SYWC_BOVIN
ID SYWC_BOVIN Reviewed; 476 AA.
AC P17248; Q3SZK9;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 3.
DT 03-AUG-2022, entry version 159.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Pancreas;
RX PubMed=1907847; DOI=10.1021/bi00245a021;
RA Garret M., Pajot B., Trezeguet V., Labouesse J., Merle M., Gandar J.-C.,
RA Benedetto J.-P., Sallafranque M.-L., Alterio J., Gueguen M., Sarger C.,
RA Labouesse B., Bonnet J.;
RT "A mammalian tryptophanyl-tRNA synthetase shows little homology to
RT prokaryotic synthetases but near identity with mammalian peptide chain
RT release factor.";
RL Biochemistry 30:7809-7817(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-475.
RC TISSUE=Pancreas;
RA Garret M., Trezeguet V., Pajot B., Gandar J.-C., Merle M., Guegueiv M.,
RA Benedetto J.-P., Sarger C., Alteriot J., la Bouessec B., Labouesse J.,
RA Bonnet J.;
RL Submitted (MAR-1990) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 112-124; 337-354 AND 424-476.
RC TISSUE=Pancreas;
RX PubMed=2631684;
RA Zargarova T.A., Kovaleva G.K., Favorova O.O., Levina N.B.,
RA Telezhinskaia I.N.;
RT "Amino acid sequence of various peptides of tryptophanyl-tRNA-synthetase
RT from bovine pancreas.";
RL Bioorg. Khim. 15:1307-1312(1989).
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 -!- 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; X53918; CAA37872.1; -; mRNA.
DR EMBL; BC102806; AAI02807.1; -; mRNA.
DR EMBL; X52113; CAA36356.1; -; mRNA.
DR PIR; A40279; YWBO.
DR RefSeq; NP_776643.1; NM_174218.1.
DR AlphaFoldDB; P17248; -.
DR SMR; P17248; -.
DR STRING; 9913.ENSBTAP00000006139; -.
DR PaxDb; P17248; -.
DR PeptideAtlas; P17248; -.
DR PRIDE; P17248; -.
DR Ensembl; ENSBTAT00000006139; ENSBTAP00000006139; ENSBTAG00000004679.
DR GeneID; 281576; -.
DR KEGG; bta:281576; -.
DR CTD; 7453; -.
DR VEuPathDB; HostDB:ENSBTAG00000004679; -.
DR VGNC; VGNC:36863; WARS1.
DR eggNOG; KOG2145; Eukaryota.
DR GeneTree; ENSGT00940000153724; -.
DR HOGENOM; CLU_032621_0_1_1; -.
DR InParanoid; P17248; -.
DR OMA; SIYHRFM; -.
DR OrthoDB; 817008at2759; -.
DR TreeFam; TF105669; -.
DR BRENDA; 6.1.1.2; 908.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000004679; Expressed in corpus epididymis and 108 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019210; F:kinase inhibitor activity; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0045765; P:regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0010835; P:regulation of protein ADP-ribosylation; IEA:Ensembl.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IBA:GO_Central.
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 Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Ligase; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..476
FT /note="Tryptophan--tRNA ligase, cytoplasmic"
FT /id="PRO_0000136737"
FT CHAIN 76..476
FT /note="T1-TrpRS"
FT /evidence="ECO:0000250"
FT /id="PRO_0000386459"
FT CHAIN 99..476
FT /note="T2-TrpRS"
FT /evidence="ECO:0000250"
FT /id="PRO_0000386460"
FT DOMAIN 13..69
FT /note="WHEP-TRS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00531"
FT REGION 1..117
FT /note="Dispensable to the catalytic activity"
FT REGION 63..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 169..178
FT /note="'HIGH' region"
FT MOTIF 354..358
FT /note="'KMSKS' region"
FT MOD_RES 159
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32921"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23381"
FT CONFLICT 17
FT /note="L -> M (in Ref. 3; CAA36356)"
FT /evidence="ECO:0000305"
FT CONFLICT 228..229
FT /note="IA -> T (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 451..459
FT /note="QARRKEVTD -> ESRKEVDM (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 53812 MW; 53ABC6859A7C6632 CRC64;
MADMSNGEQG CGSPLELFHS IAAQGELVRD LKARNAAKDE IDSAVKMLLS LKTSYKAATG
EDYKVDCPPG DPAPESGEGL DATEADEDFV DPWTVQTSSA KGIDYDKLIV RFGSSKIDKE
LVNRIERATG QRPHRFLRRG IFFSHRDMHQ ILDAYENKKP FYLYTGRGPS SEAMHVGHLI
PFIFTKWLQD VFNVPLVIQM TDDEKYLWKD LTLDQAYGYA VENAKDIIAC GFDINKTFIF
SDLDYMGMSP GFYKNVVKIQ KHVTFNQVKG IFGFTDSDCI GKISFPAIQA APSFSNSFPQ
IFRDRTDVQC LIPCAIDQDP YFRMTRDVAP RIGYPKPALL HSTFFPALQG AQTKMSASDP
NSSIFLTDTA KQIKTKVNKH AFSGGRDTVE EHRQFGGNCD VDVSFMYLTF FLEDDDKLEQ
IRRDYTSGAM LTGELKKELI EVLQPLIAEH QARRKEVTDE IVKEFMTPRK LSYDFQ
