SYYM_MOUSE
ID SYYM_MOUSE Reviewed; 472 AA.
AC Q8BYL4; Q6PAH7;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Tyrosine--tRNA ligase, mitochondrial;
DE EC=6.1.1.1 {ECO:0000250|UniProtKB:Q9Y2Z4};
DE AltName: Full=Tyrosyl-tRNA synthetase;
DE Short=TyrRS;
DE Flags: Precursor;
GN Name=Yars2;
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 TISSUE=Jaw, and Limb;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-472.
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus;
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 [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).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-362, 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 -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-
CC step reaction: tyrosine is first activated by ATP to form Tyr-AMP and
CC then transferred to the acceptor end of tRNA(Tyr).
CC {ECO:0000250|UniProtKB:Q9Y2Z4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-
CC tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706,
CC Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2Z4};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9Y2Z4}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q9Y2Z4}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; BC060295; AAH60295.1; -; mRNA.
DR EMBL; AK039123; BAC30245.1; -; mRNA.
DR CCDS; CCDS27983.1; -.
DR RefSeq; NP_937889.1; NM_198246.2.
DR AlphaFoldDB; Q8BYL4; -.
DR SMR; Q8BYL4; -.
DR BioGRID; 213872; 4.
DR STRING; 10090.ENSMUSP00000055277; -.
DR iPTMnet; Q8BYL4; -.
DR PhosphoSitePlus; Q8BYL4; -.
DR EPD; Q8BYL4; -.
DR MaxQB; Q8BYL4; -.
DR PaxDb; Q8BYL4; -.
DR PeptideAtlas; Q8BYL4; -.
DR PRIDE; Q8BYL4; -.
DR ProteomicsDB; 254512; -.
DR Antibodypedia; 24801; 146 antibodies from 25 providers.
DR Ensembl; ENSMUST00000059955; ENSMUSP00000055277; ENSMUSG00000022792.
DR GeneID; 70120; -.
DR KEGG; mmu:70120; -.
DR UCSC; uc007yie.2; mouse.
DR CTD; 51067; -.
DR MGI; MGI:1917370; Yars2.
DR VEuPathDB; HostDB:ENSMUSG00000022792; -.
DR eggNOG; KOG2623; Eukaryota.
DR GeneTree; ENSGT00390000013709; -.
DR HOGENOM; CLU_024003_1_0_1; -.
DR InParanoid; Q8BYL4; -.
DR OMA; YMMAKDS; -.
DR OrthoDB; 914272at2759; -.
DR PhylomeDB; Q8BYL4; -.
DR TreeFam; TF105974; -.
DR BioGRID-ORCS; 70120; 30 hits in 73 CRISPR screens.
DR PRO; PR:Q8BYL4; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8BYL4; protein.
DR Bgee; ENSMUSG00000022792; Expressed in epiblast (generic) and 230 other tissues.
DR ExpressionAtlas; Q8BYL4; baseline and differential.
DR Genevisible; Q8BYL4; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0000049; F:tRNA binding; ISO:MGI.
DR GO; GO:0072545; F:tyrosine binding; ISO:MGI.
DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; ISO:MGI.
DR GO; GO:0070184; P:mitochondrial tyrosyl-tRNA aminoacylation; ISO:MGI.
DR GO; GO:0043039; P:tRNA aminoacylation; ISO:MGI.
DR CDD; cd00805; TyrRS_core; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR InterPro; IPR002307; Tyr-tRNA-ligase.
DR InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR PANTHER; PTHR11766; PTHR11766; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR TIGRFAMs; TIGR00234; tyrS; 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 ?..472
FT /note="Tyrosine--tRNA ligase, mitochondrial"
FT /id="PRO_0000035831"
FT MOTIF 77..86
FT /note="'HIGH' region"
FT MOTIF 276..280
FT /note="'KMSKS' region"
FT BINDING 72
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 116
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 216
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 220
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 223
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 242
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 279
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 350
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT MOD_RES 362
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
SQ SEQUENCE 472 AA; 52597 MW; 7775B040E3E8A2F1 CRC64;
MAAPMLRRLC RVPQSLVWLR GSRAVRPGAR GMLVAPRARG LFKEFFPESG TKTELPELFD
RRRAGSSPQT VYCGFDPTGD SLHVGHLLTL LGLFHFQRAG HNVIALVGGS TALLGDPSGR
TKGREALSAE CVRANAHALR RGLEALAANH ARLFADGRPW GSFTVLDNAA WFQEQHLVDF
LATVGGHFRM GTLLSRLSVQ SRLKSPEGMS LAEFFYQVLQ AYDFYYLFQH YGCRVQLGGS
DQLGNIMSGY EFIHKLTGED VFGITVPLIT STTGAKLGKS AGNAVWLNRE KTSPFELYQF
FVRQQDDSVE RYLKLFTFLP LPEIDHIMQL HVKEPEKRVA QKRLAAEVTK LVHGQEGLDS
AKRCTQALYH SSIEALEVMS DQELKELFKE ASFSELVLDP GTSVIDTCRK ANAIPDGPRG
YRMITEGGVS INHRQVTNPE SVLVIGQHIL KNGLSLLKIG KRNFYIIKWL QL
