|Protein Name||Arginyl-tRNA synthetase, cytoplasmic|
|Ref Sequence ID||NP_001098808.1|
|Protein Existence Status||Reviewed: Experimental evidence at transcript level|
|Protein Function||tRNA-binding protein that catalyzes the esterification of l-arginine to its cognate tRNA; aminoacyl adenylate formation occurs in the presence of amino acids, ATP and Mg2+, and then the aminoacyl group of the enzyme-bound intermediate is transferred to the 30-end of the cognate tRNA to form an aminoacyl-tRNA; protein translation, one ArgRS isoform,a component of the multi-synthetase complex, interacts with several proteins, such as the tRNA-associating factor p43 and leucyl-tRNA synthetase, through its 72 amino acid N-terminal extension; play a role in the N-end rule pathway of ubiquitin-dependent protein degradation by participating in the formation and provision of ArgtRNAArg to arginyl-tRNA transferase for arginylation of all acidic N-terminal residue, as well as oxidized cysteine. The free form of human cytoplasmic arginyl-tRNA synthetase (hcArgRS) is hypothesized to participate in ubiquitin-dependent protein degradation by offering arginyl-tRNA(Arg) to arginyl-tRNA transferase (ATE1).|
|Biochemical Properties||native form of mammalian arginyl-tRNA synthetase (ArgRS) is a monomer; p43 to ArgRS reduces the apparent KM of ArgRS to tRNA; one of the nine synthetase components of a multienzyme complex containing three auxiliary proteins; require the presence of cognate tRNA for amino acid activation; second isoform, lacks the N-terminal extension and exists as a free protein|
|Significance in milk||might play a part in tissue differentiation and regulation of mammary gland; individual tRNA's and aminoacyl-tRNA synthetases correspond to the amino acid composition of the main milk proteins|
|PTMs||N-acetylation at Methionine|
| Site(s) of PTM(s) |
|Predicted Disorder Regions||NA|
|TM Helix Prediction||No TM helices|
|Bibliography||1. Kim, H. S. et al. (2014) ‘The crystal structure of arginyl-tRNA synthetase from Homo sapiens’, FEBS Letters, 588(14), pp. 2328–2334. doi: 10.1016/j.febslet.2014.05.027. |
2. Elska, A. et al. (1971) ‘tRNA and aminoacyl-tRNA synthetases during differentiation and various functional states of the mammary gland’, Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 247(3), pp. 430–440. doi: 10.1016/0005-2787(71)90029-3.
3. Guigou, L., Shalak, V. and Mirande, M. (2004) ‘The tRNA-Interacting Factor p43 Associates with Mammalian Arginyl-tRNA Synthetase but Does Not Modify Its tRNA Aminoacylation Properties †’, Biochemistry, 43(15), pp. 4592–4600. doi: 10.1021/bi036150e. 4.Yang F, Xia X, Lei HY, Wang ED. Hemin binds to human cytoplasmic arginyl-tRNA synthetase and inhibits its catalytic activity. J Biol Chem. 2010 Dec 10;285(50):39437-46. doi: 10.1074/jbc.M110.159913. Epub 2010 Oct 5. PMID: 20923763; PMCID: PMC2998122.