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Database: UniProt
Entry: SYRC_MOUSE
LinkDB: SYRC_MOUSE
Original site: 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   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, 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}.
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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   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; 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.
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
//
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