|Protein Name||1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1|
|Milk Fraction||Whey, Exosome|
|Ref Sequence ID||NP_777242.1|
|Protein Existence Status||Reviewed: Experimental evidence at protein level|
|Protein Function||class of phospholipases that cleaves phospholipids on the diacylglycerol (DAG) side of the phosphodiester bond producing DAGs and phosphomonoesters; constitutes an important step in the inositide signaling pathways; plays an important role in brain function and is thus associated with brain disorders; it regulates both cortical development and synaptic plasticity; participate in the differentiation and activation of immune cells that control both the innate and adaptive immune systems; linked to the development of myeloproliferative neoplasm in mice; specifi c key role in cell migration and invasion, therefore contributing to carcinogenesis|
|Biochemical Properties||calcium (Ca2+)-dependent phosphodiesterases; PI-PLCß enzymes are usually activated by G protein-coupled receptors; PI-PLCγ subtypes are commonly activated by receptor tyrosine kinase (RTK), via SH2 domain-phospho-tyrosine interaction; Most of PI-PLCß may have a high guanosine; triphosphatase activating protein (GAP) activity|
|Significance in milk||responsible for the hydrolyses of phospholipids of the MFG membrane, thereby affecting the stability of the cream emulsion;|
|PTMs||Palmitoylation at Ser, Phosphorylation at Ser/Thr|
| Site(s) of PTM(s) |
|Predicted Disorder Regions||470-525,849-871,1200-1216|
|TM Helix Prediction||No TM helices|
|Significance of PTMs||Palmitoylation at Cys-17 by ZDHHC21 regulates the signaling activity of PLCB1 and the function of the endothelial barrier. Palmitoylation by ZDHHC21 is stimulated by inflammation.|
|Additional Comments||13 mammalian PLC isozymes identified so far are organized within 6 families: β(1–4), γ(1–2), δ(1,3,4), ε, ζ and η(1–2); phospholipase treatment of milk was found to reduce fat losses in whey and cooking water and to increase CY by improving fat and moisture retention in the cheese curd in Mozzarella cheese|
|Bibliography||1. Xiao, W., Hong, H., Kawakami, Y., Kato, Y., Wu, D., Yasudo, H., … Kawakami, T. (2009). Tumor suppression by phospholipase C-beta3 via SHP-1-mediated dephosphorylation of Stat5. Cancer Cell, 16(2), 161–171. https://doi.org/10.1016/j.ccr.2009.05.018. |
2. Lin, X. H., Kitamura, N., Hashimoto, T., Shirakawa, O., & Maeda, K. (1999). Opposite changes in phosphoinositide-specific phospholipase C immunoreactivity in the left prefrontal and superior temporal cortex of patients with chronic schizophrenia. Biological Psychiatry, 46(12), 1665–1671. https://doi.org/10.1016/s0006-3223(99)00036-0.
3. Koh, H.-Y. (2013). Phospholipase C-β1 and schizophrenia-related behaviors. Advances in Biological Regulation, 53(3), 242–248. https://doi.org/10.1016/j.jbior.2013.08.002.
4. Ross, E. M., Mateu, D., Gomes, A. V, Arana, C., Tran, T., & Litosch, I. (2006). Structural determinants for phosphatidic acid regulation of phospholipase C-beta1. The Journal of Biological Chemistry, 281(44), 33087–33094. https://doi.org/10.1074/jbc.M606487200.
5. Poli, A., Mongiorgi, S., Cocco, L., & Follo, M. Y. (2014). Protein kinase C involvement in cell cycle modulation. Biochemical Society Transactions, 42(5), 1471–1476. https://doi.org/10.1042/BST20140128.
6. Béziau, D. M., Toussaint, F., Blanchette, A., Dayeh, N. R., Charbel, C., Tardif, J. C., … Ledoux, J. (2015). Expression of Phosphoinositide-Specific Phospholipase C Isoforms in Native Endothelial Cells. PLoS ONE, 10(4). https://doi.org/10.1371/journal.pone.0123769.
7. Dadousis, C., Pegolo, S., Rosa, G. J. M., Gianola, D., Bittante, G., & Cecchinato, A. (2017). Pathway-based genome-wide association analysis of milk coagulation properties, curd firmness, cheese yield, and curd nutrient recovery in dairy cattle. Journal of Dairy Science, 100(2), 1223–1231. https://doi.org/10.3168/jds.2016-11587.