SYTC2_MOUSE
ID SYTC2_MOUSE Reviewed; 790 AA.
AC Q8BLY2; Q8CHT2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Threonine--tRNA ligase 2, cytoplasmic;
DE EC=6.1.1.3 {ECO:0000269|PubMed:29579307};
DE AltName: Full=Threonyl-tRNA synthetase;
DE Short=ThrRS;
DE AltName: Full=Threonyl-tRNA synthetase protein 3;
GN Name=Tars3; Synonyms=Tarsl2;
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=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=Mammary tumor;
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, Pancreas, Spleen,
RC 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 FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP NUCLEAR LOCALIZATION SIGNAL, AND MUTAGENESIS OF HIS-222; HIS-226; CYS-480;
RP ARG-509 AND 774-LYS--LYS-780.
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 -!- SUBUNIT: May be a component of the multisynthetase complex (MSC), a
CC large multi-subunit complex which contains at least eight different
CC aminoacyl-tRNA synthetases plus three auxillary subunits AIMP1, AIMP2
CC and EEF1E1. Interacts with the MSC components EPRS1, AIMP1, AIMP2 and
CC KARS1. {ECO:0000250|UniProtKB:A2RTX5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29579307}. Nucleus
CC {ECO:0000269|PubMed:29579307}. Note=Primarily cytoplasmic. Also
CC detected at lower levels in the nucleus. {ECO:0000269|PubMed:29579307}.
CC -!- TISSUE SPECIFICITY: Ubiquitous (at protein level). Strongly expressed
CC in muscle (at protein level). Moderately expressed in heart and liver
CC (at protein level). Weakly expressed in stomach, kidney, testis,
CC spleen, brain, fat and lung (at protein level).
CC {ECO:0000269|PubMed:29579307}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AK040927; BAC30749.1; -; mRNA.
DR EMBL; BC039225; AAH39225.1; -; mRNA.
DR CCDS; CCDS21339.1; -.
DR RefSeq; NP_758514.2; NM_172310.2.
DR AlphaFoldDB; Q8BLY2; -.
DR SMR; Q8BLY2; -.
DR BioGRID; 234870; 2.
DR STRING; 10090.ENSMUSP00000032728; -.
DR PhosphoSitePlus; Q8BLY2; -.
DR EPD; Q8BLY2; -.
DR jPOST; Q8BLY2; -.
DR MaxQB; Q8BLY2; -.
DR PaxDb; Q8BLY2; -.
DR PeptideAtlas; Q8BLY2; -.
DR PRIDE; Q8BLY2; -.
DR ProteomicsDB; 263195; -.
DR Antibodypedia; 53619; 141 antibodies from 20 providers.
DR DNASU; 272396; -.
DR Ensembl; ENSMUST00000032728; ENSMUSP00000032728; ENSMUSG00000030515.
DR GeneID; 272396; -.
DR KEGG; mmu:272396; -.
DR UCSC; uc009hgr.2; mouse.
DR CTD; 272396; -.
DR MGI; MGI:2444486; Tarsl2.
DR VEuPathDB; HostDB:ENSMUSG00000030515; -.
DR eggNOG; KOG1637; Eukaryota.
DR GeneTree; ENSGT00940000159348; -.
DR HOGENOM; CLU_008554_0_3_1; -.
DR InParanoid; Q8BLY2; -.
DR OMA; IWDEAEK; -.
DR OrthoDB; 813937at2759; -.
DR PhylomeDB; Q8BLY2; -.
DR TreeFam; TF300858; -.
DR BioGRID-ORCS; 272396; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Tarsl2; mouse.
DR PRO; PR:Q8BLY2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BLY2; protein.
DR Bgee; ENSMUSG00000030515; Expressed in quadriceps femoris and 217 other tissues.
DR Genevisible; Q8BLY2; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; IDA:UniProtKB.
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; Coiled coil;
KW Cytoplasm; Ligase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:A2RTX5"
FT CHAIN 2..790
FT /note="Threonine--tRNA ligase 2, cytoplasmic"
FT /id="PRO_0000333829"
FT DOMAIN 148..210
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT REGION 80..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 13..68
FT /evidence="ECO:0000255"
FT MOTIF 774..780
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:29579307"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:A2RTX5"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2RTX5"
FT MUTAGEN 222
FT /note="H->A: Impairs post-transfer editing activity but no
FT effect on aminoacylation activity; when associated with A-
FT 226."
FT /evidence="ECO:0000269|PubMed:29579307"
FT MUTAGEN 226
FT /note="H->A: Impairs post-transfer editing activity but no
FT effect on aminoacylation activity; when associated with A-
FT 222."
FT /evidence="ECO:0000269|PubMed:29579307"
FT MUTAGEN 480
FT /note="C->A: Impairs aminoacylation activity."
FT /evidence="ECO:0000269|PubMed:29579307"
FT MUTAGEN 509
FT /note="R->A: Impairs aminoacylation activity."
FT /evidence="ECO:0000269|PubMed:29579307"
FT MUTAGEN 774..780
FT /note="KLKNLKK->ALANLAA: Abolishes nuclear localization."
FT /evidence="ECO:0000269|PubMed:29579307"
FT CONFLICT 381
FT /note="F -> I (in Ref. 2; AAH39225)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 790 AA; 91318 MW; 50554D74CC75BB29 CRC64;
MAAQALAAQA VASRLQRQEE DIRWLCAEVQ RLRDEQLRGP ERGQAEGPRL TREVAQLQAE
NRDLHQRLCG LRLRLAEQRR TEAGRAAAHE PPTQNQEKDT KKKRLKQSEP GREVKQPNFI
KERLQLFETL KTDHQLLPAT QEKKNTNNVI SVRVAGGKTV QGERWKTTPY QVAAGISKEL
AEHTVIAKVN GVLWDLDRPL EGDSTVELLM FDNEEAQAVY WHSSAHILGE AMELYYGGHL
CYGPPIENGF YYDMFIEDRV VSSTELSALE NICKTIIKEK QPFERLEVSK DTLLEMFKYN
KFKCRILKEK VDTPTTTVYR CGPLIDLCKG PHVRHTGKIK AIKIFKNSST YWEGNPEMET
LQRIYGISFP DSKMMKDWEK FQEEAKSRDH RKIGKEQELF FFHDLSPGSC FFLPRGAFIY
NALMDFIREE YHKRNFTEVL SPNMYNSKLW ETSGHWQHYS NNMFTFDVEK DTFALKPMNC
PGHCLMFAHR PRSWREMPVR FADFGVLHRN ELSGTLSGLT RVRRFQQDDA HIFCMVEQIE
EEIKGCLHFL QSVYSTFGFS FQLNLSTRPE HFLGEIEIWD EAERQLQNSL VEFGKPWKIN
PGDGAFYGPK IDIKIKDAIG RYHQCATIQL DFQLPIRFNL TYVSKDGDDK NRPVIIHRAI
LGSVERMIAI LSENYGGKWP LWLSPRQVMV IPVGPACENY ALQVSKECFE EGFMADVDLD
DSCTLNKKIR NAQLAQYNFI LVVGEKEKIN NAVNVRTRDN KIHGEISIAS VIEKLKNLKK
SRTLNAEEDF
