|Protein Name||Heat shock protein 105 kDa|
|Milk Fraction||MFGM, Exosome|
|Ref Sequence Id||NP_001068770.1|
|Amino Acid Lenth||859|
|Protein Existence Status||Reviewed: Experimental evidence at transcript level|
|Presence in other biological fluids/tissue/cells||105-kDa heat-shock protein (HSP105) as a mammalian high molecular mass heat-shock protein in human, mouse, and rat cells; moderately expressed in adrenal, spleen, liver, lung, and heart; Small amounts of HSP105 are expressed in the kidney, stomach, muscle, testis, and lens. However, in brain HSP105-a was characteristically highly expressed over HSP105-b|
|Protein Function||induced in various tissues of rat after whole-body hyperthermia; HSP105 level of HSP10S increased markedly in the embryos from gestational day (GD) 9 to 11, then decreased gradually by GD 14; plays important roles in mouse embryogenesis; prevent the aggregation of heat-denatured proteins in vitro;|
|Biochemical Properties||HSPI05 is composed of two isoforms with slightly different isoelectric points with slightly different isoelectric points, acidic and basic isoforms; mRNA was also induced by azetidine-2-carboxylic acid, sodium arsenite, zinc sulfate, and cupric sulfate;|
|Significance in milk||heat stress proteins in mamary gland|
|Significance of PTMs||sensitive to heat stress and mainly responsible for mammary cell protection from heat stress|
|Bibliography||1. Ichiyanagi, T., Imai, T., Kajiwara, C., Mizukami, S., Nakai, A., Nakayama, T., & Udono, H. (2010). Essential role of endogenous heat shock protein 90 of dendritic cells in antigen cross-presentation. Journal of Immunology (Baltimore, Md. : 1950), 185(5), 2693–2700. https://doi.org/10.4049/jimmunol.1000821. |
2. French, J. B., Zhao, H., An, S., Niessen, S., Deng, Y., Cravatt, B. F., & Benkovic, S. J. (2013). Hsp70/Hsp90 chaperone machinery is involved in the assembly of the purinosome. Proceedings of the National Academy of Sciences of the United States of America, 110(7), 2528–2533. https://doi.org/10.1073/pnas.1300173110
3. Srivastava, P. K., Udono, H., Blachere, N. E., & Li, Z. (1994). Heat shock proteins transfer peptides during antigen processing and CTL priming. Immunogenetics, 39(2), 93–98. https://doi.org/10.1007/bf00188611
4. Samali, A., & Cotter, T. G. (1996). Heat shock proteins increase resistance to apoptosis. Experimental Cell Research, 223(1), 163–170. https://doi.org/10.1006/excr.1996.0070.
5. Polla, B. S., Healy, A. M., Wojno, W. C., & Krane, S. M. (1987). Hormone 1 alpha,25-dihydroxyvitamin D3 modulates heat shock response in monocytes. The American Journal of Physiology, 252(6 Pt 1), C640-9. https://doi.org/10.1152/ajpcell.1987.252.6.C640.
6. Shi, Y., & Thomas, J. O. (1992). The transport of proteins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate. Molecular and Cellular Biology, 12(5), 2186–2192. https://doi.org/10.1128/mcb.12.5.2186.
7. Guidon, P. T., & Hightower, L. E. (1986). Purification and initial characterization of the 71-kilodalton rat heat-shock protein and its cognate as fatty acid binding proteins. Biochemistry, 25(11), 3231–3239. https://doi.org/10.1021/bi00359a023.
8. Chappells, T. G., Konforti, B. B., Schmids, S. L., & Rothmann, J. E. (1987). The ATPase Core of. 262(2), 746–751.