Primary Information |
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| BoMiProt ID | Bomi316 |
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| Protein Name | Protein phosphatase 1 regulatory subunit 7 |
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| Organism | Bos taurus |
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| Uniprot ID | Q3T0W4 |
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| Milk Fraction | Exosome |
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| Aminoacid Length | 360 |
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| Molecular Weight | 41388 |
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| FASTA Sequence |
Download |
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| Gene Name | PPP1R7 |
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| Gene ID | 505297 |
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| Protein Existence Status | Reviewed: Experimental evidence at protein level |
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Secondary Information |
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| Protein Function | serine/threonine phosphatase that regulates diverse, essential cellular processes
such as cell cycle progression, protein synthesis, muscle contraction, carbohydrate metabolism,
transcription and neuronal signaling; |
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| Biochemical Properties | specific inhibitory proteins,
such as inhibitor-2 and DARPP-32, bind and block the protein phosphatase1 catalytic active site, which
contains two metal ions (Mn2+), that are
required for the enzymatic activity; The catalytic site of PP1 is at the intersection of
three potential substrate binding regions, the hydrophobic, acidic and C-terminal grooves; two Mn2+ ions bind the PP1 active site in solution; apo form of the enzyme is only stable for
short periods of time before it begins to form soluble aggregates; prominent inhibitors are microcystin, nodularin
, calyculin A, tautomycin and okadaic acid; PP1c is also specifically inhibited by small acidic thermostable proteins, such as inhibitor-1, inhibitor-2, NIPPs (1), and
IP |
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| Significance in milk | could adjust the development and
lactation of mammary gland |
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| PTMs | phosphorylated - catalytic subunit of protein phosphatase 2A(PP2Ac) is phosphorylated by receptor and Src family
tyrosine kinases on Tyr307,upstream of its carboxyl
terminus (Leu309); In
vitro, PP2Ac phosphorylation is found to be on Thr
residue(s) catalyzed by the autophosphorylation-activated protein
kinas ; PP2Ac is methylated on Leu309 by a
novel type of carboxyl protein methyltransferase |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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| Predicted Disorder Regions | (1-65) |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | phosphorylation - (PP2Ac) phosphorylation on Tyr307 and Leu309 suppresses its activity; In
vitro, PP2Ac phosphorylation on Thr
residue(s) inactivates the enzyme |
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| Bibliography | 1. Favre, B., Turowski, P. and Hemmings, B. A. (1997) ‘Differential Inhibition and Posttranslational Modification of Protein Phosphatase 1 and 2A in MCF7 Cells Treated with Calyculin-A, Okadaic Acid, and Tautomycin’, Journal of Biological Chemistry, 272(21), pp. 13856–13863. doi: 10.1074/jbc.272.21.13856.
2. Hou, J. et al. (2017) ‘Detection and comparison of microRNAs in the caprine mammary gland tissues of colostrum and common milk stages’, BMC Genetics, 18(1), p. 38. doi: 10.1186/s12863-017-0498-2.
3. Dancheck, B. et al. (2011) ‘Molecular Investigations of the Structure and Function of the Protein Phosphatase 1−Spinophilin−Inhibitor 2 Heterotrimeric Complex’, Biochemistry, 50(7), pp. 1238–1246. doi: 10.1021/bi101774g.
4. Kelker, M. S., Page, R. and Peti, W. (2009) ‘Crystal Structures of Protein Phosphatase-1 Bound to Nodularin-R and Tautomycin: A Novel Scaffold for Structure-based Drug Design of Serine/Threonine Phosphatase Inhibitors’, Journal of Molecular Biology, 385(1), pp. 11–21. doi: 10.1016/j.jmb.2008.10.053.
5. Kita, A. et al. (2002) ‘Crystal structure of the complex between calyculin A and the catalytic subunit of protein phosphatase 1.’, Structure (London, England : 1993), 10(5), pp. 715–24. doi: 10.1016/s0969-2126(02)00764-5.
6. Maynes, J. T. et al. (2001) ‘Crystal Structure of the Tumor-promoter Okadaic Acid Bound to Protein Phosphatase-1’, Journal of Biological Chemistry, 276(47), pp. 44078–44082. doi: 10.1074/jbc.M107656200. |
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