Arginine--tRNA ligase, cytoplasmic (RARS)
The protein contains 660 amino acids for an estimated molecular weight of 75379 Da.
Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis (PubMed:25288775). Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1 (PubMed:17443684). (updated: Jan. 31, 2018)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| HLD9 | |
| dbSNP:rs244903 | |
| dbSNP:rs1059443 | |
| dbSNP:rs2305734 | |
| HLD9 |
Biological Process
Arginyl-tRNA aminoacylation
Gene expression
TRNA aminoacylation for protein translation
Cellular Component
Aminoacyl-tRNA synthetase multienzyme complex
Cytoplasm
Cytosol
Extracellular exosome
Membrane
Mitochondrion
Nucleoplasm
Nucleus
Molecular Function
Arginine binding
Arginine-tRNA ligase activity
ATP binding
Cadherin binding
TRNA binding
The reference OMIM entry for this protein is 107820
Arginyl-trna synthetase; rars
Arginyl-trna synthetase 1; rars1
Arginyl-trna synthetase, cytoplasmic
DESCRIPTION
The RARS gene encodes ArgRS, the cytoplasmic tRNA synthetase for arginine, which is a component of the multienzyme aminoacyl-tRNA synthetase complex (summary by Wolf et al., 2014).CLONING
Girjes et al. (1995) isolated a full-length cDNA corresponding to the RARS gene and identified an open reading frame of 1983 nucleotides with 87% homology to other mammalian RARS. Northern blot analysis revealed the presence of a single mRNA species of approximately 2.2 kb.GENE FUNCTION
Using forward genetic screens in Caenorhabditis elegans, Anderson et al. (2009) isolated a hypoxia-resistant reduction-of-function mutant of rrt1 (whose human homolog is RARS1), which encodes an arginyl-transfer RNA synthetase, an enzyme essential for protein translation. Knockdown of rrt1, and of most other genes encoding aminoacyl-tRNA synthetases, rescued animals from hypoxia-induced death, and the level of hypoxia resistance was inversely correlated with translation rate. The unfolded protein response was induced by hypoxia and was required for the hypoxia resistance of the reduction-of-function mutant of rrt1. Thus, Anderson et al. (2009) concluded that translational suppression produces hypoxia resistance, in part by reducing unfolding protein toxicity.MAPPING
Arfin et al. (1985) assigned the gene for arginyl-tRNA synthetase to chromosome 5 by study of somatic cell hybrids. Of the 7 aminoacyl-tRNA synthetase genes mapped to that time, 4 were on chromosome 5, which represents only about 7% of the total human genome.MOLECULAR GENETICS
In 4 patients from 3 unrelated families from the Netherlands with hypomyelinating leukodystrophy-9 (HLD9; 616140), Wolf et al. (2014) identified compound heterozygous mutations in the RARS gene (107820.0001-107820.0005). Mutations in 2 of the families were found by whole-exome sequencing and confirmed by Sanger sequencing. All patients carried 1 missense mutation and a mutation predicted to result in the loss of a functional protein in trans; functional studies of the variants were not performed. All patients presented in the first year of life with severe spasticity of the lower limbs, mild spasticity of the upper limbs, nystagmus, and mental retardation. Brain imaging was consistent with hypomyelination affecting the supra- and infratentorial regions. The severity of the overall phenotype was variable. ... More on the omim web site
Feb. 5, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 107820 was added.
Jan. 27, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed