ID   SYRM_MOUSE              Reviewed;         578 AA.
AC   Q3U186; Q8QZU7;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 129.
DE   RecName: Full=Probable arginine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.19 {ECO:0000250|UniProtKB:Q5T160};
DE   AltName: Full=Arginyl-tRNA synthetase;
DE            Short=ArgRS;
DE   Flags: Precursor;
GN   Name=Rars2; Synonyms=Rarsl;
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=NOD; TISSUE=Spleen;
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 MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
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).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-568, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA   Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT   identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC   -!- FUNCTION: Catalyzes the attachment of arginine to tRNA(Arg) in a two-
CC       step reaction: arginine is first activated by ATP to form Arg-AMP and
CC       then transferred to the acceptor end of tRNA(Arg).
CC       {ECO:0000250|UniProtKB:Q5T160}.
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:0000250|UniProtKB:Q5T160};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC       {ECO:0000250|UniProtKB:Q5T160}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AK156182; BAE33614.1; -; mRNA.
DR   EMBL; BC024878; AAH24878.1; -; mRNA.
DR   CCDS; CCDS18029.1; -.
DR   RefSeq; NP_852071.2; NM_181406.3.
DR   AlphaFoldDB; Q3U186; -.
DR   SMR; Q3U186; -.
DR   BioGRID; 224553; 13.
DR   STRING; 10090.ENSMUSP00000029968; -.
DR   iPTMnet; Q3U186; -.
DR   PhosphoSitePlus; Q3U186; -.
DR   SwissPalm; Q3U186; -.
DR   EPD; Q3U186; -.
DR   jPOST; Q3U186; -.
DR   MaxQB; Q3U186; -.
DR   PaxDb; 10090-ENSMUSP00000029968; -.
DR   PeptideAtlas; Q3U186; -.
DR   ProteomicsDB; 253443; -.
DR   Pumba; Q3U186; -.
DR   Antibodypedia; 31811; 98 antibodies from 19 providers.
DR   DNASU; 109093; -.
DR   Ensembl; ENSMUST00000029968.14; ENSMUSP00000029968.8; ENSMUSG00000028292.15.
DR   GeneID; 109093; -.
DR   KEGG; mmu:109093; -.
DR   UCSC; uc008sgf.2; mouse.
DR   AGR; MGI:1923596; -.
DR   CTD; 57038; -.
DR   MGI; MGI:1923596; Rars2.
DR   VEuPathDB; HostDB:ENSMUSG00000028292; -.
DR   eggNOG; KOG1195; Eukaryota.
DR   GeneTree; ENSGT00530000063407; -.
DR   HOGENOM; CLU_006406_6_2_1; -.
DR   InParanoid; Q3U186; -.
DR   OMA; YEFKWER; -.
DR   OrthoDB; 67085at2759; -.
DR   PhylomeDB; Q3U186; -.
DR   TreeFam; TF300888; -.
DR   BioGRID-ORCS; 109093; 18 hits in 78 CRISPR screens.
DR   PRO; PR:Q3U186; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q3U186; Protein.
DR   Bgee; ENSMUSG00000028292; Expressed in ileal epithelium and 265 other cell types or tissues.
DR   ExpressionAtlas; Q3U186; baseline and differential.
DR   GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
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   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR001278; Arg-tRNA-ligase.
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; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 1.
DR   PRINTS; PR01038; TRNASYNTHARG.
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; Q3U186; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Membrane;
KW   Mitochondrion; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..16
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..578
FT                   /note="Probable arginine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000250732"
FT   MOTIF           133..144
FT                   /note="'HIGH' region"
FT   BINDING         133..135
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         144
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         322
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         326
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         350
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   MOD_RES         568
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   CONFLICT        306
FT                   /note="D -> G (in Ref. 2; AAH24878)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        540
FT                   /note="Q -> K (in Ref. 2; AAH24878)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   578 AA;  65336 MW;  5255FAFA8F873C27 CRC64;
     MACGFRRSIA CQLSRVLALP PESLIKSISA VPVSKKEEVA DFQLSVDSLL EDNNHKSQVD
     TQDQARRLAE KLKCDTVVTA ISAGPRTLNF KINRELLTKA VLQQVTEDGC KYGLKSELFS
     DLPKKRIVVE FSSPNIAKKF HVGHLRSTII GNFIANLKEA LGHQVTRINY IGDWGMQFGL
     LGTGFQLFGY EEKLQTNPLQ HLFDVYVQVN KEATDDKNVT KLAHEFFHRL EMGDTQALSL
     WQRFRDLSIE EYTQIYKRLG IYFDEYSGES FYREKSQDVL KLLDSKGLLQ KTAEGNVVVD
     LSGTGDLSSV CTVMRSDGTS LYATRDLAAA IHRMDKYNFD TMIYVADKGQ RRHFQQVFQM
     LKIMGYDWAE RCQHVPFGIV KGMKTRRGGV TFLEDVLNEV QSRMLQNMAS IKTTKQLENP
     QETAERVGLA AVIIQDFRGT LLSDYQFSWD RVFQSRGDTG VFLQYTHARL CSLEETFGCG
     YLNDSNVACL QEPQSVSILQ HLLRFDEVLY LSSQDLQPKH IVSYLLTLSH LAAVAHKTLQ
     VKDSPPDVAG ARLHLFKAVR SVLANGMKLL GITPVCRM
//