SYWC_MOUSE
ID SYWC_MOUSE Reviewed; 481 AA.
AC P32921; Q80ZY4; Q99J58; Q9DC65;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Tryptophan--tRNA ligase, cytoplasmic;
DE EC=6.1.1.2 {ECO:0000250|UniProtKB:P23381};
DE AltName: Full=Tryptophanyl-tRNA synthetase;
DE Short=TrpRS;
DE Contains:
DE RecName: Full=T1-TrpRS;
DE Contains:
DE RecName: Full=T2-TrpRS;
GN Name=Wars1; Synonyms=Wars, Wrs;
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 [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=7932716; DOI=10.1006/jmbi.1994.1608;
RA Pajot B., Sarger C., Bonnet J., Garret M.;
RT "An alternative splicing modifies the C-terminal end of tryptophanyl-tRNA
RT synthetase in murine embryonic stem cells.";
RL J. Mol. Biol. 242:599-603(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NMRI; TISSUE=Brain, and 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 [4]
RP PROTEIN SEQUENCE OF 38-45; 56-63; 84-95; 107-123; 146-166; 186-204;
RP 209-253; 269-299; 331-370; 423-436 AND 437-452, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
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 [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-158, 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).
CC -!- FUNCTION: T1-TrpRS has aminoacylation activity while T2-TrpRS lacks it.
CC T1-TrpRS and T2-TrpRS possess angiostatic activity. T2-TrpRS inhibits
CC fluid shear stress-activated responses of endothelial cells. Regulates
CC ERK, Akt, and eNOS activation pathways that are associated with
CC angiogenesis, cytoskeletal reorganization and shear stress-responsive
CC gene expression (By similarity). {ECO:0000250|UniProtKB:P23381}.
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:P23381};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with oxidized form of
CC GAPDH (By similarity). {ECO:0000250|UniProtKB:P23381}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long;
CC IsoId=P32921-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P32921-2; Sequence=VSP_006313;
CC -!- TISSUE SPECIFICITY: Isoform 2 is widely expressed, isoform 1 is found
CC only in embryonic stem cells.
CC -!- PTM: Proteolytic cleavage generates 2 forms; T1-TrpRS and T2-TrpRS.
CC {ECO:0000250|UniProtKB:P23381}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; X69656; CAA49347.1; -; Genomic_DNA.
DR EMBL; X69657; CAA49348.1; -; Genomic_DNA.
DR EMBL; AK004541; BAB23357.1; -; mRNA.
DR EMBL; BC003450; AAH03450.1; -; mRNA.
DR EMBL; BC046232; AAH46232.1; -; mRNA.
DR CCDS; CCDS26166.1; -. [P32921-1]
DR CCDS; CCDS49171.1; -. [P32921-2]
DR PIR; S50053; S50053.
DR RefSeq; NP_001157786.1; NM_001164314.1. [P32921-2]
DR RefSeq; NP_001157960.1; NM_001164488.1. [P32921-2]
DR RefSeq; NP_035840.3; NM_011710.3. [P32921-1]
DR RefSeq; XP_006515882.1; XM_006515819.1. [P32921-1]
DR AlphaFoldDB; P32921; -.
DR SMR; P32921; -.
DR BioGRID; 204543; 24.
DR STRING; 10090.ENSMUSP00000124625; -.
DR iPTMnet; P32921; -.
DR PhosphoSitePlus; P32921; -.
DR SwissPalm; P32921; -.
DR EPD; P32921; -.
DR jPOST; P32921; -.
DR MaxQB; P32921; -.
DR PaxDb; P32921; -.
DR PeptideAtlas; P32921; -.
DR PRIDE; P32921; -.
DR ProteomicsDB; 262988; -. [P32921-1]
DR ProteomicsDB; 262989; -. [P32921-2]
DR Antibodypedia; 27522; 269 antibodies from 30 providers.
DR DNASU; 22375; -.
DR Ensembl; ENSMUST00000109848; ENSMUSP00000105474; ENSMUSG00000021266. [P32921-2]
DR Ensembl; ENSMUST00000161154; ENSMUSP00000124625; ENSMUSG00000021266. [P32921-1]
DR Ensembl; ENSMUST00000161410; ENSMUSP00000125320; ENSMUSG00000021266. [P32921-2]
DR GeneID; 22375; -.
DR KEGG; mmu:22375; -.
DR UCSC; uc007pag.2; mouse. [P32921-1]
DR CTD; 22375; -.
DR MGI; MGI:104630; Wars.
DR VEuPathDB; HostDB:ENSMUSG00000021266; -.
DR eggNOG; KOG2145; Eukaryota.
DR GeneTree; ENSGT00940000153724; -.
DR HOGENOM; CLU_032621_0_1_1; -.
DR InParanoid; P32921; -.
DR OMA; SIYHRFM; -.
DR OrthoDB; 817008at2759; -.
DR PhylomeDB; P32921; -.
DR TreeFam; TF105669; -.
DR BRENDA; 6.1.1.2; 3474.
DR BioGRID-ORCS; 22375; 24 hits in 77 CRISPR screens.
DR ChiTaRS; Wars; mouse.
DR PRO; PR:P32921; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P32921; protein.
DR Bgee; ENSMUSG00000021266; Expressed in gastrula and 253 other tissues.
DR ExpressionAtlas; P32921; baseline and differential.
DR Genevisible; P32921; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019210; F:kinase inhibitor activity; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IDA:MGI.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0045765; P:regulation of angiogenesis; ISO:MGI.
DR GO; GO:0010835; P:regulation of protein ADP-ribosylation; ISO:MGI.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IDA:CAFA.
DR CDD; cd00806; TrpRS_core; 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; IPR009068; S15_NS1_RNA-bd.
DR InterPro; IPR002306; Trp-tRNA-ligase.
DR InterPro; IPR000738; WHEP-TRS_dom.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR Pfam; PF00458; WHEP-TRS; 1.
DR PRINTS; PR01039; TRNASYNTHTRP.
DR SMART; SM00991; WHEP-TRS; 1.
DR SUPFAM; SSF47060; SSF47060; 1.
DR TIGRFAMs; TIGR00233; trpS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS00762; WHEP_TRS_1; 1.
DR PROSITE; PS51185; WHEP_TRS_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Aminoacyl-tRNA synthetase; Angiogenesis; ATP-binding;
KW Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome.
FT CHAIN 1..481
FT /note="Tryptophan--tRNA ligase, cytoplasmic"
FT /id="PRO_0000136739"
FT CHAIN 75..481
FT /note="T1-TrpRS"
FT /evidence="ECO:0000250"
FT /id="PRO_0000386463"
FT CHAIN 98..481
FT /note="T2-TrpRS"
FT /evidence="ECO:0000250"
FT /id="PRO_0000386464"
FT DOMAIN 12..68
FT /note="WHEP-TRS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00531"
FT MOTIF 168..177
FT /note="'HIGH' region"
FT MOTIF 353..357
FT /note="'KMSKS' region"
FT MOD_RES 158
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23381"
FT VAR_SEQ 476..481
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_006313"
FT CONFLICT 52
FT /note="M -> V (in Ref. 3; AAH03450)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="V -> A (in Ref. 3; AAH46232)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="F -> P (in Ref. 1; CAA49347/CAA49348)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="Q -> E (in Ref. 1; CAA49347/CAA49348)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="I -> S (in Ref. 1; CAA49347/CAA49348)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 54358 MW; 39B55989AE895346 CRC64;
MADMPSGESC TSPLELFNSI ATQGELVRSL KAGNAPKDEI DSAVKMLLSL KMSYKAAMGE
EYKAGCPPGN PTAGRNCDSD ATKASEDFVD PWTVRTSSAK GIDYDKLIVQ FGSSKIDKEL
INRIERATGQ RPHRFLRRGI FFSHRDMNQI LDAYENKKPF YLYTGRGPSS EAMHLGHLVP
FIFTKWLQDV FNVPLVIQMS DDEKYLWKDL TLEQAYSYTV ENAKDIIACG FDINKTFIFS
DLEYMGQSPG FYRNVVKIQK HVTFNQVKGI FGFTDSDCIG KISFPAVQAA PSFSNSFPKI
FRDRTDIQCL IPCAIDQDPY FRMTRDVAPR IGHPKPALLH STFFPALQGA QTKMSASDPN
SSIFLTDTAK QIKSKVNKHA FSGGRDTVEE HRQFGGNCEV DVSFMYLTFF LEDDDRLEQI
RKDYTSGAML TGELKKTLID VLQPLIAEHQ ARRKAVTEET VKEFMTPRQL SFHFQCFCFD
T
