LOCUS       NP_001121131             902 aa            linear   ROD 31-MAR-2024
DEFINITION  methionine--tRNA ligase, cytoplasmic [Rattus norvegicus].
ACCESSION   NP_001121131
VERSION     NP_001121131.1
DBSOURCE    REFSEQ: accession NM_001127659.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 902)
  AUTHORS   Topalidou,I., Cattin-Ortola,J., Pappas,A.L., Cooper,K.,
            Merrihew,G.E., MacCoss,M.J. and Ailion,M.
  TITLE     The EARP Complex and Its Interactor EIPR-1 Are Required for Cargo
            Sorting to Dense-Core Vesicles
  JOURNAL   PLoS Genet 12 (5), e1006074 (2016)
   PUBMED   27191843
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 902)
  AUTHORS   Han,J.M., Jeong,S.J., Park,M.C., Kim,G., Kwon,N.H., Kim,H.K.,
            Ha,S.H., Ryu,S.H. and Kim,S.
  TITLE     Leucyl-tRNA synthetase is an intracellular leucine sensor for the
            mTORC1-signaling pathway
  JOURNAL   Cell 149 (2), 410-424 (2012)
   PUBMED   22424946
REFERENCE   3  (residues 1 to 902)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   4  (residues 1 to 902)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 902)
  AUTHORS   Yannay-Cohen,N., Carmi-Levy,I., Kay,G., Yang,C.M., Han,J.M.,
            Kemeny,D.M., Kim,S., Nechushtan,H. and Razin,E.
  TITLE     LysRS serves as a key signaling molecule in the immune response by
            regulating gene expression
  JOURNAL   Mol Cell 34 (5), 603-611 (2009)
   PUBMED   19524539
REFERENCE   6  (residues 1 to 902)
  AUTHORS   Kaminska,M., Havrylenko,S., Decottignies,P., Le Marechal,P.,
            Negrutskii,B. and Mirande,M.
  TITLE     Dynamic Organization of Aminoacyl-tRNA Synthetase Complexes in the
            Cytoplasm of Human Cells
  JOURNAL   J Biol Chem 284 (20), 13746-13754 (2009)
   PUBMED   19289464
REFERENCE   7  (residues 1 to 902)
  AUTHORS   Kaminska,M., Havrylenko,S., Decottignies,P., Gillet,S., Le
            Marechal,P., Negrutskii,B. and Mirande,M.
  TITLE     Dissection of the structural organization of the aminoacyl-tRNA
            synthetase complex
  JOURNAL   J Biol Chem 284 (10), 6053-6060 (2009)
   PUBMED   19131329
REFERENCE   8  (residues 1 to 902)
  AUTHORS   Kim,J.Y., Kang,Y.S., Lee,J.W., Kim,H.J., Ahn,Y.H., Park,H., Ko,Y.G.
            and Kim,S.
  TITLE     p38 is essential for the assembly and stability of macromolecular
            tRNA synthetase complex: implications for its physiological
            significance
  JOURNAL   Proc Natl Acad Sci U S A 99 (12), 7912-7916 (2002)
   PUBMED   12060739
REFERENCE   9  (residues 1 to 902)
  AUTHORS   Kaminska,M., Shalak,V. and Mirande,M.
  TITLE     The appended C-domain of human methionyl-tRNA synthetase has a
            tRNA-sequestering function
  JOURNAL   Biochemistry 40 (47), 14309-14316 (2001)
   PUBMED   11714285
REFERENCE   10 (residues 1 to 902)
  AUTHORS   Ko,Y.G., Kang,Y.S., Kim,E.K., Park,S.G. and Kim,S.
  TITLE     Nucleolar localization of human methionyl-tRNA synthetase and its
            role in ribosomal RNA synthesis
  JOURNAL   J Cell Biol 149 (3), 567-574 (2000)
   PUBMED   10791971
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1149184.1,
                                           SRR22399481.2966676.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..902
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..902
                     /product="methionine--tRNA ligase, cytoplasmic"
                     /EC_number="6.1.1.10"
                     /note="methionine-tRNA synthetase"
                     /calculated_mol_wt=101451
     Region          1..74
                     /region_name="GST_N_5"
                     /note="Glutathione S-transferase, N-terminal domain;
                     pfam18485"
                     /db_xref="CDD:436537"
     Region          77..179
                     /region_name="GST_C_MetRS_N"
                     /note="Glutathione S-transferase C-terminal-like, alpha
                     helical domain of Methionyl-tRNA synthetase from higher
                     eukaryotes; cd10307"
                     /db_xref="CDD:198340"
     Site            order(98..100,102..107,109..110,120,123,129..130)
                     /site_type="other"
                     /note="putative protein interface 1 [polypeptide binding]"
                     /db_xref="CDD:198340"
     Site            order(128..132,167..168,170..171,175,178..179)
                     /site_type="other"
                     /note="putative protein interface 2 [polypeptide binding]"
                     /db_xref="CDD:198340"
     Region          258..878
                     /region_name="PLN02610"
                     /note="probable methionyl-tRNA synthetase"
                     /db_xref="CDD:215329"
     CDS             1..902
                     /gene="Mars1"
                     /gene_synonym="Mars"
                     /coded_by="NM_001127659.1:11..2719"
                     /db_xref="GeneID:299851"
                     /db_xref="RGD:1305321"
ORIGIN      
        1 mrlfvsegsp gslpvlaaaa rargraelli stvgpeecvv pfltrpkvpv lqldsgnylf
       61 sasaicryff llcgweqddl tnqwleweat elqpvlsaal yclvvqgkkg edvlgplrrv
      121 lthidhslsr qncpflagdt esladivlwg alypllqdpa ylpeelgalq swfqtlstqe
      181 pcqraaetvl kqqgvlalrp ylqkqpqpqp lppegravsn epeeeelatl seediiaava
      241 awekglenlp plqpqqhpvl pvpgernvli tsalpyvnnv phlgniigcv lsadvfarys
      301 rlrqwntlyl cgtdeygtat etkameeglt pqeicdkyha ihvdiyrwfn isfdtfgrtt
      361 tplqtkitqd ifqrlltrgf vlqdtveqlr ceqcarflad rfvegvcpfc gyeeargdqc
      421 dkcgklinai elkrpqckvc rshpvvkssk hlfldlpkle krledwlgkt mpgsdwtpna
      481 rfiirswlrd glkprcitrd lkwgtpvple gfedkvfyvw fdatigylsi tanytdqwer
      541 wwknpeqvdl yqfmakdnvp fhglvfpcsa lgaednytlv knliateyln yedgkfsksr
      601 gigvfgdmaq dtgipadiwr fyllyirpeg qdsafswtdl liknnselln nlgnfinrag
      661 mfvskffggc vpemvlthdd rrlvahvswe lqryhqllek vrirdalrsi ltisrhgnqy
      721 iqvnepwkri kgdemdrqra gtvtgmavni aallsvmlqp ymptvsstiq tqlqlpeaac
      781 rilatsfict lpaghrigtv splfqklend qienlrqrfg ggqakgspkp avveavttag
      841 sqdiqvlvde vtkqgnivre lkaqkadknq vaaevaklld lkkqlalaeg kpietpkgkk
      901 kk
//
