ID SYTM_MOUSE Reviewed; 723 AA.
AC Q3UQ84; B2RW19; Q9D0D6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 24-JAN-2024, entry version 132.
DE RecName: Full=Threonine--tRNA ligase, mitochondrial;
DE EC=6.1.1.3 {ECO:0000250|UniProtKB:Q9BW92};
DE AltName: Full=Threonyl-tRNA synthetase;
DE Short=ThrRS;
DE AltName: Full=Threonyl-tRNA synthetase-like 1;
DE Flags: Precursor;
GN Name=Tars2; Synonyms=Tarsl1;
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=Mammary gland;
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 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, Spleen, and
RC 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 attachment of threonine to tRNA(Thr) in a two-
CC step reaction: threonine is first activated by ATP to form Thr-AMP and
CC then transferred to the acceptor end of tRNA(Thr). Also edits
CC incorrectly charged tRNA(Thr) via its editing domain.
CC {ECO:0000250|UniProtKB:Q9BW92}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-
CC threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670,
CC Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3;
CC Evidence={ECO:0000250|UniProtKB:Q9BW92};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9BW92}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AK142685; BAE25159.1; -; mRNA.
DR EMBL; AK011540; BAB27683.1; -; mRNA.
DR EMBL; BC147501; AAI47502.1; -; mRNA.
DR CCDS; CCDS38548.1; -.
DR RefSeq; NP_001157089.1; NM_001163617.1.
DR RefSeq; NP_001157090.1; NM_001163618.1.
DR RefSeq; NP_082207.2; NM_027931.3.
DR AlphaFoldDB; Q3UQ84; -.
DR SMR; Q3UQ84; -.
DR BioGRID; 214943; 8.
DR STRING; 10090.ENSMUSP00000029752; -.
DR iPTMnet; Q3UQ84; -.
DR PhosphoSitePlus; Q3UQ84; -.
DR SwissPalm; Q3UQ84; -.
DR EPD; Q3UQ84; -.
DR MaxQB; Q3UQ84; -.
DR PaxDb; 10090-ENSMUSP00000029752; -.
DR PeptideAtlas; Q3UQ84; -.
DR ProteomicsDB; 254800; -.
DR Pumba; Q3UQ84; -.
DR Antibodypedia; 34029; 89 antibodies from 20 providers.
DR DNASU; 71807; -.
DR Ensembl; ENSMUST00000029752.15; ENSMUSP00000029752.9; ENSMUSG00000028107.15.
DR GeneID; 71807; -.
DR KEGG; mmu:71807; -.
DR UCSC; uc008qkr.2; mouse.
DR AGR; MGI:1919057; -.
DR CTD; 80222; -.
DR MGI; MGI:1919057; Tars2.
DR VEuPathDB; HostDB:ENSMUSG00000028107; -.
DR eggNOG; KOG1637; Eukaryota.
DR GeneTree; ENSGT00940000161600; -.
DR InParanoid; Q3UQ84; -.
DR OMA; PILEQTC; -.
DR OrthoDB; 1119631at2759; -.
DR PhylomeDB; Q3UQ84; -.
DR TreeFam; TF300858; -.
DR BioGRID-ORCS; 71807; 20 hits in 81 CRISPR screens.
DR ChiTaRS; Tars2; mouse.
DR PRO; PR:Q3UQ84; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q3UQ84; Protein.
DR Bgee; ENSMUSG00000028107; Expressed in ectoderm and 267 other cell types or tissues.
DR ExpressionAtlas; Q3UQ84; baseline and differential.
DR Genevisible; Q3UQ84; 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; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd01667; TGS_ThrRS; 1.
DR CDD; cd00860; ThrRS_anticodon; 1.
DR CDD; cd00771; ThrRS_core; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR HAMAP; MF_00184; Thr_tRNA_synth; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR002320; Thr-tRNA-ligase_IIa.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR047246; ThrRS_anticodon.
DR InterPro; IPR033728; ThrRS_core.
DR InterPro; IPR012947; tRNA_SAD.
DR NCBIfam; TIGR00418; thrS; 1.
DR PANTHER; PTHR11451:SF27; THREONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11451; THREONINE-TRNA LIGASE; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF02824; TGS; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR01047; TRNASYNTHTHR.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51880; TGS; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..723
FT /note="Threonine--tRNA ligase, mitochondrial"
FT /id="PRO_0000254587"
FT DOMAIN 64..126
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BW92"
FT CONFLICT 9
FT /note="R -> G (in Ref. 1; BAB27683)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 723 AA; 81700 MW; 046BF1D524D1EDCA CRC64;
MGLCLRWRRL GFPLPEFRRC ELHTVREASA PTPPHWLAER FGLFEELWTA HVKKLASMTQ
KKARAIKISL PEGQKVDAVA WNTTPYQLAH QISVTLADTA VAAEVNGELY DLDRPLETDC
HLRFLTFDSP EGKAVFWHSS AHVLGAAAEQ QLGAVLCRGP STESGFYHDF FLGKERTVRS
AELPILERIC QELIAAAQPF RRLEASRDQL RQLFKDNHFK LHLIEEKVTG PTATVYGCGM
SVDLCRGPHL RHTGQIGALK LLTNSSALWR SLGAPETLQR VSGISFPKVE LLRNWEARRE
AAELRDHRRI GKEQELFFFH ELSPGSCFFL PRGTRVYNAL VAFIRAEYAR RGFSEVKTPT
LFSTKLWEQS GHWEHYRADM FSLKPPGTDG VDNSQSGHPA RCPKDTLALK PMNCPAHCLM
FAHRPRSWRE LPVRLADFGA LHRAEASGSL GGLTRLWRFQ QDDAHIFCAP HQLEAEIQGC
LDFLRCVYSV LGFSFHLALS TRPPGFLGEP RLWDQAEQVL QQALEKFGEP WDLNPGDGAF
YGPKIDVHLH DALGRPHQCG TIQLDFQLPL RFDLQYKGPA GTPECPVLIH RAVLGSVERL
LGVLAESCGG KWPLWLSPLQ VVVIPVRTEQ EEYARQVQQC LQAAGLVSDL DADSGLTLSR
RVRRAQLAHY NFQFVVGQRE QSQRTVNVRT RDNRQLGERD LAESVQRLLE LQNARVPNAE
EVF
//
