|Protein Name||Protein S100-A12|
|Ref Sequence ID||NP_777076.1|
|Protein Existence Status||Reviewed: Experimental evidence at protein level|
|Presence in other biological fluids/tissue/cells||neutrophils, monocytes, smooth muscle cells;|
|Protein Function||important mediators in many different cellular functions involving immunity, inflammation, cell proliferation, apoptosis and other activities; expression of S100A12 increased at some cases of human inflammatory diseases; modulate interactions between cytoskeletal elements and membranes; inhibits aggregation of aldolase and GAPDH and may have Ca2+-dependent chaperone/anti-chaperone-like functions; play a role in vascular remodeling|
|Biochemical Properties||calcium binding proteins; hinge domain are chemotactic for monocytes and mast cells; presence of a pseudo‐EF‐hand calcium‐binding site|
|Significance in milk||S100A12 was positively associated with the somatic cell count and the sodium and chloride concentrations of milk; a negative correlation was found between S100A12 and the potassium concentration and pH of milk; S100A12 level in milk may serve as a diagnostic tool for subclinical mastitis in cows without obvious clinical signs|
| Site(s) of PTM(s) |
|Predicted Disorder Regions||NA|
|TM Helix Prediction||No TM helices|
|Bibliography||1. Zhong, K., Zhang, C.-Y., Zha, G.-M., Wang, X.-J., Jiao, X.-Q., Zhu, H.-S., & Wang, Y.-Y. (2018). S100 calcium-binding protein A12 as a diagnostic index for subclinical mastitis in cows. Reproduction in Domestic Animals = Zuchthygiene, 53(6), 1442–1447. https://doi.org/10.1111/rda.13273. |
2. Hofmann Bowman, M., Wilk, J., Heydemann, A., Kim, G., Rehman, J., Lodato, J. A., … McNally, E. M. (2010). S100A12 mediates aortic wall remodeling and aortic aneurysm. Circulation Research, 106(1), 145–154. https://doi.org/10.1161/CIRCRESAHA.109.209486.
3. Hatakeyama, T., Okada, M., Shimamoto, S., Kubota, Y., & Kobayashi, R. (2004). Identification of intracellular target proteins of the calcium-signaling protein S100A12. European Journal of Biochemistry, 271(18), 3765–3775. https://doi.org/10.1111/j.1432-1033.2004.04318.
4. Vogl, T., Pröpper, C., Hartmann, M., Strey, A., Strupat, K., van den Bos, C., … Roth, J. (1999). S100A12 is expressed exclusively by granulocytes and acts independently from MRP8 and MRP14. The Journal of Biological Chemistry, 274(36), 25291–25296. https://doi.org/10.1074/jbc.274.36.25291.