SYMC_MOUSE
ID SYMC_MOUSE Reviewed; 902 AA.
AC Q68FL6;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Methionine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.10 {ECO:0000250|UniProtKB:P56192};
DE AltName: Full=Methionyl-tRNA synthetase;
DE Short=MetRS;
GN Name=Mars1; Synonyms=Mars;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [2]
RP SUBUNIT.
RX PubMed=12060739; DOI=10.1073/pnas.122110199;
RA Kim J.Y., Kang Y.-S., Lee J.-W., Kim H.J., Ahn Y.H., Park H., Ko Y.-G.,
RA Kim S.;
RT "p38 is essential for the assembly and stability of macromolecular tRNA
RT synthetase complex: implications for its physiological significance.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7912-7916(2002).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827 AND THR-837, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the specific attachment of an amino acid to its
CC cognate tRNA in a 2 step reaction: the amino acid (AA) is first
CC activated by ATP to form AA-AMP and then transferred to the acceptor
CC end of the tRNA. Plays a role in the synthesis of ribosomal RNA in the
CC nucleolus. {ECO:0000250|UniProtKB:P56192}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-
CC methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667,
CC Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530,
CC ChEBI:CHEBI:456215; EC=6.1.1.10;
CC Evidence={ECO:0000250|UniProtKB:P56192};
CC -!- SUBUNIT: Monomer. Part of a multisubunit complex that groups tRNA
CC ligases for Arg (RARS1), Asp (DARS1), Gln (QARS1), Ile (IARS1), Leu
CC (LARS1), Lys (KARS1), Met (MARS1) the bifunctional ligase for Glu and
CC Pro (EPRS1) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and
CC EEF1E1/p18. Forms a linear complex that contains MARS1, EEF1E1, EPRS1
CC and AIMP2 that is at the core of the multisubunit complex.
CC {ECO:0000269|PubMed:12060739}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P56192}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P56192}. Note=Localizes to the nucleolus in
CC proliferative cells but disappears in quiescent cells.
CC {ECO:0000250|UniProtKB:P56192}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; BC079643; AAH79643.1; -; mRNA.
DR CCDS; CCDS24237.1; -.
DR RefSeq; NP_001003913.1; NM_001003913.2.
DR RefSeq; NP_001165053.1; NM_001171582.1.
DR AlphaFoldDB; Q68FL6; -.
DR SMR; Q68FL6; -.
DR BioGRID; 229747; 12.
DR IntAct; Q68FL6; 2.
DR MINT; Q68FL6; -.
DR STRING; 10090.ENSMUSP00000037446; -.
DR iPTMnet; Q68FL6; -.
DR PhosphoSitePlus; Q68FL6; -.
DR SwissPalm; Q68FL6; -.
DR EPD; Q68FL6; -.
DR jPOST; Q68FL6; -.
DR MaxQB; Q68FL6; -.
DR PaxDb; Q68FL6; -.
DR PeptideAtlas; Q68FL6; -.
DR PRIDE; Q68FL6; -.
DR ProteomicsDB; 254506; -.
DR Antibodypedia; 1110; 177 antibodies from 29 providers.
DR DNASU; 216443; -.
DR Ensembl; ENSMUST00000037290; ENSMUSP00000037446; ENSMUSG00000040354.
DR GeneID; 216443; -.
DR KEGG; mmu:216443; -.
DR UCSC; uc007hiz.2; mouse.
DR CTD; 4141; -.
DR MGI; MGI:1345633; Mars1.
DR VEuPathDB; HostDB:ENSMUSG00000040354; -.
DR eggNOG; KOG0867; Eukaryota.
DR eggNOG; KOG1247; Eukaryota.
DR GeneTree; ENSGT00550000075017; -.
DR HOGENOM; CLU_009710_3_2_1; -.
DR InParanoid; Q68FL6; -.
DR OMA; HGNGYMQ; -.
DR OrthoDB; 333013at2759; -.
DR PhylomeDB; Q68FL6; -.
DR TreeFam; TF300526; -.
DR BioGRID-ORCS; 216443; 26 hits in 74 CRISPR screens.
DR ChiTaRS; Mars; mouse.
DR PRO; PR:Q68FL6; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q68FL6; protein.
DR Bgee; ENSMUSG00000040354; Expressed in floor plate of midbrain and 259 other tissues.
DR ExpressionAtlas; Q68FL6; baseline and differential.
DR Genevisible; Q68FL6; MM.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IDA:CAFA.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IMP:CAFA.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISO:MGI.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; ISO:MGI.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IDA:CAFA.
DR GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; ISO:MGI.
DR GO; GO:0009303; P:rRNA transcription; ISO:MGI.
DR CDD; cd07957; Anticodon_Ia_Met; 1.
DR CDD; cd00814; MetRS_core; 1.
DR Gene3D; 2.20.28.20; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00098; Met_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR041598; MARS_N.
DR InterPro; IPR023458; Met-tRNA_ligase_1.
DR InterPro; IPR014758; Met-tRNA_synth.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR033911; MetRS_core.
DR InterPro; IPR029038; MetRS_Zn.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009068; S15_NS1_RNA-bd.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR000738; WHEP-TRS_dom.
DR PANTHER; PTHR45765; PTHR45765; 1.
DR Pfam; PF19303; Anticodon_3; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF18485; GST_N_5; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR Pfam; PF00458; WHEP-TRS; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SMART; SM00991; WHEP-TRS; 1.
DR SUPFAM; SSF47060; SSF47060; 1.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF57770; SSF57770; 1.
DR TIGRFAMs; TIGR00398; metG; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS00762; WHEP_TRS_1; 1.
DR PROSITE; PS51185; WHEP_TRS_2; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1..902
FT /note="Methionine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000139263"
FT DOMAIN 74..212
FT /note="GST C-terminal"
FT DOMAIN 843..899
FT /note="WHEP-TRS"
FT MOTIF 275..285
FT /note="'HIGH' region"
FT MOTIF 595..599
FT /note="'KMSKS' region"
FT BINDING 598
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 837
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 902 AA; 101431 MW; ACCE81F1D8049027 CRC64;
MRLFVSEGSP GSLPVLAAAA RARGRAELLI STVGPEECVV PFLTRPKVPV LQLDSGNYLF
SASAICRYFF LLCGWEQDDL TNQWLEWEAT ELQPVLSAAL HCLVVQGKKG EDILGPLRRV
LTHIDHSLSR QNCPFLAGDT ESLADIVLWG ALYPLLQDPA YLPEELGALQ SWFQTLSTQE
PCQRAAETVL KQQGVLALRL YLQKQPQPQP PPPEGRTVSN ELEEEELATL SEEDIVTAVA
AWEKGLESLP PLKLQQHPVL PVPGERNVLI TSALPYVNNV PHLGNIIGCV LSADVFARYC
RLRQWNTLYL CGTDEYGTAT ETKAMEEGLT PREICDKYHA IHADIYRWFG ISFDTFGRTT
TPQQTKITQD IFQRLLTRGF VLRDTVEQLR CERCARFLAD RFVEGVCPFC GYEEARGDQC
DRCGKLINAI ELKKPQCKIC RSCPVVRSSQ HLFLDLPKLE KRLEDWLGKT VPGSDWTPNA
RFIIRSWLRD GLKPRCITRD LKWGTPVPLE GFEDKVFYVW FDATIGYVSI TANYTDQWEK
WWKNPEQVDL YQFMAKDNVP FHGLVFPCSV LGAEDNYTLV KHIIATEYLN YEDGKFSKSR
GIGVFGDMAK DTGIPADIWR FYLLYIRPEG QDSAFSWTDL LIKNNSELLN NLGNFINRAG
MFVSKFFGGC VPEMALTPDD RRLVAHVSWE LQHYHQLLEK VRIRDALRSI LTISRHGNQY
IQVNEPWKRI KGGEMDRQRA GTVTGMAVNM AALLSVMLQP YMPTVSSTIQ TQLQLPPAAC
RILATSFICT LPAGHRIGTV SPLFQKLEND QIENLRQRFG GGQAKGSPKP AAVEAVTAAG
SQHIQTLTDE VTKQGNVVRE LKAQKADKNQ VAAEVAKLLD LKKQLALAEG KPIETPKGKK
KK
