Search by BoMiProt ID - Bomi10462


Primary Information

BoMiProt ID Bomi10462
Protein Name Vascular endothelial growth factor B/VEGF-related factor
Organism Bos taurus
Uniprot IdQ9XS49
Milk FractionWhey
Ref Sequence Id NP_776912.1
Aminoacid Length 207
Molecular Weight 21655
Fasta Sequence https://www.uniprot.org/uniprot/Q9XS49.fasta
Gene Name VEGFB/VRF
Gene Id 282121
Protein Existence Status reviewed

Secondary Information

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
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 Bomi10462
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
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
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
na
Predicted Disorder Regions (19-33), (119-207)
DisProt Annotation
TM Helix Prediction No TM helices
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