SYEM_MOUSE
ID SYEM_MOUSE Reviewed; 523 AA.
AC Q9CXJ1; Q3TJB3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Probable glutamate--tRNA ligase, mitochondrial;
DE EC=6.1.1.17;
DE AltName: Full=Glutamyl-tRNA synthetase;
DE Short=GluRS;
DE Flags: Precursor;
GN Name=Ears2; Synonyms=Kiaa1970;
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; TISSUE=Head, and Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, 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).
RN [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-256, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-
CC step reaction: glutamate is first activated by ATP to form Glu-AMP and
CC then transferred to the acceptor end of tRNA(Glu). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-
CC glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663,
CC Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC ChEBI:CHEBI:456215; EC=6.1.1.17;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC Glutamate--tRNA ligase type 1 subfamily. {ECO:0000305}.
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DR EMBL; AK014324; BAB29273.1; -; mRNA.
DR EMBL; AK167506; BAE39582.1; -; mRNA.
DR EMBL; AK169225; BAE40994.1; -; mRNA.
DR EMBL; BC025907; AAH25907.1; -; mRNA.
DR CCDS; CCDS21807.1; -.
DR RefSeq; NP_080416.1; NM_026140.3.
DR AlphaFoldDB; Q9CXJ1; -.
DR SMR; Q9CXJ1; -.
DR STRING; 10090.ENSMUSP00000033159; -.
DR BindingDB; Q9CXJ1; -.
DR iPTMnet; Q9CXJ1; -.
DR PhosphoSitePlus; Q9CXJ1; -.
DR SwissPalm; Q9CXJ1; -.
DR EPD; Q9CXJ1; -.
DR MaxQB; Q9CXJ1; -.
DR PaxDb; Q9CXJ1; -.
DR PeptideAtlas; Q9CXJ1; -.
DR PRIDE; Q9CXJ1; -.
DR ProteomicsDB; 253434; -.
DR Antibodypedia; 25969; 129 antibodies from 22 providers.
DR DNASU; 67417; -.
DR Ensembl; ENSMUST00000033159; ENSMUSP00000033159; ENSMUSG00000030871.
DR GeneID; 67417; -.
DR KEGG; mmu:67417; -.
DR UCSC; uc009joe.2; mouse.
DR CTD; 124454; -.
DR MGI; MGI:1914667; Ears2.
DR VEuPathDB; HostDB:ENSMUSG00000030871; -.
DR eggNOG; KOG1149; Eukaryota.
DR GeneTree; ENSGT00390000009759; -.
DR HOGENOM; CLU_015768_6_3_1; -.
DR InParanoid; Q9CXJ1; -.
DR OMA; WDEGPFF; -.
DR OrthoDB; 879920at2759; -.
DR PhylomeDB; Q9CXJ1; -.
DR TreeFam; TF313268; -.
DR BioGRID-ORCS; 67417; 25 hits in 62 CRISPR screens.
DR ChiTaRS; Ears2; mouse.
DR PRO; PR:Q9CXJ1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9CXJ1; protein.
DR Bgee; ENSMUSG00000030871; Expressed in atrioventricular valve and 187 other tissues.
DR Genevisible; Q9CXJ1; MM.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; ISO:MGI.
DR GO; GO:0050561; F:glutamate-tRNA(Gln) ligase activity; ISO:MGI.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; ISO:MGI.
DR GO; GO:0070127; P:tRNA aminoacylation for mitochondrial protein translation; ISO:MGI.
DR CDD; cd00808; GluRS_core; 1.
DR Gene3D; 1.10.10.350; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00022; Glu_tRNA_synth_type1; 1.
DR InterPro; IPR045462; aa-tRNA-synth_I_cd-bd.
DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR InterPro; IPR004527; Glu-tRNA-ligase_bac/mito.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR033910; GluRS_core.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF19269; Anticodon_2; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF48163; SSF48163; 1.
DR TIGRFAMs; TIGR00464; gltX_bact; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW Transit peptide.
FT TRANSIT 1..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 42..523
FT /note="Probable glutamate--tRNA ligase, mitochondrial"
FT /id="PRO_0000254562"
FT MOTIF 45..53
FT /note="'HIGH' region"
FT MOTIF 284..288
FT /note="'KMSKS' region"
FT BINDING 40..42
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 228..232
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 284..288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 256
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 486
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5JPH6"
FT CONFLICT 188
FT /note="R -> S (in Ref. 1; BAE39582)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="T -> A (in Ref. 1; BAE39582)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 58326 MW; 39D506771FB96608 CRC64;
MAAPLKRLLL AEPHVVALGH RVGRREASLG PDPGAPVRVR FAPSPTGFLH LGGLRTALYN
YIFAKKHQGS FILRLEDTDQ SRLVPGAAES IEDMLEWAGI PPDESPRRGG PAGPYCQSQR
LALYAQATEA LLRSGAAYPC FCLPQRLELL KKEALRSRQT PRYDNRCRNL SQAQVAQKLA
VDPKPAIRFR LEEAVPAFQD LVYGWTQHEV ASVEGDPVIL KSDGFPTYHL ACVVDDHHMS
ISHVLRGSEW LVSTSKHLLL YQALGWQPPR FAHLPLLLNR DGSKLSKRQG DIFLEHFAAT
GFLPEALLDI ITNCGSGFAE NQMGRTLPEL ITQFDLTRIT CHSALLDLEK LPEFNRLHLR
RLVSSETQRP QLVEKLQGLV KEAFGSELQN KDVLDPAYME RILLLRQGHI SRLQDLVSPV
YSYLWTRPAV HRSELGASSE NVDVIAKRLL GLLERPGLSL TQDVLNRELK KLSEGLEGAK
HSSVMKLLRM ALSGQLQGPP VAEMMVSLGP KEVRERIQKV LSS
