SYTC_MOUSE
ID SYTC_MOUSE Reviewed; 722 AA.
AC Q9D0R2; Q3TL42; Q7TMQ2; Q8BMI6; Q9CX03;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Threonine--tRNA ligase 1, cytoplasmic;
DE EC=6.1.1.3 {ECO:0000269|PubMed:29579307};
DE AltName: Full=Threonine--tRNA ligase, cytoplasmic;
DE AltName: Full=Threonyl-tRNA synthetase;
DE Short=ThrRS;
DE AltName: Full=Threonyl-tRNA synthetase 1;
GN Name=Tars1; Synonyms=Tars {ECO:0000312|MGI:MGI:106314};
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=Amnion, Bone marrow, Forelimb, and Heart;
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=C3H/He; TISSUE=Mesenchymal stem cell;
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 ISGYLATION.
RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT human cells.";
RL Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-297, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-242, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
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).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF HIS-154 AND HIS-158.
RX PubMed=29579307; DOI=10.1093/nar/gky211;
RA Chen Y., Ruan Z.R., Wang Y., Huang Q., Xue M.Q., Zhou X.L., Wang E.D.;
RT "A threonyl-tRNA synthetase-like protein has tRNA aminoacylation and
RT editing activities.";
RL Nucleic Acids Res. 46:3643-3656(2018).
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, at the post-
CC transfer stage. {ECO:0000269|PubMed:29579307}.
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:0000269|PubMed:29579307};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.74 uM for tRNA(Thr) {ECO:0000269|PubMed:29579307};
CC KM=0.30 mM for L-threonine {ECO:0000269|PubMed:29579307};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P26639}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29579307}.
CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AK010256; BAB26799.1; -; mRNA.
DR EMBL; AK011146; BAB27429.2; -; mRNA.
DR EMBL; AK031064; BAC27235.1; -; mRNA.
DR EMBL; AK152945; BAE31616.1; -; mRNA.
DR EMBL; AK166693; BAE38950.1; -; mRNA.
DR EMBL; AK167597; BAE39654.1; -; mRNA.
DR EMBL; AK168969; BAE40773.1; -; mRNA.
DR EMBL; BC055371; AAH55371.1; -; mRNA.
DR CCDS; CCDS27385.1; -.
DR RefSeq; NP_149065.2; NM_033074.3.
DR AlphaFoldDB; Q9D0R2; -.
DR SMR; Q9D0R2; -.
DR BioGRID; 226055; 14.
DR STRING; 10090.ENSMUSP00000022849; -.
DR ChEMBL; CHEMBL3751649; -.
DR iPTMnet; Q9D0R2; -.
DR PhosphoSitePlus; Q9D0R2; -.
DR SwissPalm; Q9D0R2; -.
DR EPD; Q9D0R2; -.
DR jPOST; Q9D0R2; -.
DR MaxQB; Q9D0R2; -.
DR PaxDb; Q9D0R2; -.
DR PeptideAtlas; Q9D0R2; -.
DR PRIDE; Q9D0R2; -.
DR ProteomicsDB; 263196; -.
DR Antibodypedia; 9874; 180 antibodies from 30 providers.
DR DNASU; 110960; -.
DR Ensembl; ENSMUST00000022849; ENSMUSP00000022849; ENSMUSG00000022241.
DR GeneID; 110960; -.
DR KEGG; mmu:110960; -.
DR UCSC; uc007vhc.1; mouse.
DR CTD; 110960; -.
DR MGI; MGI:106314; Tars.
DR VEuPathDB; HostDB:ENSMUSG00000022241; -.
DR eggNOG; KOG1637; Eukaryota.
DR GeneTree; ENSGT00940000154969; -.
DR HOGENOM; CLU_008554_0_1_1; -.
DR InParanoid; Q9D0R2; -.
DR OMA; FYYDFAY; -.
DR OrthoDB; 813937at2759; -.
DR PhylomeDB; Q9D0R2; -.
DR TreeFam; TF300858; -.
DR BioGRID-ORCS; 110960; 26 hits in 75 CRISPR screens.
DR ChiTaRS; Tars; mouse.
DR PRO; PR:Q9D0R2; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9D0R2; protein.
DR Bgee; ENSMUSG00000022241; Expressed in primitive streak and 276 other tissues.
DR ExpressionAtlas; Q9D0R2; baseline and differential.
DR Genevisible; Q9D0R2; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IDA:UniProtKB.
DR CDD; cd00771; ThrRS_core; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 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; IPR033728; ThrRS_core.
DR InterPro; IPR012947; tRNA_SAD.
DR PANTHER; PTHR11451; PTHR11451; 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; SSF55186; SSF55186; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00418; thrS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51880; TGS; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..722
FT /note="Threonine--tRNA ligase 1, cytoplasmic"
FT /id="PRO_0000101120"
FT DOMAIN 78..142
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 242
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 245
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P26639"
FT MOD_RES 297
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 452
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P26639"
FT MUTAGEN 154
FT /note="H->A: Impairs post-transfer editing activity but no
FT effect on aminoacylation activity; when associated with A-
FT 158."
FT /evidence="ECO:0000269|PubMed:29579307"
FT MUTAGEN 158
FT /note="H->A: Impairs post-transfer editing activity but no
FT effect on aminoacylation activity; when associated with A-
FT 154."
FT /evidence="ECO:0000269|PubMed:29579307"
FT CONFLICT 176
FT /note="P -> S (in Ref. 1; BAB26799)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="I -> T (in Ref. 1; BAB26799)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="H -> Y (in Ref. 2; AAH55371)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="R -> G (in Ref. 1; BAB26799)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="I -> T (in Ref. 2; AAH55371)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="D -> Y (in Ref. 1; BAC27235)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 722 AA; 83356 MW; FFBA7DC409BFD0B1 CRC64;
MSQEKASSPS GKMDGEKPVD ASEEKRKEGG KKKSKDGGGD GGRAELNPWP EYINTRLDMY
NKLKAEHDSI LAEKAAKDSK PIKVTLPDGK QVDAESWKTT PYQIACGISQ GLADNTVVAK
VNKVVWDLDR PLETDCTLEL LKFEDEEAQA VYWHSSAHIM GEAMERVYGG CLCYGPPIEN
GFYYDMYLEE GGVSSNDFSS LETLCKKIIK EKQTFERLEV KKETLLEMFK YNKFKCRILN
EKVNTPTTTV YRCGPLIDLC RGPHVRHTGK IKTLKIHKNS STYWEGKADM ETLQRIYGIS
FPDPKLLKEW EKFQEEAKNR DHRKIGRDQE LYFFHELSPG SCFFLPKGAY IYNTLMEFIR
SEYRKRGFQE VVTPNIFNSR LWMTSGHWQH YSENMFSFEV EKEQFALKPM NCPGHCLMFD
HRPRSWRELP LRLADFGVLH RNELSGALTG LTRVRRFQQD DAHIFCAMEQ IEDEIKGCLD
FLRTVYSVFG FSFKLNLSTR PEKFLGDIEI WNQAEKQLEN SLNEFGEKWE LNPGDGAFYG
PKIDIQIKDA IGRYHQCATI QLDFQLPIRF NLTYVSHDGD DKKRPVIVHR AILGSVERMI
AILTENYGGK WPFWLSPRQV MVVPVGPTCD EYAQKVRQQF HDAKFMADTD LDPGCTLNKK
IRNAQLAQYN FILVVGEKEK ASGTVNIRTR DNKVHGERTV EETVRRLQQL KQTRSKQAEE
EF
