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UniProt functional annotation for P54136 | ||
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| UniProt code: P54136. |
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| Organism: | |
Homo sapiens (Human). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. |
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| Function: | |
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). {ECO:0000269|PubMed:17443684, ECO:0000269|PubMed:25288775}. |
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| Catalytic activity: | |
Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl- tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA- COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215; EC=6.1.1.19; Evidence={ECO:0000269|PubMed:16055448, ECO:0000269|PubMed:25288775}; |
| Biophysicochemical properties: | |
Kinetic parameters: KM=3.9 uM for arginine (ATP-PPi exchange at 37 degrees Celsius) {ECO:0000269|PubMed:16055448}; KM=3.5 uM for arginine (arginylation at 37 degrees Celsius) {ECO:0000269|PubMed:16055448}; KM=1183 uM for ATP (ATP-PPi exchange at 37 Celsius) {ECO:0000269|PubMed:16055448}; KM=910 uM for ATP (arginylation at 37 Celsius) {ECO:0000269|PubMed:16055448}; KM=0.05 uM for calf liver tRNA-Arg (ATP-PPi exchange at 37 Celsius) {ECO:0000269|PubMed:16055448}; KM=0.41 uM for calf liver tRNA-Arg (arginylation at 37 Celsius) {ECO:0000269|PubMed:16055448}; |
| Subunit: | |
Interacts (via N-terminus) with AIMP1 (via N-terminus); this stimulates its catalytic activity (PubMed:10358004, PubMed:25288775). Interacts (via N-terminus) with LARS2 (via C-terminus) (PubMed:16055448, PubMed:17443684). Monomer (PubMed:24859084). Part of a multisubunit complex that groups tRNA ligases for Arg (RARS1), Asp (DARS1), Gln (QARS1), Ile (IARS1), Leu (LARS1), Lys (KARS1), Met (MARS1) the bifunctional ligase for Glu and Pro (EPRS1) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18 (PubMed:19131329, PubMed:19289464). Interacts with QARS1 (PubMed:24656866). Part of a complex composed of RARS1, QARS1 and AIMP1 (PubMed:25288775). {ECO:0000269|PubMed:10358004, ECO:0000269|PubMed:16055448, ECO:0000269|PubMed:17443684, ECO:0000269|PubMed:19131329, ECO:0000269|PubMed:19289464, ECO:0000269|PubMed:24656866, ECO:0000269|PubMed:24859084, ECO:0000269|PubMed:25288775}. |
| Subcellular location: | |
Cytoplasm {ECO:0000269|PubMed:10791971, ECO:0000269|PubMed:16055448, ECO:0000269|PubMed:16430231}. Cytoplasm, cytosol {ECO:0000269|PubMed:19289464}. |
| Domain: | |
The alpha-helical N-terminus (residues 1-72) mediates interaction with AIMP1 and thereby contributes to the assembly of the multisynthetase complex. {ECO:0000269|PubMed:25288775}. |
| Disease: | |
Leukodystrophy, hypomyelinating, 9 (HLD9) [MIM:616140]: An autosomal recessive neurodegenerative disorder characterized by delayed psychomotor development, severe spasticity, nystagmus, and ataxia associated with diffuse hypomyelination apparent on brain MRI. {ECO:0000269|PubMed:24777941}. Note=The disease is caused by variants affecting the gene represented in this entry. |
| Similarity: | |
Belongs to the class-I aminoacyl-tRNA synthetase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.