ID SYRC_MOUSE Reviewed; 660 AA. AC Q9D0I9; Q3THP2; Q3TM73; Q3U8R2; Q3U930; Q5SXA8; Q8VDW1; DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2002, sequence version 2. DT 27-MAR-2024, entry version 175. DE RecName: Full=Arginine--tRNA ligase, cytoplasmic; DE EC=6.1.1.19 {ECO:0000269|PubMed:12060739}; DE AltName: Full=Arginyl-tRNA synthetase; DE Short=ArgRS; GN Name=Rars1; Synonyms=Rars; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RC TISSUE=Bone marrow macrophage, Embryo, Embryonic head, and Lung; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech 2; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP SUBUNIT, CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=12060739; DOI=10.1073/pnas.122110199; RA Kim J.Y., Kang Y.-S., Lee J.-W., Kim H.J., Ahn Y.H., Park H., Ko Y.-G., RA Kim S.; RT "p38 is essential for the assembly and stability of macromolecular tRNA RT synthetase complex: implications for its physiological significance."; RL Proc. Natl. Acad. Sci. U.S.A. 99:7912-7916(2002). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Forms part of a macromolecular complex that catalyzes the CC attachment of specific amino acids to cognate tRNAs during protein CC synthesis (PubMed:12060739). Modulates the secretion of AIMP1 and may CC be involved in generation of the inflammatory cytokine EMAP2 from CC AIMP1. {ECO:0000250|UniProtKB:P54136, ECO:0000269|PubMed:12060739}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl- CC tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA- CC COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215; CC EC=6.1.1.19; Evidence={ECO:0000269|PubMed:12060739}; CC -!- SUBUNIT: Interacts (via N-terminus) with AIMP1 (via N-terminus); this CC stimulates its catalytic activity. Interacts (via N-terminus) with CC LARS2 (via C-terminus). Monomer (By similarity). Part of a multisubunit CC complex that groups tRNA ligases for Arg (RARS1), Asp (DARS1), Gln CC (QARS1), Ile (IARS1), Leu (LARS1), Lys (KARS1), Met (MARS1) the CC bifunctional ligase for Glu and Pro (EPRS1) and the auxiliary subunits CC AIMP1/p43, AIMP2/p38 and EEF1E1/p18 (PubMed:12060739). Interacts with CC QARS1. Part of a complex composed of RARS1, QARS1 and AIMP1 (By CC similarity). {ECO:0000250|UniProtKB:P54136, CC ECO:0000269|PubMed:12060739}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P54136}. CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:P54136}. CC -!- DOMAIN: The alpha-helical N-terminus (residues 1-72) mediates CC interaction with AIMP1 and thereby contributes to the assembly of the CC multisynthetase complex. {ECO:0000250|UniProtKB:P54136}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK011383; BAB27583.1; -; mRNA. DR EMBL; AK076160; BAC36226.1; -; mRNA. DR EMBL; AK149856; BAE29127.1; -; mRNA. DR EMBL; AK151966; BAE30837.1; -; mRNA. DR EMBL; AK152108; BAE30955.1; -; mRNA. DR EMBL; AK166097; BAE38569.1; -; mRNA. DR EMBL; AK168194; BAE40154.1; -; mRNA. DR EMBL; AL596084; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466658; EDL16275.1; -; Genomic_DNA. DR EMBL; BC020132; AAH20132.1; -; mRNA. DR CCDS; CCDS24544.1; -. DR RefSeq; NP_080212.2; NM_025936.3. DR AlphaFoldDB; Q9D0I9; -. DR SMR; Q9D0I9; -. DR BioGRID; 222643; 23. DR IntAct; Q9D0I9; 4. DR STRING; 10090.ENSMUSP00000018992; -. DR GlyGen; Q9D0I9; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9D0I9; -. DR MetOSite; Q9D0I9; -. DR PhosphoSitePlus; Q9D0I9; -. DR SwissPalm; Q9D0I9; -. DR EPD; Q9D0I9; -. DR jPOST; Q9D0I9; -. DR MaxQB; Q9D0I9; -. DR PaxDb; 10090-ENSMUSP00000018992; -. DR PeptideAtlas; Q9D0I9; -. DR ProteomicsDB; 253442; -. DR Pumba; Q9D0I9; -. DR Antibodypedia; 1285; 280 antibodies from 33 providers. DR DNASU; 104458; -. DR Ensembl; ENSMUST00000018992.4; ENSMUSP00000018992.4; ENSMUSG00000018848.5. DR GeneID; 104458; -. DR KEGG; mmu:104458; -. DR UCSC; uc007ilh.2; mouse. DR AGR; MGI:1914297; -. DR CTD; 5917; -. DR MGI; MGI:1914297; Rars1. DR VEuPathDB; HostDB:ENSMUSG00000018848; -. DR eggNOG; KOG4426; Eukaryota. DR GeneTree; ENSGT00530000063407; -. DR HOGENOM; CLU_006406_5_1_1; -. DR InParanoid; Q9D0I9; -. DR OMA; CKSMLAW; -. DR OrthoDB; 67085at2759; -. DR PhylomeDB; Q9D0I9; -. DR TreeFam; TF106111; -. DR BioGRID-ORCS; 104458; 23 hits in 80 CRISPR screens. DR PRO; PR:Q9D0I9; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; Q9D0I9; Protein. DR Bgee; ENSMUSG00000018848; Expressed in embryonic post-anal tail and 278 other cell types or tissues. DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IDA:CAFA. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; HDA:MGI. DR GO; GO:0005730; C:nucleolus; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0034618; F:arginine binding; ISO:MGI. DR GO; GO:0004814; F:arginine-tRNA ligase activity; IMP:CAFA. DR GO; GO:0005524; F:ATP binding; ISO:MGI. DR GO; GO:0000049; F:tRNA binding; ISO:MGI. DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IDA:CAFA. DR CDD; cd00671; ArgRS_core; 1. DR Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR HAMAP; MF_00123; Arg_tRNA_synth; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR001278; Arg-tRNA-ligase. DR InterPro; IPR005148; Arg-tRNA-synth_N. DR InterPro; IPR036695; Arg-tRNA-synth_N_sf. DR InterPro; IPR035684; ArgRS_core. DR InterPro; IPR008909; DALR_anticod-bd. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd. DR NCBIfam; TIGR00456; argS; 1. DR PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1. DR PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 1. DR Pfam; PF03485; Arg_tRNA_synt_N; 1. DR Pfam; PF05746; DALR_1; 1. DR Pfam; PF00750; tRNA-synt_1d; 1. DR PRINTS; PR01038; TRNASYNTHARG. DR SMART; SM01016; Arg_tRNA_synt_N; 1. DR SMART; SM00836; DALR_1; 1. DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1. DR SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. DR Genevisible; Q9D0I9; MM. PE 1: Evidence at protein level; KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..660 FT /note="Arginine--tRNA ligase, cytoplasmic" FT /id="PRO_0000151659" FT REGION 1..72 FT /note="Could be involved in the assembly of the FT multisynthetase complex" FT REGION 529..543 FT /note="Interaction with tRNA" FT /evidence="ECO:0000250|UniProtKB:Q05506" FT MOTIF 201..212 FT /note="'HIGH' region" FT BINDING 200..202 FT /ligand="L-arginine" FT /ligand_id="ChEBI:CHEBI:32682" FT /evidence="ECO:0000250|UniProtKB:P54136" FT BINDING 211 FT /ligand="L-arginine" FT /ligand_id="ChEBI:CHEBI:32682" FT /evidence="ECO:0000250|UniProtKB:P54136" FT BINDING 384 FT /ligand="L-arginine" FT /ligand_id="ChEBI:CHEBI:32682" FT /evidence="ECO:0000250|UniProtKB:P54136" FT BINDING 388 FT /ligand="L-arginine" FT /ligand_id="ChEBI:CHEBI:32682" FT /evidence="ECO:0000250|UniProtKB:P54136" FT BINDING 412 FT /ligand="L-arginine" FT /ligand_id="ChEBI:CHEBI:32682" FT /evidence="ECO:0000250|UniProtKB:P54136" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P54136" FT CONFLICT 5 FT /note="V -> M (in Ref. 1; BAE30955)" FT /evidence="ECO:0000305" FT CONFLICT 178 FT /note="L -> H (in Ref. 1; BAB27583)" FT /evidence="ECO:0000305" FT CONFLICT 184 FT /note="Q -> E (in Ref. 1; BAE40154)" FT /evidence="ECO:0000305" FT CONFLICT 210 FT /note="G -> V (in Ref. 1; BAB27583)" FT /evidence="ECO:0000305" FT CONFLICT 252 FT /note="L -> M (in Ref. 1; BAE38569)" FT /evidence="ECO:0000305" FT CONFLICT 281 FT /note="D -> G (in Ref. 1; BAE40154)" FT /evidence="ECO:0000305" FT CONFLICT 288 FT /note="K -> E (in Ref. 1; BAE40154)" FT /evidence="ECO:0000305" FT CONFLICT 418 FT /note="T -> I (in Ref. 1; BAE40154)" FT /evidence="ECO:0000305" FT CONFLICT 474 FT /note="M -> L (in Ref. 1; BAB27583)" FT /evidence="ECO:0000305" FT CONFLICT 591 FT /note="D -> N (in Ref. 1; BAE38569)" FT /evidence="ECO:0000305" SQ SEQUENCE 660 AA; 75674 MW; 6E8EBCC590FAB81D CRC64; MDGLVAQCSA RLLQQEREIK ALTAEIDRLK NCGCLEASPS LEQLREENLK LKYRLNILRR SLQEERRKPT KNMININSRL QEVFGCAIRA AYPDLENPPL IVTPSQQPKF GDYQCNSAMG ISQMLKAKEQ KVSPREIAEN ITKHLPNNKY IDKVEIAGPG FINVHLRKDF VSEQLTSLLV NGVQLPVLGD KEKVIVDFSS PNIAKEMHVG HLRSTIIGES MSRLFEFAGY DVLRLNHVGD WGTQFGMLIA HLQDKFPDYL TVSPPIGDLQ AFYKESKKRF DADEEFKKRA YQCVVLLQSK NPDIMKAWNL ICDVSREEFK KIYDALDITL IERGESFYQD RMKDIVKEFE DKGFVQVDDG RKIVFVPGCS VPLTIVKSDG GYTYDTSDLA AIKQRLFEEK ANKIIYVVDN GQAIHFQTIF AAAQMIGWYD PKVTLVTHVG FGVVLGEDKK KFKTRSGETV RLMDLLEEGL KRSMDKLKEK ERDKVLTEEE LKAAQTSVAY GCIKYADLSH NRLNDYIFSF DKMLDDRGNT AAYLLYAFTR IRSIARLANI DEAMLQRAAR ETKIILDHEK EWKLGRCILR FPEILQKILD DLFLHTLCDY IYELATTFTE FYDSCYCVEK DRQTGKVLKV NMWRMLLCEA VAAVMAKGFD ILGIKPVQRM //