| Linking IDs | |
|---|
| Bibliography | 1.Olofsson B, Pajusola K, von Euler G, Chilov D, Alitalo K, Eriksson U. Genomic organization of the mouse and human genes for vascular endothelial growth factor B (VEGF-B) and characterization of a second splice isoform. J Biol Chem. 1996 Aug 9;271(32):19310-7. doi: 10.1074/jbc.271.32.19310. PMID: 8702615. 2.Tsuchiya, N., Sato, K., Akao, T., Kakinuma, H., Sasaki, R., Shimoda, N., Satoh, S., Habuchi, T., Ogawa, O., & Kato, T. (2001). Quantitative analysis of gene expressions of vascular endothelial growth factor-related factors and their receptors in renal cell carcinoma. The Tohoku journal of experimental medicine, 195(2), 101–113. https://doi.org/10.1620/tjem.195.101 |
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