SYWC_RAT
ID SYWC_RAT Reviewed; 481 AA.
AC Q6P7B0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-473.
RA Soares M.B., Casavant T.L., Sheffield V.C., Bonaldo M.F., Bair T.B.,
RA Scheetz T.E., Snir E., Akabogu I., Bair J.L., Berger B., Crouch K.,
RA Davis A., Eystone M.E., Keppel C., Kucaba T.A., Lebeck M., Lin J.L.,
RA de Melo A.I.R., Rehmann J., Reiter R.S., Schaefer K., Smith C., Tack D.,
RA Trout K., Lin J.J.-C.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-424.
RC TISSUE=Prostate;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 429-481.
RX PubMed=8889548; DOI=10.1101/gr.6.9.791;
RA Bonaldo M.F., Lennon G., Soares M.B.;
RT "Normalization and subtraction: two approaches to facilitate gene
RT discovery.";
RL Genome Res. 6:791-806(1996).
RN [4]
RP PROTEIN SEQUENCE OF 269-299 AND 331-353, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
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 {ECO:0000250}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH61752.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY724504; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC061752; AAH61752.1; ALT_INIT; mRNA.
DR EMBL; BG376398; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_006240604.1; XM_006240542.3.
DR RefSeq; XP_008763034.1; XM_008764812.2.
DR AlphaFoldDB; Q6P7B0; -.
DR SMR; Q6P7B0; -.
DR BioGRID; 260721; 6.
DR IntAct; Q6P7B0; 3.
DR MINT; Q6P7B0; -.
DR STRING; 10116.ENSRNOP00000006128; -.
DR iPTMnet; Q6P7B0; -.
DR PhosphoSitePlus; Q6P7B0; -.
DR jPOST; Q6P7B0; -.
DR PaxDb; Q6P7B0; -.
DR PRIDE; Q6P7B0; -.
DR Ensembl; ENSRNOT00000006128; ENSRNOP00000006128; ENSRNOG00000004359.
DR GeneID; 314442; -.
DR UCSC; RGD:1308278; rat.
DR CTD; 7453; -.
DR RGD; 1308278; Wars.
DR eggNOG; KOG2145; Eukaryota.
DR GeneTree; ENSGT00940000153724; -.
DR InParanoid; Q6P7B0; -.
DR OMA; SIYHRFM; -.
DR OrthoDB; 817008at2759; -.
DR PhylomeDB; Q6P7B0; -.
DR TreeFam; TF105669; -.
DR PRO; PR:Q6P7B0; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000004359; Expressed in pancreas and 19 other tissues.
DR ExpressionAtlas; Q6P7B0; baseline and differential.
DR Genevisible; Q6P7B0; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019210; F:kinase inhibitor activity; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:0045765; P:regulation of angiogenesis; ISO:RGD.
DR GO; GO:0010835; P:regulation of protein ADP-ribosylation; ISO:RGD.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; ISO:RGD.
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; Angiogenesis; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Ligase; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..481
FT /note="Tryptophan--tRNA ligase, cytoplasmic"
FT /id="PRO_0000274190"
FT CHAIN 75..481
FT /note="T1-TrpRS"
FT /evidence="ECO:0000250"
FT /id="PRO_0000386469"
FT CHAIN 98..481
FT /note="T2-TrpRS"
FT /evidence="ECO:0000250"
FT /id="PRO_0000386470"
FT DOMAIN 12..68
FT /note="WHEP-TRS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00531"
FT REGION 65..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000250|UniProtKB:P32921"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23381"
FT CONFLICT 385
FT /note="R -> S (in Ref. 1; AY724504)"
FT /evidence="ECO:0000305"
FT CONFLICT 423..424
FT /note="DY -> VS (in Ref. 2; AAH61752)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 54144 MW; 5CB5E7BAB46FF695 CRC64;
MADMPSGESC TSPLELFNSI AAQGELVRSL KAGNAPKDEI ESAVKMLLSL KMNYKTAMGE
EYKAGCPPGN STAGSNGDPD ATKASEDFVD PWTVRTSSAK GIDYDKLIVQ FGSSKIDKEL
INRIERATGQ RPHRFLRRGI FFSHRDMNQI LDAYENKKPF YLYTGRGPSS EAMHLGHLVP
FIFTKWLQDV FDVPLVIQMS DDEKYLWKDL TLEQAYSYTV ENAKDIIACG FDVNKTFIFS
DLEYMGQSPG FYKNVVKIQK HVTFNQVKGI FGFTDSDCIG KISFPAVQAA PSFSNSFPKI
FRDRTDIQCL IPCAIDQDPY FRMTRDVAPR IGHPKPALLH STFFPALQGA QTKMSASDPN
SSIFLTDTAK QIKSKVNKHA FSGGRDTVEE HRQFGGNCEV DVSFMYLTFF LEDDDSLEQI
RKDYTSGAML TGELKKTLID VLQPLIAEHQ ARRKAVTEET VKEFMAPRQL SFHFQCFCFD
T
