Full text data of RARS
RARS
[Confidence: low (only semi-automatic identification from reviews)]
Arginine--tRNA ligase, cytoplasmic; 6.1.1.19 (Arginyl-tRNA synthetase; ArgRS)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Arginine--tRNA ligase, cytoplasmic; 6.1.1.19 (Arginyl-tRNA synthetase; ArgRS)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P54136
ID SYRC_HUMAN Reviewed; 660 AA.
AC P54136; B2RBS9; Q53GY4; Q9BWA1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-APR-2002, sequence version 2.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=Arginine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.19;
DE AltName: Full=Arginyl-tRNA synthetase;
DE Short=ArgRS;
GN Name=RARS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT project: 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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric 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
RT of tRNA synthetase.";
RL J. Biol. Chem. 274:16673-16676(1999).
RN [8]
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND INTERACTION
RP 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
RT synthetase is indispensable in its interaction with arginyl-tRNA
RT synthetase in the multi-tRNA synthetase complex.";
RL J. Biol. Chem. 280:34755-34763(2005).
RN [9]
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
RT two translation initiations by a single mRNA.";
RL Biochemistry 45:1338-1344(2006).
RN [10]
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.,
RA Zatelli M.C., Uberti E.C.;
RT "Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer
RT cell lines.";
RL J. Cell. Physiol. 212:293-297(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
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.,
RA Walther T.C., 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 [13]
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.,
RA Buerckstuemmer T., 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Forms part of a macromolecular complex that catalyzes
CC the attachment of specific amino acids to cognate tRNAs during
CC protein synthesis. Modulates the secretion of AIMP1 and may be
CC involved in generation of the inflammatory cytokine EMAP2 from
CC AIMP1.
CC -!- CATALYTIC ACTIVITY: ATP + L-arginine + tRNA(Arg) = AMP +
CC diphosphate + L-arginyl-tRNA(Arg).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.9 uM for arginine (ATP-PPi exchange at 37 degrees Celsius);
CC KM=3.5 uM for arginine (arginylation at 37 degrees Celsius);
CC KM=1183 uM for ATP (ATP-PPi exchange at 37 Celsius);
CC KM=910 uM for ATP (arginylation at 37 Celsius);
CC KM=0.05 uM for calf liver tRNA-Arg (ATP-PPi exchange at 37
CC Celsius);
CC KM=0.41 uM for calf liver tRNA-Arg (arginylation at 37 Celsius);
CC -!- SUBUNIT: Interacts (via N-terminus) with AIMP1 (via N-terminus);
CC this stimulates its catalytic activity. Interacts (via N-terminus)
CC with LARS2 (via C-terminus). Monomer; also part of a multisubunit
CC complex that groups tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu,
CC Lys, Met and Pro.
CC -!- INTERACTION:
CC Q9P2J5:LARS; NbExp=3; IntAct=EBI-355482, EBI-356077;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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 N-terminus (AA 1-72) has two regions predicted to be
CC alpha-helical that might be involved in the multisynthetase
CC complex assembly.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC family.
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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 PIR; JC4365; JC4365.
DR RefSeq; NP_002878.2; NM_002887.3.
DR UniGene; Hs.654907; -.
DR ProteinModelPortal; P54136; -.
DR SMR; P54136; 72-660.
DR IntAct; P54136; 8.
DR MINT; MINT-5006018; -.
DR STRING; 9606.ENSP00000231572; -.
DR BindingDB; P54136; -.
DR ChEMBL; CHEMBL2824; -.
DR PhosphoSite; P54136; -.
DR DMDM; 20178331; -.
DR PaxDb; P54136; -.
DR PeptideAtlas; P54136; -.
DR PRIDE; P54136; -.
DR DNASU; 5917; -.
DR Ensembl; ENST00000231572; ENSP00000231572; ENSG00000113643.
DR GeneID; 5917; -.
DR KEGG; hsa:5917; -.
DR UCSC; uc003lzx.3; human.
DR CTD; 5917; -.
DR GeneCards; GC05P167846; -.
DR HGNC; HGNC:9870; RARS.
DR HPA; HPA003979; -.
DR HPA; HPA004130; -.
DR MIM; 107820; gene.
DR neXtProt; NX_P54136; -.
DR PharmGKB; PA34231; -.
DR eggNOG; COG0018; -.
DR HOGENOM; HOG000247212; -.
DR HOVERGEN; HBG029238; -.
DR InParanoid; P54136; -.
DR KO; K01887; -.
DR OMA; PDITKAW; -.
DR OrthoDB; EOG764725; -.
DR PhylomeDB; P54136; -.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; RARS_(gene); -.
DR GenomeRNAi; 5917; -.
DR NextBio; 23038; -.
DR PRO; PR:P54136; -.
DR ArrayExpress; P54136; -.
DR Bgee; P54136; -.
DR CleanEx; HS_RARS; -.
DR Genevestigator; P54136; -.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0034618; F:arginine binding; IEA:Ensembl.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:Ensembl.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; TAS:ProtInc.
DR Gene3D; 3.30.1360.70; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR001278; Arg-tRNA-ligase_Ia.
DR InterPro; IPR015945; Arg-tRNA-synth_Ia_core.
DR InterPro; IPR005148; Arg-tRNA-synth_N.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_1a_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; Alternative initiation; Aminoacyl-tRNA synthetase;
KW ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Ligase; Nucleotide-binding; Polymorphism; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1 660 Arginine--tRNA ligase, cytoplasmic.
FT /FTId=PRO_0000035797.
FT REGION 1 72 Could be involved in the assembly of the
FT multisynthetase complex.
FT MOTIF 201 212 "HIGH" region.
FT MOD_RES 1 1 N-acetylmethionine.
FT VAR_SEQ 1 72 Missing (in isoform Monomeric).
FT /FTId=VSP_018905.
FT VARIANT 3 3 V -> I (in dbSNP:rs244903).
FT /FTId=VAR_020106.
FT VARIANT 135 135 R -> G (in dbSNP:rs1059443).
FT /FTId=VAR_052635.
FT VARIANT 397 397 F -> Y (in dbSNP:rs2305734).
FT /FTId=VAR_020107.
FT CONFLICT 39 39 P -> S (in Ref. 1; AAB35627).
FT CONFLICT 130 131 QK -> PE (in Ref. 1; AAB35627).
FT CONFLICT 135 137 REI -> GEF (in Ref. 1; AAB35627).
FT CONFLICT 147 156 DNECIEKVEI -> AMDVLKRVEF (in Ref. 1;
FT AAB35627).
FT CONFLICT 164 164 V -> G (in Ref. 1; AAB35627).
FT CONFLICT 278 278 K -> N (in Ref. 3; BAG37326).
FT CONFLICT 308 312 WKLIC -> YLLMS (in Ref. 1; AAB35627).
FT CONFLICT 341 341 R -> G (in Ref. 4; BAD96517).
FT CONFLICT 358 358 D -> G (in Ref. 3; BAG37326).
FT CONFLICT 487 487 T -> A (in Ref. 4; BAD96517).
FT CONFLICT 567 567 D -> V (in Ref. 1; AAB35627).
FT CONFLICT 635 640 MLLCEA -> ILCET (in Ref. 1; AAB35627).
FT CONFLICT 651 651 I -> T (in Ref. 1; AAB35627).
FT CONFLICT 657 660 VQRM -> GPRV (in Ref. 1; AAB35627).
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
//
ID SYRC_HUMAN Reviewed; 660 AA.
AC P54136; B2RBS9; Q53GY4; Q9BWA1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-APR-2002, sequence version 2.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=Arginine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.19;
DE AltName: Full=Arginyl-tRNA synthetase;
DE Short=ArgRS;
GN Name=RARS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT project: 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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric 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
RT of tRNA synthetase.";
RL J. Biol. Chem. 274:16673-16676(1999).
RN [8]
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND INTERACTION
RP 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
RT synthetase is indispensable in its interaction with arginyl-tRNA
RT synthetase in the multi-tRNA synthetase complex.";
RL J. Biol. Chem. 280:34755-34763(2005).
RN [9]
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
RT two translation initiations by a single mRNA.";
RL Biochemistry 45:1338-1344(2006).
RN [10]
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.,
RA Zatelli M.C., Uberti E.C.;
RT "Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer
RT cell lines.";
RL J. Cell. Physiol. 212:293-297(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
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.,
RA Walther T.C., 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 [13]
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.,
RA Buerckstuemmer T., 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Forms part of a macromolecular complex that catalyzes
CC the attachment of specific amino acids to cognate tRNAs during
CC protein synthesis. Modulates the secretion of AIMP1 and may be
CC involved in generation of the inflammatory cytokine EMAP2 from
CC AIMP1.
CC -!- CATALYTIC ACTIVITY: ATP + L-arginine + tRNA(Arg) = AMP +
CC diphosphate + L-arginyl-tRNA(Arg).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.9 uM for arginine (ATP-PPi exchange at 37 degrees Celsius);
CC KM=3.5 uM for arginine (arginylation at 37 degrees Celsius);
CC KM=1183 uM for ATP (ATP-PPi exchange at 37 Celsius);
CC KM=910 uM for ATP (arginylation at 37 Celsius);
CC KM=0.05 uM for calf liver tRNA-Arg (ATP-PPi exchange at 37
CC Celsius);
CC KM=0.41 uM for calf liver tRNA-Arg (arginylation at 37 Celsius);
CC -!- SUBUNIT: Interacts (via N-terminus) with AIMP1 (via N-terminus);
CC this stimulates its catalytic activity. Interacts (via N-terminus)
CC with LARS2 (via C-terminus). Monomer; also part of a multisubunit
CC complex that groups tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu,
CC Lys, Met and Pro.
CC -!- INTERACTION:
CC Q9P2J5:LARS; NbExp=3; IntAct=EBI-355482, EBI-356077;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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 N-terminus (AA 1-72) has two regions predicted to be
CC alpha-helical that might be involved in the multisynthetase
CC complex assembly.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC family.
CC -----------------------------------------------------------------------
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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 PIR; JC4365; JC4365.
DR RefSeq; NP_002878.2; NM_002887.3.
DR UniGene; Hs.654907; -.
DR ProteinModelPortal; P54136; -.
DR SMR; P54136; 72-660.
DR IntAct; P54136; 8.
DR MINT; MINT-5006018; -.
DR STRING; 9606.ENSP00000231572; -.
DR BindingDB; P54136; -.
DR ChEMBL; CHEMBL2824; -.
DR PhosphoSite; P54136; -.
DR DMDM; 20178331; -.
DR PaxDb; P54136; -.
DR PeptideAtlas; P54136; -.
DR PRIDE; P54136; -.
DR DNASU; 5917; -.
DR Ensembl; ENST00000231572; ENSP00000231572; ENSG00000113643.
DR GeneID; 5917; -.
DR KEGG; hsa:5917; -.
DR UCSC; uc003lzx.3; human.
DR CTD; 5917; -.
DR GeneCards; GC05P167846; -.
DR HGNC; HGNC:9870; RARS.
DR HPA; HPA003979; -.
DR HPA; HPA004130; -.
DR MIM; 107820; gene.
DR neXtProt; NX_P54136; -.
DR PharmGKB; PA34231; -.
DR eggNOG; COG0018; -.
DR HOGENOM; HOG000247212; -.
DR HOVERGEN; HBG029238; -.
DR InParanoid; P54136; -.
DR KO; K01887; -.
DR OMA; PDITKAW; -.
DR OrthoDB; EOG764725; -.
DR PhylomeDB; P54136; -.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; RARS_(gene); -.
DR GenomeRNAi; 5917; -.
DR NextBio; 23038; -.
DR PRO; PR:P54136; -.
DR ArrayExpress; P54136; -.
DR Bgee; P54136; -.
DR CleanEx; HS_RARS; -.
DR Genevestigator; P54136; -.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0034618; F:arginine binding; IEA:Ensembl.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:Ensembl.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; TAS:ProtInc.
DR Gene3D; 3.30.1360.70; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR001278; Arg-tRNA-ligase_Ia.
DR InterPro; IPR015945; Arg-tRNA-synth_Ia_core.
DR InterPro; IPR005148; Arg-tRNA-synth_N.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_1a_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; Alternative initiation; Aminoacyl-tRNA synthetase;
KW ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Ligase; Nucleotide-binding; Polymorphism; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1 660 Arginine--tRNA ligase, cytoplasmic.
FT /FTId=PRO_0000035797.
FT REGION 1 72 Could be involved in the assembly of the
FT multisynthetase complex.
FT MOTIF 201 212 "HIGH" region.
FT MOD_RES 1 1 N-acetylmethionine.
FT VAR_SEQ 1 72 Missing (in isoform Monomeric).
FT /FTId=VSP_018905.
FT VARIANT 3 3 V -> I (in dbSNP:rs244903).
FT /FTId=VAR_020106.
FT VARIANT 135 135 R -> G (in dbSNP:rs1059443).
FT /FTId=VAR_052635.
FT VARIANT 397 397 F -> Y (in dbSNP:rs2305734).
FT /FTId=VAR_020107.
FT CONFLICT 39 39 P -> S (in Ref. 1; AAB35627).
FT CONFLICT 130 131 QK -> PE (in Ref. 1; AAB35627).
FT CONFLICT 135 137 REI -> GEF (in Ref. 1; AAB35627).
FT CONFLICT 147 156 DNECIEKVEI -> AMDVLKRVEF (in Ref. 1;
FT AAB35627).
FT CONFLICT 164 164 V -> G (in Ref. 1; AAB35627).
FT CONFLICT 278 278 K -> N (in Ref. 3; BAG37326).
FT CONFLICT 308 312 WKLIC -> YLLMS (in Ref. 1; AAB35627).
FT CONFLICT 341 341 R -> G (in Ref. 4; BAD96517).
FT CONFLICT 358 358 D -> G (in Ref. 3; BAG37326).
FT CONFLICT 487 487 T -> A (in Ref. 4; BAD96517).
FT CONFLICT 567 567 D -> V (in Ref. 1; AAB35627).
FT CONFLICT 635 640 MLLCEA -> ILCET (in Ref. 1; AAB35627).
FT CONFLICT 651 651 I -> T (in Ref. 1; AAB35627).
FT CONFLICT 657 660 VQRM -> GPRV (in Ref. 1; AAB35627).
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
//
MIM
107820
*RECORD*
*FIELD* NO
107820
*FIELD* TI
*107820 ARGINYL-tRNA SYNTHETASE 1; RARS1
;;ARGINYL-tRNA SYNTHETASE, CYTOPLASMIC;;
RARS
read more*FIELD* TX
CLONING
Girjes et al. (1995) isolated a full-length cDNA corresponding to the
RARS gene and identified an open reading frame of 1983 nucleotides with
87% homology to other mammalian RARS. Northern blot analysis revealed
the presence of a single mRNA species of approximately 2.2 kb.
GENE FUNCTION
Using forward genetic screens in Caenorhabditis elegans, Anderson et al.
(2009) isolated a hypoxia-resistant reduction-of-function mutant of rrt1
(whose human homolog is RARS1), which encodes an arginyl-transfer RNA
synthetase, an enzyme essential for protein translation. Knockdown of
rrt1, and of most other genes encoding aminoacyl-tRNA synthetases,
rescued animals from hypoxia-induced death, and the level of hypoxia
resistance was inversely correlated with translation rate. The unfolded
protein response was induced by hypoxia and was required for the hypoxia
resistance of the reduction-of-function mutant of rrt1. Thus, Anderson
et al. (2009) concluded that translational suppression produces hypoxia
resistance, in part by reducing unfolding protein toxicity.
MAPPING
Arfin et al. (1985) assigned the gene for arginyl-tRNA synthetase to
chromosome 5 by study of somatic cell hybrids. Of the 7 aminoacyl-tRNA
synthetase genes mapped to that time, 4 were on chromosome 5, which
represents only about 7% of the total human genome.
*FIELD* SA
Carlock et al. (1985)
*FIELD* RF
1. Anderson, L. L.; Mao, X.; Scott, B. A.; Crowder, C. M.: Survival
from hypoxia in C. elegans by inactivation of aminoacyl-tRNA synthetases. Science 323:
630-633, 2009.
2. Arfin, S.; Carlock, L.; Gerken, S.; Wasmuth, J.: Clustering of
genes encoding aminoacyl-tRNA synthetases on human chromosome 5. (Abstract) Am.
J. Hum. Genet. 37: A228, 1985.
3. Carlock, L. R.; Skarecky, D.; Dana, S. L.; Wasmuth, J. J.: Deletion
mapping of human chromosome 5 using chromosome-specific DNA probes. Am.
J. Hum. Genet. 37: 839-852, 1985.
4. Girjes, A. A.; Hobson, K.; Chen, P.; Lavin, M. F.: Cloning and
characterization of cDNA encoding a human arginyl-tRNA synthetase. Gene 164:
347-350, 1995.
*FIELD* CN
Ada Hamosh - updated: 3/10/2009
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
alopez: 03/12/2009
terry: 3/10/2009
alopez: 10/11/2007
mark: 3/11/1996
terry: 2/28/1996
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/26/1989
marie: 3/25/1988
marie: 12/15/1986
reenie: 6/4/1986
*RECORD*
*FIELD* NO
107820
*FIELD* TI
*107820 ARGINYL-tRNA SYNTHETASE 1; RARS1
;;ARGINYL-tRNA SYNTHETASE, CYTOPLASMIC;;
RARS
read more*FIELD* TX
CLONING
Girjes et al. (1995) isolated a full-length cDNA corresponding to the
RARS gene and identified an open reading frame of 1983 nucleotides with
87% homology to other mammalian RARS. Northern blot analysis revealed
the presence of a single mRNA species of approximately 2.2 kb.
GENE FUNCTION
Using forward genetic screens in Caenorhabditis elegans, Anderson et al.
(2009) isolated a hypoxia-resistant reduction-of-function mutant of rrt1
(whose human homolog is RARS1), which encodes an arginyl-transfer RNA
synthetase, an enzyme essential for protein translation. Knockdown of
rrt1, and of most other genes encoding aminoacyl-tRNA synthetases,
rescued animals from hypoxia-induced death, and the level of hypoxia
resistance was inversely correlated with translation rate. The unfolded
protein response was induced by hypoxia and was required for the hypoxia
resistance of the reduction-of-function mutant of rrt1. Thus, Anderson
et al. (2009) concluded that translational suppression produces hypoxia
resistance, in part by reducing unfolding protein toxicity.
MAPPING
Arfin et al. (1985) assigned the gene for arginyl-tRNA synthetase to
chromosome 5 by study of somatic cell hybrids. Of the 7 aminoacyl-tRNA
synthetase genes mapped to that time, 4 were on chromosome 5, which
represents only about 7% of the total human genome.
*FIELD* SA
Carlock et al. (1985)
*FIELD* RF
1. Anderson, L. L.; Mao, X.; Scott, B. A.; Crowder, C. M.: Survival
from hypoxia in C. elegans by inactivation of aminoacyl-tRNA synthetases. Science 323:
630-633, 2009.
2. Arfin, S.; Carlock, L.; Gerken, S.; Wasmuth, J.: Clustering of
genes encoding aminoacyl-tRNA synthetases on human chromosome 5. (Abstract) Am.
J. Hum. Genet. 37: A228, 1985.
3. Carlock, L. R.; Skarecky, D.; Dana, S. L.; Wasmuth, J. J.: Deletion
mapping of human chromosome 5 using chromosome-specific DNA probes. Am.
J. Hum. Genet. 37: 839-852, 1985.
4. Girjes, A. A.; Hobson, K.; Chen, P.; Lavin, M. F.: Cloning and
characterization of cDNA encoding a human arginyl-tRNA synthetase. Gene 164:
347-350, 1995.
*FIELD* CN
Ada Hamosh - updated: 3/10/2009
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
alopez: 03/12/2009
terry: 3/10/2009
alopez: 10/11/2007
mark: 3/11/1996
terry: 2/28/1996
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/26/1989
marie: 3/25/1988
marie: 12/15/1986
reenie: 6/4/1986