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Q9D0I9

- SYRC_MOUSE

UniProt

Q9D0I9 - SYRC_MOUSE

Protein

Arginine--tRNA ligase, cytoplasmic

Gene

Rars

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (16 Apr 2002)
      Previous versions | rss
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    Functioni

    Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1 By similarity.By similarity

    Catalytic activityi

    ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).

    GO - Molecular functioni

    1. arginine binding Source: Ensembl
    2. arginine-tRNA ligase activity Source: UniProtKB-EC
    3. ATP binding Source: UniProtKB-KW
    4. tRNA binding Source: Ensembl

    GO - Biological processi

    1. arginyl-tRNA aminoacylation Source: Ensembl

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arginine--tRNA ligase, cytoplasmic (EC:6.1.1.19)
    Alternative name(s):
    Arginyl-tRNA synthetase
    Short name:
    ArgRS
    Gene namesi
    Name:Rars
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1914297. Rars.

    Subcellular locationi

    GO - Cellular componenti

    1. aminoacyl-tRNA synthetase multienzyme complex Source: Ensembl
    2. mitochondrion Source: MGI
    3. nucleus Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 660660Arginine--tRNA ligase, cytoplasmicPRO_0000151659Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9D0I9.
    PaxDbiQ9D0I9.
    PRIDEiQ9D0I9.

    PTM databases

    PhosphoSiteiQ9D0I9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9D0I9.
    BgeeiQ9D0I9.
    CleanExiMM_RARS.
    GenevestigatoriQ9D0I9.

    Interactioni

    Subunit structurei

    Interacts (via N-terminus) with AIMP1 (via N-terminus); this stimulates its catalytic activity. Interacts (via N-terminus) with LARS2 (via C-terminus). Monomer; also part of a multisubunit complex that groups tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu, Lys, Met and Pro By similarity. Interacts with QARS By similarity.By similarity

    Protein-protein interaction databases

    BioGridi222643. 7 interactions.
    IntActiQ9D0I9. 4 interactions.
    MINTiMINT-1869825.
    STRINGi10090.ENSMUSP00000018992.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D0I9.
    SMRiQ9D0I9. Positions 57-660.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 7272Could be involved in the assembly of the multisynthetase complexAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi201 – 21212"HIGH" regionAdd
    BLAST

    Domaini

    The N-terminus (AA 1-72) has two regions predicted to be alpha-helical that might be involved in the multisynthetase complex assembly.

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0018.
    GeneTreeiENSGT00530000063407.
    HOVERGENiHBG029238.
    InParanoidiQ3U8R2.
    KOiK01887.
    OMAiKCFDILG.
    OrthoDBiEOG764725.
    PhylomeDBiQ9D0I9.
    TreeFamiTF106111.

    Family and domain databases

    Gene3Di1.10.730.10. 1 hit.
    3.30.1360.70. 1 hit.
    3.40.50.620. 1 hit.
    HAMAPiMF_00123. Arg_tRNA_synth.
    InterProiIPR001412. aa-tRNA-synth_I_CS.
    IPR001278. Arg-tRNA-ligase.
    IPR005148. Arg-tRNA-synth_N.
    IPR008909. DALR_anticod-bd.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009080. tRNAsynth_1a_anticodon-bd.
    [Graphical view]
    PANTHERiPTHR11956. PTHR11956. 1 hit.
    PfamiPF03485. Arg_tRNA_synt_N. 1 hit.
    PF05746. DALR_1. 1 hit.
    PF00750. tRNA-synt_1d. 1 hit.
    [Graphical view]
    PRINTSiPR01038. TRNASYNTHARG.
    SMARTiSM01016. Arg_tRNA_synt_N. 1 hit.
    SM00836. DALR_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF47323. SSF47323. 1 hit.
    SSF55190. SSF55190. 1 hit.
    TIGRFAMsiTIGR00456. argS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9D0I9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDGLVAQCSA RLLQQEREIK ALTAEIDRLK NCGCLEASPS LEQLREENLK    50
    LKYRLNILRR SLQEERRKPT KNMININSRL QEVFGCAIRA AYPDLENPPL 100
    IVTPSQQPKF GDYQCNSAMG ISQMLKAKEQ KVSPREIAEN ITKHLPNNKY 150
    IDKVEIAGPG FINVHLRKDF VSEQLTSLLV NGVQLPVLGD KEKVIVDFSS 200
    PNIAKEMHVG HLRSTIIGES MSRLFEFAGY DVLRLNHVGD WGTQFGMLIA 250
    HLQDKFPDYL TVSPPIGDLQ AFYKESKKRF DADEEFKKRA YQCVVLLQSK 300
    NPDIMKAWNL ICDVSREEFK KIYDALDITL IERGESFYQD RMKDIVKEFE 350
    DKGFVQVDDG RKIVFVPGCS VPLTIVKSDG GYTYDTSDLA AIKQRLFEEK 400
    ANKIIYVVDN GQAIHFQTIF AAAQMIGWYD PKVTLVTHVG FGVVLGEDKK 450
    KFKTRSGETV RLMDLLEEGL KRSMDKLKEK ERDKVLTEEE LKAAQTSVAY 500
    GCIKYADLSH NRLNDYIFSF DKMLDDRGNT AAYLLYAFTR IRSIARLANI 550
    DEAMLQRAAR ETKIILDHEK EWKLGRCILR FPEILQKILD DLFLHTLCDY 600
    IYELATTFTE FYDSCYCVEK DRQTGKVLKV NMWRMLLCEA VAAVMAKGFD 650
    ILGIKPVQRM 660
    Length:660
    Mass (Da):75,674
    Last modified:April 16, 2002 - v2
    Checksum:i6E8EBCC590FAB81D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51V → M in BAE30955. (PubMed:16141072)Curated
    Sequence conflicti178 – 1781L → H in BAB27583. (PubMed:16141072)Curated
    Sequence conflicti184 – 1841Q → E in BAE40154. (PubMed:16141072)Curated
    Sequence conflicti210 – 2101G → V in BAB27583. (PubMed:16141072)Curated
    Sequence conflicti252 – 2521L → M in BAE38569. (PubMed:16141072)Curated
    Sequence conflicti281 – 2811D → G in BAE40154. (PubMed:16141072)Curated
    Sequence conflicti288 – 2881K → E in BAE40154. (PubMed:16141072)Curated
    Sequence conflicti418 – 4181T → I in BAE40154. (PubMed:16141072)Curated
    Sequence conflicti474 – 4741M → L in BAB27583. (PubMed:16141072)Curated
    Sequence conflicti591 – 5911D → N in BAE38569. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK011383 mRNA. Translation: BAB27583.1.
    AK076160 mRNA. Translation: BAC36226.1.
    AK149856 mRNA. Translation: BAE29127.1.
    AK151966 mRNA. Translation: BAE30837.1.
    AK152108 mRNA. Translation: BAE30955.1.
    AK166097 mRNA. Translation: BAE38569.1.
    AK168194 mRNA. Translation: BAE40154.1.
    AL596084 Genomic DNA. Translation: CAI24388.1.
    CH466658 Genomic DNA. Translation: EDL16275.1.
    BC020132 mRNA. Translation: AAH20132.1.
    CCDSiCCDS24544.1.
    RefSeqiNP_080212.2. NM_025936.3.
    UniGeneiMm.284906.

    Genome annotation databases

    EnsembliENSMUST00000018992; ENSMUSP00000018992; ENSMUSG00000018848.
    GeneIDi104458.
    KEGGimmu:104458.
    UCSCiuc007ilh.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK011383 mRNA. Translation: BAB27583.1 .
    AK076160 mRNA. Translation: BAC36226.1 .
    AK149856 mRNA. Translation: BAE29127.1 .
    AK151966 mRNA. Translation: BAE30837.1 .
    AK152108 mRNA. Translation: BAE30955.1 .
    AK166097 mRNA. Translation: BAE38569.1 .
    AK168194 mRNA. Translation: BAE40154.1 .
    AL596084 Genomic DNA. Translation: CAI24388.1 .
    CH466658 Genomic DNA. Translation: EDL16275.1 .
    BC020132 mRNA. Translation: AAH20132.1 .
    CCDSi CCDS24544.1.
    RefSeqi NP_080212.2. NM_025936.3.
    UniGenei Mm.284906.

    3D structure databases

    ProteinModelPortali Q9D0I9.
    SMRi Q9D0I9. Positions 57-660.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 222643. 7 interactions.
    IntActi Q9D0I9. 4 interactions.
    MINTi MINT-1869825.
    STRINGi 10090.ENSMUSP00000018992.

    PTM databases

    PhosphoSitei Q9D0I9.

    Proteomic databases

    MaxQBi Q9D0I9.
    PaxDbi Q9D0I9.
    PRIDEi Q9D0I9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000018992 ; ENSMUSP00000018992 ; ENSMUSG00000018848 .
    GeneIDi 104458.
    KEGGi mmu:104458.
    UCSCi uc007ilh.2. mouse.

    Organism-specific databases

    CTDi 5917.
    MGIi MGI:1914297. Rars.

    Phylogenomic databases

    eggNOGi COG0018.
    GeneTreei ENSGT00530000063407.
    HOVERGENi HBG029238.
    InParanoidi Q3U8R2.
    KOi K01887.
    OMAi KCFDILG.
    OrthoDBi EOG764725.
    PhylomeDBi Q9D0I9.
    TreeFami TF106111.

    Miscellaneous databases

    NextBioi 357144.
    PROi Q9D0I9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9D0I9.
    Bgeei Q9D0I9.
    CleanExi MM_RARS.
    Genevestigatori Q9D0I9.

    Family and domain databases

    Gene3Di 1.10.730.10. 1 hit.
    3.30.1360.70. 1 hit.
    3.40.50.620. 1 hit.
    HAMAPi MF_00123. Arg_tRNA_synth.
    InterProi IPR001412. aa-tRNA-synth_I_CS.
    IPR001278. Arg-tRNA-ligase.
    IPR005148. Arg-tRNA-synth_N.
    IPR008909. DALR_anticod-bd.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009080. tRNAsynth_1a_anticodon-bd.
    [Graphical view ]
    PANTHERi PTHR11956. PTHR11956. 1 hit.
    Pfami PF03485. Arg_tRNA_synt_N. 1 hit.
    PF05746. DALR_1. 1 hit.
    PF00750. tRNA-synt_1d. 1 hit.
    [Graphical view ]
    PRINTSi PR01038. TRNASYNTHARG.
    SMARTi SM01016. Arg_tRNA_synt_N. 1 hit.
    SM00836. DALR_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47323. SSF47323. 1 hit.
    SSF55190. SSF55190. 1 hit.
    TIGRFAMsi TIGR00456. argS. 1 hit.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Bone marrow macrophage, Embryo, Embryonic head and Lung.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Czech 2.
      Tissue: Mammary tumor.

    Entry informationi

    Entry nameiSYRC_MOUSE
    AccessioniPrimary (citable) accession number: Q9D0I9
    Secondary accession number(s): Q3THP2
    , Q3TM73, Q3U8R2, Q3U930, Q5SXA8, Q8VDW1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 16, 2002
    Last sequence update: April 16, 2002
    Last modified: October 1, 2014
    This is version 114 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3