ID SYLM_MOUSE Reviewed; 902 AA.
AC Q8VDC0; A6H6S4;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 155.
DE RecName: Full=Probable leucine--tRNA ligase, mitochondrial;
DE EC=6.1.1.4;
DE AltName: Full=Leucyl-tRNA synthetase;
DE Short=LeuRS;
DE Flags: Precursor;
GN Name=Lars2;
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 [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=12461651; DOI=10.1007/s00335-002-3037-y;
RA Kiss H., Darai E., Kiss C., Kost-Alimova M., Klein G., Dumanski J.P.,
RA Imreh S.;
RT "Comparative human/murine sequence analysis of the common eliminated region
RT 1 from human 3p21.3.";
RL Mamm. Genome 13:646-655(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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=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).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-67, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AJ428066; CAD20988.1; -; mRNA.
DR EMBL; BC080303; AAH80303.1; -; mRNA.
DR EMBL; BC138206; AAI38207.1; -; mRNA.
DR EMBL; BC145982; AAI45983.1; -; mRNA.
DR CCDS; CCDS23659.1; -.
DR RefSeq; NP_001335096.1; NM_001348167.1.
DR RefSeq; NP_001335097.1; NM_001348168.1.
DR RefSeq; NP_694808.1; NM_153168.3.
DR AlphaFoldDB; Q8VDC0; -.
DR SMR; Q8VDC0; -.
DR BioGRID; 221873; 3.
DR STRING; 10090.ENSMUSP00000036710; -.
DR iPTMnet; Q8VDC0; -.
DR PhosphoSitePlus; Q8VDC0; -.
DR SwissPalm; Q8VDC0; -.
DR EPD; Q8VDC0; -.
DR MaxQB; Q8VDC0; -.
DR PaxDb; 10090-ENSMUSP00000036710; -.
DR ProteomicsDB; 253440; -.
DR Pumba; Q8VDC0; -.
DR Antibodypedia; 29557; 188 antibodies from 25 providers.
DR DNASU; 102436; -.
DR Ensembl; ENSMUST00000038863.9; ENSMUSP00000036710.8; ENSMUSG00000035202.9.
DR GeneID; 102436; -.
DR KEGG; mmu:102436; -.
DR UCSC; uc009sgd.1; mouse.
DR AGR; MGI:2142973; -.
DR MGI; MGI:2142973; Lars2.
DR VEuPathDB; HostDB:ENSMUSG00000035202; -.
DR eggNOG; KOG0435; Eukaryota.
DR GeneTree; ENSGT00390000015114; -.
DR HOGENOM; CLU_004427_0_1_1; -.
DR InParanoid; Q8VDC0; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 2876972at2759; -.
DR PhylomeDB; Q8VDC0; -.
DR TreeFam; TF105662; -.
DR BRENDA; 6.1.1.4; 3474.
DR BioGRID-ORCS; 102436; 28 hits in 81 CRISPR screens.
DR ChiTaRS; Lars2; mouse.
DR PRO; PR:Q8VDC0; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8VDC0; Protein.
DR Bgee; ENSMUSG00000035202; Expressed in animal zygote and 236 other cell types or tissues.
DR ExpressionAtlas; Q8VDC0; baseline and differential.
DR Genevisible; Q8VDC0; MM.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; ISO:MGI.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; ISO:MGI.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF3; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 3.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..902
FT /note="Probable leucine--tRNA ligase, mitochondrial"
FT /id="PRO_0000035807"
FT MOTIF 91..101
FT /note="'HIGH' region"
FT MOTIF 638..642
FT /note="'KMSKS' region"
FT BINDING 641
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 67
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 235
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15031"
SQ SEQUENCE 902 AA; 101480 MW; F5ED21E130F3A5FC CRC64;
MASTCQRLSF YVSPLKRQLV SRPPVILWER LIPGCSRSIY SATGKWTKEY TLQTRKDVEK
WWHQQIKEQA SRVSEEDKLK PKFYLLSMFP YPSGKLHMGH VRVYTLSDTI ARFQKMRGMQ
VINPMGWDAF GLPAENAAIE RNLHPESWTQ SNIKHMRKQL DRLGLCFSWD REITTCLPDY
YKWTQYLFIK LYEAGLAYQK EALVNWDPVD QTVLANEQVN EYGCSWRSGA KVEKKYLRQW
FIKTTAYAKA MQDALADLPE WYGIKGMQAH WIGDCVGCHL DFTLKVDGED TGEKLTAYTA
TPEAIYGISH VAISPSHGLL HGCSSVKKAL QKALVPGRDC LTPVMAVSML TLQEVPIVIM
ANPDLEGSLD SKIGIPSTSS EDTRLAQALG LPYSEVIEAS PDGTERLSGS AEFTGMTRQD
AFVALTRKAR GMRVGGHVTS NKLKDWLISR QRYWGTPIPI VHCPACGPVP VPLQDLPVIL
PSIASLTGRG GSPLATALEW VNCSCPRCKG SAKRETDTMD TFVDSAWYYF RYTDPHNTQS
PFGSALADFW MPVDLYIGGK EHAVMHLFYA RFLSHFCHDQ KMVKHREPFH KLLAQGLIKG
QTFRLPSGQC LKKEDIDFTG PAPVCAKTKE KLEVTWEKMS KSKHNGVDPE EIVAQYGIDT
IRLYILFAAP PEKDILWDVK TDALPGVLRW QQRLWSLTTR FIEARTSGTV PQPQLLNSKE
KTKAQNLWEY KNAVIAQVTT HFTEDFALNS VVSQLMGLSS ALSQASQRVV LHSPEFEDAL
CALLVMAAPL APHVTSELWA GLTLVPSKLC DHYAWDSGVM LQAWPTVDSQ FLQKPDMVQM
AVLINNKACG KIPVPQHVAQ DQDKVHELVL QSELGMKLLQ GRSIKKAFLS PRTALINFLV
QE
//
