SYRC_MOUSE
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 03-AUG-2022, entry version 166.
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, Pancreas,
RC 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; 21.
DR IntAct; Q9D0I9; 4.
DR STRING; 10090.ENSMUSP00000018992; -.
DR iPTMnet; Q9D0I9; -.
DR PhosphoSitePlus; Q9D0I9; -.
DR SwissPalm; Q9D0I9; -.
DR EPD; Q9D0I9; -.
DR jPOST; Q9D0I9; -.
DR MaxQB; Q9D0I9; -.
DR PaxDb; Q9D0I9; -.
DR PeptideAtlas; Q9D0I9; -.
DR PRIDE; Q9D0I9; -.
DR ProteomicsDB; 253442; -.
DR Antibodypedia; 1285; 247 antibodies from 33 providers.
DR DNASU; 104458; -.
DR Ensembl; ENSMUST00000018992; ENSMUSP00000018992; ENSMUSG00000018848.
DR GeneID; 104458; -.
DR KEGG; mmu:104458; -.
DR UCSC; uc007ilh.2; mouse.
DR CTD; 104458; -.
DR MGI; MGI:1914297; Rars.
DR VEuPathDB; HostDB:ENSMUSG00000018848; -.
DR eggNOG; KOG4426; Eukaryota.
DR GeneTree; ENSGT00530000063407; -.
DR HOGENOM; CLU_006406_5_1_1; -.
DR InParanoid; Q9D0I9; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 463402at2759; -.
DR PhylomeDB; Q9D0I9; -.
DR TreeFam; TF106111; -.
DR BioGRID-ORCS; 104458; 23 hits in 75 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 274 other tissues.
DR Genevisible; Q9D0I9; MM.
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; -; 1.
DR Gene3D; 3.40.50.620; -; 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 PANTHER; PTHR11956; PTHR11956; 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; SSF47323; 1.
DR SUPFAM; SSF55190; SSF55190; 1.
DR TIGRFAMs; TIGR00456; argS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
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