ID SYRC_HUMAN Reviewed; 660 AA. AC P54136; B2RBS9; Q53GY4; Q9BWA1; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2002, sequence version 2. DT 27-MAR-2024, entry version 223. DE RecName: Full=Arginine--tRNA ligase, cytoplasmic; DE EC=6.1.1.19 {ECO:0000269|PubMed:16055448, ECO:0000269|PubMed:25288775}; DE AltName: Full=Arginyl-tRNA synthetase; DE Short=ArgRS; GN Name=RARS1 {ECO:0000312|HGNC:HGNC:9870}; Synonyms=RARS; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7590355; DOI=10.1016/0378-1119(95)00502-w; RA Girjes A.A., Hobson K., Chen P., Lavin M.F.; RT "Cloning and characterization of cDNA encoding a human arginyl-tRNA RT synthetase."; RL Gene 164:347-350(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Muscle; 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 [6] RP PROTEIN SEQUENCE OF 1-11. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [7] RP INTERACTION WITH AIMP1. RX PubMed=10358004; DOI=10.1074/jbc.274.24.16673; RA Park S.G., Jung K.H., Lee J.S., Jo Y.J., Motegi H., Kim S., Shiba K.; RT "Precursor of pro-apoptotic cytokine modulates aminoacylation activity of RT tRNA synthetase."; RL J. Biol. Chem. 274:16673-16676(1999). RN [8] RP SUBCELLULAR LOCATION. RX PubMed=10791971; DOI=10.1083/jcb.149.3.567; RA Ko Y.G., Kang Y.S., Kim E.K., Park S.G., Kim S.; RT "Nucleolar localization of human methionyl-tRNA synthetase and its role in RT ribosomal RNA synthesis."; RL J. Cell Biol. 149:567-574(2000). RN [9] RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, RP AND INTERACTION WITH LARS2. RX PubMed=16055448; DOI=10.1074/jbc.m413511200; RA Ling C., Yao Y.N., Zheng Y.G., Wei H., Wang L., Wu X.F., Wang E.D.; RT "The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase RT is indispensable in its interaction with arginyl-tRNA synthetase in the RT multi-tRNA synthetase complex."; RL J. Biol. Chem. 280:34755-34763(2005). RN [10] RP SUBCELLULAR LOCATION, AND ALTERNATIVE INITIATION. RX PubMed=16430231; DOI=10.1021/bi051675n; RA Zheng Y.-G., Wei H., Ling C., Xu M.-G., Wang E.-D.; RT "Two forms of human cytoplasmic arginyl-tRNA synthetase produced from two RT translation initiations by a single mRNA."; RL Biochemistry 45:1338-1344(2006). RN [11] RP FUNCTION, AND INTERACTION WITH AIMP1. RX PubMed=17443684; DOI=10.1002/jcp.21083; RA Bottoni A., Vignali C., Piccin D., Tagliati F., Luchin A., Zatelli M.C., RA Uberti E.C.; RT "Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer cell RT lines."; RL J. Cell. Physiol. 212:293-297(2007). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=19131329; DOI=10.1074/jbc.m809636200; RA Kaminska M., Havrylenko S., Decottignies P., Gillet S., Le Marechal P., RA Negrutskii B., Mirande M.; RT "Dissection of the structural organization of the aminoacyl-tRNA synthetase RT complex."; RL J. Biol. Chem. 284:6053-6060(2009). RN [14] RP SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=19289464; DOI=10.1074/jbc.m900480200; RA Kaminska M., Havrylenko S., Decottignies P., Le Marechal P., Negrutskii B., RA Mirande M.; RT "Dynamic Organization of Aminoacyl-tRNA Synthetase Complexes in the RT Cytoplasm of Human Cells."; RL J. Biol. Chem. 284:13746-13754(2009). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [19] RP INTERACTION WITH QARS1. RX PubMed=24656866; DOI=10.1016/j.ajhg.2014.03.003; RA Zhang X., Ling J., Barcia G., Jing L., Wu J., Barry B.J., Mochida G.H., RA Hill R.S., Weimer J.M., Stein Q., Poduri A., Partlow J.N., Ville D., RA Dulac O., Yu T.W., Lam A.T., Servattalab S., Rodriguez J., Boddaert N., RA Munnich A., Colleaux L., Zon L.I., Soll D., Walsh C.A., Nabbout R.; RT "Mutations in QARS, encoding glutaminyl-tRNA synthetase, cause progressive RT microcephaly, cerebral-cerebellar atrophy, and intractable seizures."; RL Am. J. Hum. Genet. 94:547-558(2014). RN [20] RP INVOLVEMENT IN HLD9, AND VARIANTS HLD9 GLY-2 AND GLN-512. RX PubMed=24777941; DOI=10.1002/ana.24167; RA Wolf N.I., Salomons G.S., Rodenburg R.J., Pouwels P.J., Schieving J.H., RA Derks T.G., Fock J.M., Rump P., van Beek D.M., van der Knaap M.S., RA Waisfisz Q.; RT "Mutations in RARS cause hypomyelination."; RL Ann. Neurol. 76:134-139(2014). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [22] {ECO:0007744|PDB:4Q2T, ECO:0007744|PDB:4Q2X, ECO:0007744|PDB:4Q2Y} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 73-660 IN COMPLEXES WIT ARGININE RP AND CANAVANINE, AND SUBUNIT. RX PubMed=24859084; DOI=10.1016/j.febslet.2014.05.027; RA Kim H.S., Cha S.Y., Jo C.H., Han A., Hwang K.Y.; RT "The crystal structure of arginyl-tRNA synthetase from Homo sapiens."; RL FEBS Lett. 588:2328-2334(2014). RN [23] {ECO:0007744|PDB:4R3Z} RP X-RAY CRYSTALLOGRAPHY (4.03 ANGSTROMS) IN COMPLEX WITH QARS1 AND AIMP1, RP SUBUNIT, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=25288775; DOI=10.1073/pnas.1408836111; RA Fu Y., Kim Y., Jin K.S., Kim H.S., Kim J.H., Wang D., Park M., Jo C.H., RA Kwon N.H., Kim D., Kim M.H., Jeon Y.H., Hwang K.Y., Kim S., Cho Y.; RT "Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for RT mammalian translation."; RL Proc. Natl. Acad. Sci. U.S.A. 111:15084-15089(2014). 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:25288775). Modulates the secretion of AIMP1 and may CC be involved in generation of the inflammatory cytokine EMAP2 from AIMP1 CC (PubMed:17443684). {ECO:0000269|PubMed:17443684, CC ECO:0000269|PubMed:25288775}. 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:16055448, CC ECO:0000269|PubMed:25288775}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=3.9 uM for arginine (ATP-PPi exchange at 37 degrees Celsius) CC {ECO:0000269|PubMed:16055448}; CC KM=3.5 uM for arginine (arginylation at 37 degrees Celsius) CC {ECO:0000269|PubMed:16055448}; CC KM=1183 uM for ATP (ATP-PPi exchange at 37 Celsius) CC {ECO:0000269|PubMed:16055448}; CC KM=910 uM for ATP (arginylation at 37 Celsius) CC {ECO:0000269|PubMed:16055448}; CC KM=0.05 uM for calf liver tRNA-Arg (ATP-PPi exchange at 37 Celsius) CC {ECO:0000269|PubMed:16055448}; CC KM=0.41 uM for calf liver tRNA-Arg (arginylation at 37 Celsius) CC {ECO:0000269|PubMed:16055448}; CC -!- SUBUNIT: Interacts (via N-terminus) with AIMP1 (via N-terminus); this CC stimulates its catalytic activity (PubMed:10358004, PubMed:25288775). CC Interacts (via N-terminus) with LARS2 (via C-terminus) CC (PubMed:16055448, PubMed:17443684). Monomer (PubMed:24859084). Part of CC a multisubunit complex that groups tRNA ligases for Arg (RARS1), Asp CC (DARS1), Gln (QARS1), Ile (IARS1), Leu (LARS1), Lys (KARS1), Met CC (MARS1) the bifunctional ligase for Glu and Pro (EPRS1) and the CC auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18 CC (PubMed:19131329, PubMed:19289464). Interacts with QARS1 CC (PubMed:24656866). Part of a complex composed of RARS1, QARS1 and AIMP1 CC (PubMed:25288775). {ECO:0000269|PubMed:10358004, CC ECO:0000269|PubMed:16055448, ECO:0000269|PubMed:17443684, CC ECO:0000269|PubMed:19131329, ECO:0000269|PubMed:19289464, CC ECO:0000269|PubMed:24656866, ECO:0000269|PubMed:24859084, CC ECO:0000269|PubMed:25288775}. CC -!- INTERACTION: CC P54136; Q12904-2: AIMP1; NbExp=3; IntAct=EBI-355482, EBI-12412735; CC P54136; Q96NT0: CCDC115; NbExp=3; IntAct=EBI-355482, EBI-2810325; CC P54136; Q9P2J5: LARS1; NbExp=4; IntAct=EBI-355482, EBI-356077; CC P54136; Q96K83: ZNF521; NbExp=3; IntAct=EBI-355482, EBI-6597673; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10791971, CC ECO:0000269|PubMed:16055448, ECO:0000269|PubMed:16430231}. Cytoplasm, CC cytosol {ECO:0000269|PubMed:19289464}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=Complexed; CC IsoId=P54136-1; Sequence=Displayed; CC Name=Monomeric; CC IsoId=P54136-2; Sequence=VSP_018905; 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:0000269|PubMed:25288775}. CC -!- DISEASE: Leukodystrophy, hypomyelinating, 9 (HLD9) [MIM:616140]: An CC autosomal recessive neurodegenerative disorder characterized by delayed CC psychomotor development, severe spasticity, nystagmus, and ataxia CC associated with diffuse hypomyelination apparent on brain MRI. CC {ECO:0000269|PubMed:24777941}. Note=The disease is caused by variants CC affecting the gene represented in this entry. 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; S80343; AAB35627.1; -; mRNA. DR EMBL; BT007394; AAP36058.1; -; mRNA. DR EMBL; AK314795; BAG37326.1; -; mRNA. DR EMBL; AK222797; BAD96517.1; -; mRNA. DR EMBL; BC000528; AAH00528.1; -; mRNA. DR EMBL; BC014619; AAH14619.1; -; mRNA. DR CCDS; CCDS4367.1; -. [P54136-1] DR PIR; JC4365; JC4365. DR RefSeq; NP_002878.2; NM_002887.3. [P54136-1] DR PDB; 4Q2T; X-ray; 2.40 A; A/B=73-660. DR PDB; 4Q2X; X-ray; 2.80 A; A/B=73-660. DR PDB; 4Q2Y; X-ray; 2.80 A; A/B=73-660. DR PDB; 4R3Z; X-ray; 4.03 A; B=1-660. DR PDB; 4ZAJ; X-ray; 2.22 A; A=73-660. DR PDBsum; 4Q2T; -. DR PDBsum; 4Q2X; -. DR PDBsum; 4Q2Y; -. DR PDBsum; 4R3Z; -. DR PDBsum; 4ZAJ; -. DR AlphaFoldDB; P54136; -. DR SMR; P54136; -. DR BioGRID; 111852; 320. DR ComplexPortal; CPX-2469; Multiaminoacyl-tRNA synthetase complex. DR CORUM; P54136; -. DR IntAct; P54136; 68. DR MINT; P54136; -. DR STRING; 9606.ENSP00000231572; -. DR BindingDB; P54136; -. DR ChEMBL; CHEMBL2824; -. DR GlyGen; P54136; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P54136; -. DR MetOSite; P54136; -. DR PhosphoSitePlus; P54136; -. DR SwissPalm; P54136; -. DR BioMuta; RARS; -. DR DMDM; 20178331; -. DR EPD; P54136; -. DR jPOST; P54136; -. DR MassIVE; P54136; -. DR MaxQB; P54136; -. DR PaxDb; 9606-ENSP00000231572; -. DR PeptideAtlas; P54136; -. DR ProteomicsDB; 56650; -. [P54136-1] DR ProteomicsDB; 56651; -. [P54136-2] DR Pumba; P54136; -. DR ABCD; P54136; 1 sequenced antibody. DR Antibodypedia; 1285; 280 antibodies from 33 providers. DR DNASU; 5917; -. DR Ensembl; ENST00000231572.8; ENSP00000231572.3; ENSG00000113643.9. [P54136-1] DR GeneID; 5917; -. DR KEGG; hsa:5917; -. DR MANE-Select; ENST00000231572.8; ENSP00000231572.3; NM_002887.4; NP_002878.2. DR UCSC; uc003lzx.4; human. [P54136-1] DR AGR; HGNC:9870; -. DR CTD; 5917; -. DR DisGeNET; 5917; -. DR GeneCards; RARS1; -. DR HGNC; HGNC:9870; RARS1. DR HPA; ENSG00000113643; Low tissue specificity. DR MalaCards; RARS1; -. DR MIM; 107820; gene. DR MIM; 616140; phenotype. DR neXtProt; NX_P54136; -. DR OpenTargets; ENSG00000113643; -. DR Orphanet; 438114; RARS-related autosomal recessive hypomyelinating leukodystrophy. DR PharmGKB; PA34231; -. DR VEuPathDB; HostDB:ENSG00000113643; -. DR eggNOG; KOG4426; Eukaryota. DR GeneTree; ENSGT00530000063407; -. DR HOGENOM; CLU_006406_5_1_1; -. DR InParanoid; P54136; -. DR OMA; CKSMLAW; -. DR OrthoDB; 67085at2759; -. DR PhylomeDB; P54136; -. DR TreeFam; TF106111; -. DR BRENDA; 6.1.1.19; 2681. DR PathwayCommons; P54136; -. DR Reactome; R-HSA-2408522; Selenoamino acid metabolism. DR Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation. DR SABIO-RK; P54136; -. DR SignaLink; P54136; -. DR SIGNOR; P54136; -. DR BioGRID-ORCS; 5917; 644 hits in 1127 CRISPR screens. DR ChiTaRS; RARS; human. DR GeneWiki; RARS_(gene); -. DR GenomeRNAi; 5917; -. DR Pharos; P54136; Tchem. DR PRO; PR:P54136; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; P54136; Protein. DR Bgee; ENSG00000113643; Expressed in calcaneal tendon and 154 other cell types or tissues. DR ExpressionAtlas; P54136; baseline and differential. DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:CAFA. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:CAFA. DR GO; GO:0034618; F:arginine binding; IEA:Ensembl. DR GO; GO:0004814; F:arginine-tRNA ligase activity; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0000049; F:tRNA binding; IEA:Ensembl. DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IDA:UniProtKB. DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome. 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; P54136; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative initiation; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; KW Direct protein sequencing; Disease variant; Leukodystrophy; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..660 FT /note="Arginine--tRNA ligase, cytoplasmic" FT /id="PRO_0000035797" 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:0000269|PubMed:24859084, FT ECO:0007744|PDB:4Q2T" FT BINDING 211 FT /ligand="L-arginine" FT /ligand_id="ChEBI:CHEBI:32682" FT /evidence="ECO:0000269|PubMed:24859084, FT ECO:0007744|PDB:4Q2T" FT BINDING 384 FT /ligand="L-arginine" FT /ligand_id="ChEBI:CHEBI:32682" FT /evidence="ECO:0000269|PubMed:24859084, FT ECO:0007744|PDB:4Q2T" FT BINDING 388 FT /ligand="L-arginine" FT /ligand_id="ChEBI:CHEBI:32682" FT /evidence="ECO:0000269|PubMed:24859084, FT ECO:0007744|PDB:4Q2T" FT BINDING 412 FT /ligand="L-arginine" FT /ligand_id="ChEBI:CHEBI:32682" FT /evidence="ECO:0000269|PubMed:24859084, FT ECO:0007744|PDB:4Q2T" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT VAR_SEQ 1..72 FT /note="Missing (in isoform Monomeric)" FT /evidence="ECO:0000305" FT /id="VSP_018905" FT VARIANT 2 FT /note="D -> G (in HLD9; dbSNP:rs672601372)" FT /evidence="ECO:0000269|PubMed:24777941" FT /id="VAR_072666" FT VARIANT 3 FT /note="V -> I (in dbSNP:rs244903)" FT /id="VAR_020106" FT VARIANT 135 FT /note="R -> G (in dbSNP:rs1059443)" FT /id="VAR_052635" FT VARIANT 397 FT /note="F -> Y (in dbSNP:rs2305734)" FT /id="VAR_020107" FT VARIANT 512 FT /note="R -> Q (in HLD9; dbSNP:rs369398935)" FT /evidence="ECO:0000269|PubMed:24777941" FT /id="VAR_072667" FT CONFLICT 39 FT /note="P -> S (in Ref. 1; AAB35627)" FT /evidence="ECO:0000305" FT CONFLICT 130..131 FT /note="QK -> PE (in Ref. 1; AAB35627)" FT /evidence="ECO:0000305" FT CONFLICT 135..137 FT /note="REI -> GEF (in Ref. 1; AAB35627)" FT /evidence="ECO:0000305" FT CONFLICT 147..156 FT /note="DNECIEKVEI -> AMDVLKRVEF (in Ref. 1; AAB35627)" FT /evidence="ECO:0000305" FT CONFLICT 164 FT /note="V -> G (in Ref. 1; AAB35627)" FT /evidence="ECO:0000305" FT CONFLICT 278 FT /note="K -> N (in Ref. 3; BAG37326)" FT /evidence="ECO:0000305" FT CONFLICT 308..312 FT /note="WKLIC -> YLLMS (in Ref. 1; AAB35627)" FT /evidence="ECO:0000305" FT CONFLICT 341 FT /note="R -> G (in Ref. 4; BAD96517)" FT /evidence="ECO:0000305" FT CONFLICT 358 FT /note="D -> G (in Ref. 3; BAG37326)" FT /evidence="ECO:0000305" FT CONFLICT 487 FT /note="T -> A (in Ref. 4; BAD96517)" FT /evidence="ECO:0000305" FT CONFLICT 567 FT /note="D -> V (in Ref. 1; AAB35627)" FT /evidence="ECO:0000305" FT CONFLICT 635..640 FT /note="MLLCEA -> ILCET (in Ref. 1; AAB35627)" FT /evidence="ECO:0000305" FT CONFLICT 651 FT /note="I -> T (in Ref. 1; AAB35627)" FT /evidence="ECO:0000305" FT CONFLICT 657..660 FT /note="VQRM -> GPRV (in Ref. 1; AAB35627)" FT /evidence="ECO:0000305" FT HELIX 76..91 FT /evidence="ECO:0007829|PDB:4ZAJ" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:4ZAJ" FT STRAND 108..110 FT /evidence="ECO:0007829|PDB:4ZAJ" FT STRAND 112..115 FT /evidence="ECO:0007829|PDB:4ZAJ" FT HELIX 117..123 FT /evidence="ECO:0007829|PDB:4ZAJ" FT HELIX 134..143 FT /evidence="ECO:0007829|PDB:4ZAJ" FT STRAND 149..155 FT /evidence="ECO:0007829|PDB:4ZAJ" FT TURN 158..160 FT /evidence="ECO:0007829|PDB:4Q2T" FT STRAND 162..166 FT /evidence="ECO:0007829|PDB:4ZAJ" FT HELIX 168..181 FT /evidence="ECO:0007829|PDB:4ZAJ" FT STRAND 193..197 FT /evidence="ECO:0007829|PDB:4ZAJ" FT HELIX 209..227 FT /evidence="ECO:0007829|PDB:4ZAJ" FT STRAND 231..236 FT /evidence="ECO:0007829|PDB:4ZAJ" FT STRAND 241..243 FT /evidence="ECO:0007829|PDB:4Q2T" FT HELIX 244..255 FT /evidence="ECO:0007829|PDB:4ZAJ" FT HELIX 257..260 FT /evidence="ECO:0007829|PDB:4ZAJ" FT HELIX 269..282 FT /evidence="ECO:0007829|PDB:4ZAJ" FT HELIX 285..298 FT /evidence="ECO:0007829|PDB:4ZAJ" FT TURN 302..304 FT /evidence="ECO:0007829|PDB:4ZAJ" FT HELIX 305..325 FT /evidence="ECO:0007829|PDB:4ZAJ" FT HELIX 335..341 FT /evidence="ECO:0007829|PDB:4ZAJ" FT HELIX 342..351 FT /evidence="ECO:0007829|PDB:4ZAJ" FT STRAND 355..358 FT /evidence="ECO:0007829|PDB:4ZAJ" FT STRAND 361..364 FT /evidence="ECO:0007829|PDB:4ZAJ" FT STRAND 373..376 FT /evidence="ECO:0007829|PDB:4ZAJ" FT HELIX 384..397 FT /evidence="ECO:0007829|PDB:4ZAJ" FT STRAND 402..409 FT /evidence="ECO:0007829|PDB:4ZAJ" FT HELIX 410..412 FT /evidence="ECO:0007829|PDB:4ZAJ" FT HELIX 413..425 FT /evidence="ECO:0007829|PDB:4ZAJ" FT TURN 431..433 FT /evidence="ECO:0007829|PDB:4ZAJ" FT STRAND 434..441 FT /evidence="ECO:0007829|PDB:4ZAJ" FT STRAND 449..451 FT /evidence="ECO:0007829|PDB:4ZAJ" FT STRAND 455..458 FT /evidence="ECO:0007829|PDB:4ZAJ" FT HELIX 462..478 FT /evidence="ECO:0007829|PDB:4ZAJ" FT STRAND 482..485 FT /evidence="ECO:0007829|PDB:4ZAJ" FT HELIX 487..490 FT /evidence="ECO:0007829|PDB:4ZAJ" FT HELIX 493..508 FT /evidence="ECO:0007829|PDB:4ZAJ" FT STRAND 512..514 FT /evidence="ECO:0007829|PDB:4Q2X" FT HELIX 520..523 FT /evidence="ECO:0007829|PDB:4ZAJ" FT STRAND 526..530 FT /evidence="ECO:0007829|PDB:4ZAJ" FT HELIX 531..546 FT /evidence="ECO:0007829|PDB:4ZAJ" FT TURN 547..549 FT /evidence="ECO:0007829|PDB:4ZAJ" FT HELIX 552..561 FT /evidence="ECO:0007829|PDB:4ZAJ" FT HELIX 569..578 FT /evidence="ECO:0007829|PDB:4ZAJ" FT HELIX 581..591 FT /evidence="ECO:0007829|PDB:4ZAJ" FT HELIX 595..614 FT /evidence="ECO:0007829|PDB:4ZAJ" FT STRAND 617..620 FT /evidence="ECO:0007829|PDB:4ZAJ" FT TURN 622..624 FT /evidence="ECO:0007829|PDB:4ZAJ" FT STRAND 627..630 FT /evidence="ECO:0007829|PDB:4ZAJ" FT HELIX 632..652 FT /evidence="ECO:0007829|PDB:4ZAJ" SQ SEQUENCE 660 AA; 75379 MW; FE9FB5C910709956 CRC64; MDVLVSECSA RLLQQEEEIK SLTAEIDRLK NCGCLGASPN LEQLQEENLK LKYRLNILRK SLQAERNKPT KNMINIISRL QEVFGHAIKA AYPDLENPPL LVTPSQQAKF GDYQCNSAMG ISQMLKTKEQ KVNPREIAEN ITKHLPDNEC IEKVEIAGPG FINVHLRKDF VSEQLTSLLV NGVQLPALGE NKKVIVDFSS PNIAKEMHVG HLRSTIIGES ISRLFEFAGY DVLRLNHVGD WGTQFGMLIA HLQDKFPDYL TVSPPIGDLQ VFYKESKKRF DTEEEFKKRA YQCVVLLQGK NPDITKAWKL ICDVSRQELN KIYDALDVSL IERGESFYQD RMNDIVKEFE DRGFVQVDDG RKIVFVPGCS IPLTIVKSDG GYTYDTSDLA AIKQRLFEEK ADMIIYVVDN GQSVHFQTIF AAAQMIGWYD PKVTRVFHAG FGVVLGEDKK KFKTRSGETV RLMDLLGEGL KRSMDKLKEK ERDKVLTAEE LNAAQTSVAY GCIKYADLSH NRLNDYIFSF DKMLDDRGNT AAYLLYAFTR IRSIARLANI DEEMLQKAAR ETKILLDHEK EWKLGRCILR FPEILQKILD DLFLHTLCDY IYELATAFTE FYDSCYCVEK DRQTGKILKV NMWRMLLCEA VAAVMAKGFD ILGIKPVQRM //