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Primary Information | |
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| BoMiProt ID | Bomi2720 |
| Protein Name | Protein S100-A9 |
| Organism | Bos taurus |
| Uniprot ID | P28783 |
| Milk Fraction | Whey, MFGM, Exosome |
| Ref Sequence ID | NP_001039793.1 |
| Aminoacid Length | 156 |
| Molecular Weight | 17114 |
| FASTA Sequence | Download |
| Gene Name | S100A9 |
| Gene ID | 532569 |
| Protein Existence Status | Reviewed: Experimental evidence at protein level |
Secondary Information | |
| Presence in other biological fluids/tissue/cells | S100A8 and S100A9 are small calcium-binding proteins that are highly expressed in neutrophil and monocyte cytosol, endothelial and epithelial cells; uterus, cervix |
| Protein Function | s100 A8 and A9 are found at high levels in the extracellular milieu during inflammatory conditions; Extracellular S100A8, S100A9, and S100A8/A9 mediate regulatory and biological functions, including antiproliferative, antitumoral, antimicrobial, and antinociceptive activities and induce neutrophil adhesion to fibrinogen in vitro; vital role in regulating the interactions between the mammalian foetus and the uterus; important in regulating reproductive functions; showed specific patterns during the different stages of pregnancy; exert strong proinflammatory and chemotactic activities by promoting leukocyte recruitment; In murine macrophages, S100A8, but not S100A9, is induced by TLR agonists in an interleukin (IL)-10-dependent manner; some agonists require cAMP and/or PGE2 generation for full expression; In murine keratinocytes, S100A8 is induced by oxidative stress whereas S100A9 is not, confirming; S100A9 is a p38 MAPK target phosphorylated after phagocyte activation; S100A9 reduces microtubule polymerization and F-actin cross-linking by the S100A8/S100A9 complex; S100A8 and S100A9 form a heterocomplex. S100A8/S100A9 inhibits casein kinase I and II suggesting a role in myeloid cell differentiation |
| Biochemical Properties | S100A8 and S100A9 form noncovalent homodimers and a heterodimer (S100A8/A9) in a calcium-dependent manner; low molecular weight S100 proteins; EF-hand Ca2+-binding proteins; form homodimers as well as heterodimers; heterodimers assemble in a Ca2+ and Zn2+-dependent manner into heterotetrameric and larger complexes; ability to self-assemble into highly heterogeneous amyloid complexes, encompassing both oligomeric species and highly stable fibrils able to grow and accumulate in the ageing prostate; the function and biochemical properties of s100 A8 and A9 are mostly simily and both of them work forming heterocomplex |
| Significance in milk | involved in the innate immune defense against pathogens; |
| Linking IDs | Bomi15 |
| Bibliography | 1. Ryckman, C., Vandal, K., Rouleau, P., Talbot, M., & Tessier, P. A. (2003). Proinflammatory activities of S100: proteins S100A8, S100A9, and S100A8/A9 induce neutrophil chemotaxis and adhesion. Journal of Immunology (Baltimore, Md. : 1950), 170(6), 3233–3242. https://doi.org/10.4049/jimmunol.170.6.3233. 2. Addis, M. F., Pisanu, S., Marogna, G., Cubeddu, T., Pagnozzi, D., Cacciotto, C., … Uzzau, S. (2013). Production and release of antimicrobial and immune defense proteins by mammary epithelial cells following Streptococcus uberis infection of sheep. Infection and Immunity, 81(9), 3182–3197. https://doi.org/10.1128/IAI.00291-13. 3. Elgawish, R. A., Ogata, Y., Hidaka, T., Nii, T., Yoshimura, Y., & Isobe, N. (2018). Changes in plasma concentrations of S100A7 and S100A8 in dairy cows during pregnancy. Reproduction in Domestic Animals = Zuchthygiene, 53(4), 1013–1015. https://doi.org/10.1111/rda.13185 |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | |
| Predicted Disorder Regions | 1-9,27-29,44-57,90-156 |
| DisProt Annotation | |
| TM Helix Prediction | No TM helices |