Primary Information |
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| BoMiProt ID | Bomi140 |
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| Protein Name | Thrombospondin-1 |
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| Organism | Bos taurus |
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| Uniprot ID | Q28178 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_776621.1 |
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| Aminoacid Length | 1170 |
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| Molecular Weight | 129534 |
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| FASTA Sequence |
Download |
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| Gene Name | THBS1 |
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| Gene ID | 281530 |
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| Protein Existence Status | Reviewed: Experimental evidence at transcript level |
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Secondary Information |
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| Presence in other biological fluids/tissue/cells | Plasma, monocytes, α-granules of platelets, |
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| Protein Function | induces endothelial cell actin reorganization and focal
adhesion disassembly and influences multiple endothelial cell functions; influences cell
attachment to and spreading on substrates; cell motility; interacts with TGFß and modulates wound healing and proliferation; anti-angiogenic; |
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| Biochemical Properties | As found in platelets, the proteins has 3chains linked by disulfide bods; pI is 4.7; degradation
of the intact molecule with trypsin yields a stable
core particle of molecular weight 210,000 comprised of
three 70,000 chains; aspartic acid/asparagine, glutamic
acid/glutamine, and cysteine are significantly high and
leucine is significantly low as compared to other mammalian proteins ; not easily reduced by thrombin due to high cystein content; |
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| Significance in milk | kinetics
of thrombospondin accumulation in human and goat milk has shown temporal variations which could be due to hormonal regulation. TSP
was detected in the initial aqueous phase of milk secretion
and its levels subsequently fell during the transition to mature
milk |
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| PTMs | Glycosylated; contains neutral sugars, amino sugars, sialic acids; |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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| Predicted Disorder Regions | (839-944) |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Bibliography | 1. Goldblum, S. E., Young, B. A., Wang, P., & Murphy-Ullrich, J. E. (1999). Thrombospondin-1 Induces Tyrosine Phosphorylation of Adherens Junction Proteins and Regulates an Endothelial Paracellular Pathway. Molecular Biology of the Cell, 10(5), 1537–1551. https://doi.org/10.1091/mbc.10.5.1537.
2. Dawes, J., Clezardin, P., & Pratt, D. (1987). Thrombospondin in Milk, Other Breast Secretions, and Breast Tissue. Seminars in Thrombosis and Hemostasis, 13(03), 378–384. https://doi.org/10.1055/s-2007-1003514.
3. Lawler, J. W., Slayter, H. S., & Coligan, J. E. (1978). Isolation and characterization of a high molecular weight glycoprotein from human blood platelets. The Journal of Biological Chemistry, 253(23), 8609–8616. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/101549. |
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