|Protein Name||Seryl-tRNA synthetase, cytoplasmic|
|Milk Fraction||MFGM, Exosome|
|Ref Sequence Id||NP_776600.1|
|Amino Acid Lenth||514|
|Protein Existence Status||Reviewed: Experimental evidence at transcript level|
|Protein Function||attachment of amino acids to their cognate tRNA species; discriminates with high selectivity among many structurally similar tRNAs and amino acids; responsible for the covalent attachment of serine to its cognate tRNASer|
|Biochemical Properties||a member of class II, an unusual enzyme compared with the other synthetases because of its substrate specificity- SerRS not only serylates tRNASer isoacceptors, but also the selenocysteine-incorporating tRNASec|
|Significance in milk||stimulate mTOR signalling pathway in presence of essential amino acids (EAA); enhancs EAA-stimulated cell proliferation and contribute to increased β-casein production in bovine mammary epithelial cells|
|Bibliography||1. Dai, W. T. et al. (2018) ‘Seryl-tRNA synthetase-mediated essential amino acids regulate β-casein synthesis via cell proliferation and mammalian target of rapamycin (mTOR) signaling pathway in bovine mammary epithelial cells’, Journal of Dairy Science, 101(11), pp. 10456–10468. doi: 10.3168/jds.2018-14568. |
2. Yokogawa, T. et al. (2000) ‘Characterization and tRNA Recognition of Mammalian Mitochondrial Seryl-tRNA Synthetase’, Journal of Biological Chemistry, 275(26), pp. 19913–19920. doi: 10.1074/jbc.M908473199.
3. Artero, J.-B. et al. (2010) ‘Crystallization and preliminary X-ray diffraction analysis of human cytosolic seryl-tRNA synthetase’, Acta Crystallographica Section F Structural Biology and Crystallization Communications, 66(11), pp. 1521–1524. doi: 10.1107/S1744309110037346.
4. Lee, W. H. et al. (1986) ‘Purification, biochemical characterization, and biological function of human esterase D.’, Proceedings of the National Academy of Sciences, 83(18), pp. 6790–6794. doi: 10.1073/pnas.83.18.6790.