SYWC_PONAB
ID SYWC_PONAB Reviewed; 472 AA.
AC Q5R4J1; Q5R784;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Tryptophan--tRNA ligase, cytoplasmic;
DE EC=6.1.1.2;
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex, and Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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 -!- SUBUNIT: Homodimer. Interacts with oxidized form of GAPDH (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Proteolytic cleavage generates 2 forms; T1-TrpRS and T2-TrpRS.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; CR860234; CAH92376.1; -; mRNA.
DR EMBL; CR861257; CAH93325.1; -; mRNA.
DR AlphaFoldDB; Q5R4J1; -.
DR SMR; Q5R4J1; -.
DR STRING; 9601.ENSPPYP00000006982; -.
DR Ensembl; ENSPPYT00000007257; ENSPPYP00000006982; ENSPPYG00000006142.
DR eggNOG; KOG2145; Eukaryota.
DR GeneTree; ENSGT00940000153724; -.
DR InParanoid; Q5R4J1; -.
DR OrthoDB; 817008at2759; -.
DR Proteomes; UP000001595; Chromosome 14.
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; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
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; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase; Angiogenesis; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..472
FT /note="Tryptophan--tRNA ligase, cytoplasmic"
FT /id="PRO_0000136740"
FT CHAIN 72..472
FT /note="T1-TrpRS"
FT /evidence="ECO:0000250"
FT /id="PRO_0000386465"
FT CHAIN 95..472
FT /note="T2-TrpRS"
FT /evidence="ECO:0000250"
FT /id="PRO_0000386466"
FT DOMAIN 9..65
FT /note="WHEP-TRS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00531"
FT MOTIF 165..174
FT /note="'HIGH' region"
FT MOTIF 350..354
FT /note="'KMSKS' region"
FT MOD_RES 155
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32921"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23381"
FT CONFLICT 5
FT /note="E -> V (in Ref. 1; CAH93325)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="E -> G (in Ref. 1; CAH93325)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="K -> E (in Ref. 1; CAH93325)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="G -> S (in Ref. 1; CAH92376)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="N -> S (in Ref. 1; CAH92376)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="P -> L (in Ref. 1; CAH93325)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 53373 MW; 8A38722E573F10D7 CRC64;
MPNSEPCVSP LELFNSIATQ GELVRSLKAG NASKDEIDSA VKMLLSLKMS YKAAMGEDYK
ANCPPGNPAP TSNHGPDATE AEEDFVDPWT VQTSSAKGID YDKLIVRFGS SKIDKELINR
IERATGQRPH RFLRRGIFFS HRDMNQVLDA YENKKPFYLY TGRGPSSEAM HVGHLIPFIF
TKWLQDVFNV PLVIQMTDDE KYLWKDLTLD QAYSYAVENA KDIIACGFDI NKTFIFSDLD
YMGMSSGFYK NVVKIQKHVT FNQVKGIFGF TDSDCIGKIS FPAIQAAPSF SNSFPQIFRD
RTDIQCLIPC AIDQDPYFRM TRDVAPRIGY PKPALLHSTF FPALQGAQTK MSASDPNSSI
FLTDTAKQIK TKVNKHAFSG GRDTIEEHRQ FGGNCDVDVS FMYLTFFLED DDKLEQIRKD
YTSGAMLTGE LKKALIEVLQ PLIAEHQARR KEVTDEIVKE FMTPRKLSFD FQ
