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Q3U186

- SYRM_MOUSE

UniProt

Q3U186 - SYRM_MOUSE

Protein

Probable arginine--tRNA ligase, mitochondrial

Gene

Rars2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (11 Oct 2005)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. arginyl-tRNA aminoacylation Source: InterPro

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable arginine--tRNA ligase, mitochondrial (EC:6.1.1.19)
    Alternative name(s):
    Arginyl-tRNA synthetase
    Short name:
    ArgRS
    Gene namesi
    Name:Rars2
    Synonyms:Rarsl
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1923596. Rars2.

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1616MitochondrionSequence AnalysisAdd
    BLAST
    Chaini17 – 578562Probable arginine--tRNA ligase, mitochondrialPRO_0000250732Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei568 – 5681N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ3U186.
    PaxDbiQ3U186.
    PRIDEiQ3U186.

    PTM databases

    PhosphoSiteiQ3U186.

    Expressioni

    Gene expression databases

    ArrayExpressiQ3U186.
    BgeeiQ3U186.
    GenevestigatoriQ3U186.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3U186.
    SMRiQ3U186. Positions 3-578.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi133 – 14412"HIGH" regionAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0018.
    GeneTreeiENSGT00530000063407.
    HOGENOMiHOG000247211.
    HOVERGENiHBG057355.
    InParanoidiQ3U186.
    KOiK01887.
    OMAiELGDMQA.
    OrthoDBiEOG7DNNTT.
    PhylomeDBiQ3U186.
    TreeFamiTF300888.

    Family and domain databases

    Gene3Di1.10.730.10. 1 hit.
    3.30.1360.70. 1 hit.
    3.40.50.620. 1 hit.
    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.
    PfamiPF05746. DALR_1. 1 hit.
    PF00750. tRNA-synt_1d. 1 hit.
    [Graphical view]
    PRINTSiPR01038. TRNASYNTHARG.
    SMARTiSM00836. 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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q3U186-1 [UniParc]FASTAAdd to Basket

    « Hide

    MACGFRRSIA CQLSRVLALP PESLIKSISA VPVSKKEEVA DFQLSVDSLL    50
    EDNNHKSQVD TQDQARRLAE KLKCDTVVTA ISAGPRTLNF KINRELLTKA 100
    VLQQVTEDGC KYGLKSELFS DLPKKRIVVE FSSPNIAKKF HVGHLRSTII 150
    GNFIANLKEA LGHQVTRINY IGDWGMQFGL LGTGFQLFGY EEKLQTNPLQ 200
    HLFDVYVQVN KEATDDKNVT KLAHEFFHRL EMGDTQALSL WQRFRDLSIE 250
    EYTQIYKRLG IYFDEYSGES FYREKSQDVL KLLDSKGLLQ KTAEGNVVVD 300
    LSGTGDLSSV CTVMRSDGTS LYATRDLAAA IHRMDKYNFD TMIYVADKGQ 350
    RRHFQQVFQM LKIMGYDWAE RCQHVPFGIV KGMKTRRGGV TFLEDVLNEV 400
    QSRMLQNMAS IKTTKQLENP QETAERVGLA AVIIQDFRGT LLSDYQFSWD 450
    RVFQSRGDTG VFLQYTHARL CSLEETFGCG YLNDSNVACL QEPQSVSILQ 500
    HLLRFDEVLY LSSQDLQPKH IVSYLLTLSH LAAVAHKTLQ VKDSPPDVAG 550
    ARLHLFKAVR SVLANGMKLL GITPVCRM 578
    Length:578
    Mass (Da):65,336
    Last modified:October 11, 2005 - v1
    Checksum:i5255FAFA8F873C27
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti306 – 3061D → G in AAH24878. (PubMed:15489334)Curated
    Sequence conflicti540 – 5401Q → K in AAH24878. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK156182 mRNA. Translation: BAE33614.1.
    BC024878 mRNA. Translation: AAH24878.1.
    CCDSiCCDS18029.1.
    RefSeqiNP_852071.2. NM_181406.3.
    UniGeneiMm.22363.

    Genome annotation databases

    EnsembliENSMUST00000029968; ENSMUSP00000029968; ENSMUSG00000028292.
    GeneIDi109093.
    KEGGimmu:109093.
    UCSCiuc008sgf.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK156182 mRNA. Translation: BAE33614.1 .
    BC024878 mRNA. Translation: AAH24878.1 .
    CCDSi CCDS18029.1.
    RefSeqi NP_852071.2. NM_181406.3.
    UniGenei Mm.22363.

    3D structure databases

    ProteinModelPortali Q3U186.
    SMRi Q3U186. Positions 3-578.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q3U186.

    Proteomic databases

    MaxQBi Q3U186.
    PaxDbi Q3U186.
    PRIDEi Q3U186.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029968 ; ENSMUSP00000029968 ; ENSMUSG00000028292 .
    GeneIDi 109093.
    KEGGi mmu:109093.
    UCSCi uc008sgf.2. mouse.

    Organism-specific databases

    CTDi 57038.
    MGIi MGI:1923596. Rars2.

    Phylogenomic databases

    eggNOGi COG0018.
    GeneTreei ENSGT00530000063407.
    HOGENOMi HOG000247211.
    HOVERGENi HBG057355.
    InParanoidi Q3U186.
    KOi K01887.
    OMAi ELGDMQA.
    OrthoDBi EOG7DNNTT.
    PhylomeDBi Q3U186.
    TreeFami TF300888.

    Miscellaneous databases

    NextBioi 361640.
    PROi Q3U186.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q3U186.
    Bgeei Q3U186.
    Genevestigatori Q3U186.

    Family and domain databases

    Gene3Di 1.10.730.10. 1 hit.
    3.30.1360.70. 1 hit.
    3.40.50.620. 1 hit.
    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 PF05746. DALR_1. 1 hit.
    PF00750. tRNA-synt_1d. 1 hit.
    [Graphical view ]
    PRINTSi PR01038. TRNASYNTHARG.
    SMARTi 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: NOD.
      Tissue: Spleen.
    2. "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 II.
      Tissue: Mammary gland.
    3. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-568, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiSYRM_MOUSE
    AccessioniPrimary (citable) accession number: Q3U186
    Secondary accession number(s): Q8QZU7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: October 11, 2005
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 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