ID SYWM_MOUSE Reviewed; 360 AA.
AC Q9CYK1; Q8BFV8;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 24-JAN-2024, entry version 143.
DE RecName: Full=Tryptophan--tRNA ligase, mitochondrial;
DE EC=6.1.1.2 {ECO:0000250|UniProtKB:Q9UGM6};
DE AltName: Full=(Mt)TrpRS;
DE AltName: Full=Tryptophanyl-tRNA synthetase;
DE Short=TrpRS;
DE Flags: Precursor;
GN Name=Wars2;
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=Cerebellum, and Embryo;
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=Kidney;
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, Lung, and Spleen;
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 tryptophan to tRNA(Trp) in a two-
CC step reaction: tryptophan is first activated by ATP to form Trp-AMP and
CC then transferred to the acceptor end of tRNA(Trp).
CC {ECO:0000250|UniProtKB:Q9UGM6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-
CC tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671,
CC Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2;
CC Evidence={ECO:0000250|UniProtKB:Q9UGM6};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q9UGM6}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9UGM6}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AK017602; BAB30833.1; -; mRNA.
DR EMBL; AK042715; BAC31342.1; -; mRNA.
DR EMBL; AK042964; BAC31422.1; -; mRNA.
DR EMBL; BC089583; AAH89583.1; -; mRNA.
DR CCDS; CCDS17672.1; -.
DR RefSeq; NP_081738.2; NM_027462.4.
DR AlphaFoldDB; Q9CYK1; -.
DR SMR; Q9CYK1; -.
DR BioGRID; 214134; 1.
DR STRING; 10090.ENSMUSP00000004343; -.
DR iPTMnet; Q9CYK1; -.
DR PhosphoSitePlus; Q9CYK1; -.
DR EPD; Q9CYK1; -.
DR MaxQB; Q9CYK1; -.
DR PaxDb; 10090-ENSMUSP00000004343; -.
DR PeptideAtlas; Q9CYK1; -.
DR ProteomicsDB; 253451; -.
DR Pumba; Q9CYK1; -.
DR Antibodypedia; 33903; 86 antibodies from 27 providers.
DR DNASU; 70560; -.
DR Ensembl; ENSMUST00000004343.7; ENSMUSP00000004343.3; ENSMUSG00000004233.15.
DR GeneID; 70560; -.
DR KEGG; mmu:70560; -.
DR UCSC; uc008qqk.1; mouse.
DR AGR; MGI:1917810; -.
DR CTD; 10352; -.
DR MGI; MGI:1917810; Wars2.
DR VEuPathDB; HostDB:ENSMUSG00000004233; -.
DR eggNOG; KOG2713; Eukaryota.
DR GeneTree; ENSGT00940000153724; -.
DR HOGENOM; CLU_029244_1_5_1; -.
DR InParanoid; Q9CYK1; -.
DR OMA; GWGQFKP; -.
DR OrthoDB; 179020at2759; -.
DR PhylomeDB; Q9CYK1; -.
DR TreeFam; TF314321; -.
DR BioGRID-ORCS; 70560; 22 hits in 76 CRISPR screens.
DR ChiTaRS; Wars2; mouse.
DR PRO; PR:Q9CYK1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9CYK1; Protein.
DR Bgee; ENSMUSG00000004233; Expressed in metanephric loop of Henle and 196 other cell types or tissues.
DR ExpressionAtlas; Q9CYK1; baseline and differential.
DR Genevisible; Q9CYK1; MM.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0070183; P:mitochondrial tryptophanyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0001570; P:vasculogenesis; IDA:MGI.
DR CDD; cd00806; TrpRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR HAMAP; MF_00140_B; Trp_tRNA_synth_B; 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; IPR002306; Trp-tRNA-ligase.
DR InterPro; IPR024109; Trp-tRNA-ligase_bac-type.
DR NCBIfam; TIGR00233; trpS; 1.
DR PANTHER; PTHR43766; TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43766:SF1; TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01039; TRNASYNTHTRP.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..18
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 19..360
FT /note="Tryptophan--tRNA ligase, mitochondrial"
FT /id="PRO_0000035829"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 48..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 167
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 179..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 226..230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT CONFLICT 148..149
FT /note="KQ -> NR (in Ref. 1; BAB30833)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 40153 MW; E777D70B3827807A CRC64;
MALFSVRKAR ECWRFIRALH KGPAATLAPQ KESGERVFSG IQPTGILHLG NYLGAIESWV
NLQEEYDTVI YSIVDLHSIT VPQDPTVLQQ SILDMTAVLL ACGINPEKSI LFQQSKVSEH
TQLSWILTCM VRLPRLQHLH QWKAKAAKQK HDGTVGLLTY PVLQAADILC YKSTHVPVGE
DQVQHMELVQ DLARSFNQKY GEFFPLPKSI LTSMKKVKSL RDPSSKMSKS DPDKLATVRI
TDSPEEIVQK FRKAVTDFTS EVTYEPDSRA GVSNMVAIHA AVSGLSVEEV VRSSAGLDTA
RYKLLVADAV IEKFAPIRKE IEKLKMDKDH LRKVLLVGSA KAKELASPVF EEVKKLVGIL
//
