SYRC_HUMAN
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 03-AUG-2022, entry version 214.
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}.
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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; 235.
DR CORUM; P54136; -.
DR IntAct; P54136; 60.
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; P54136; -.
DR PeptideAtlas; P54136; -.
DR PRIDE; P54136; -.
DR ProteomicsDB; 56650; -. [P54136-1]
DR ProteomicsDB; 56651; -. [P54136-2]
DR ABCD; P54136; 1 sequenced antibody.
DR Antibodypedia; 1285; 247 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 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; NKPLHLG; -.
DR OrthoDB; 463402at2759; -.
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 BioGRID-ORCS; 5917; 621 hits in 1052 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 152 other tissues.
DR ExpressionAtlas; P54136; baseline and differential.
DR Genevisible; P54136; HS.
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:UniProtKB.
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; -; 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 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
