SYWC_RABIT
ID SYWC_RABIT Reviewed; 475 AA.
AC P23612; Q28607;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 3.
DT 25-MAY-2022, entry version 122.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2185472; DOI=10.1073/pnas.87.9.3508;
RA Lee C.C., Craigen W.J., Muzny D.M., Harlow E., Caskey C.T.;
RT "Cloning and expression of a mammalian peptide chain release factor with
RT sequence similarity to tryptophanyl-tRNA synthetases.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:3508-3512(1990).
RN [2]
RP SEQUENCE REVISION TO 169-174 AND 227-228, AND FUNCTION.
RX PubMed=8404867; DOI=10.1002/j.1460-2075.1993.tb06079.x;
RA Frolova L.Y., Dalphin M.E., Justesen J., Powell R.J., Drugeon G.,
RA McCaughan K.K., Kisselev L.L., Tate W.P., Haenni A.-L.;
RT "Mammalian polypeptide chain release factor and tryptophanyl-tRNA
RT synthetase are distinct proteins.";
RL EMBO J. 12:4013-4019(1993).
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 ECO:0000269|PubMed:8404867}.
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}.
CC -!- CAUTION: Was originally thought to be a eukaryotic release factor
CC (ERF). {ECO:0000305|PubMed:2185472}.
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DR EMBL; M33460; AAA31246.1; ALT_SEQ; mRNA.
DR EMBL; U02595; AAB60257.1; -; mRNA.
DR PIR; A35904; YWRBPR.
DR RefSeq; NP_001075757.1; NM_001082288.1.
DR AlphaFoldDB; P23612; -.
DR SMR; P23612; -.
DR STRING; 9986.ENSOCUP00000013564; -.
DR PRIDE; P23612; -.
DR GeneID; 100009123; -.
DR KEGG; ocu:100009123; -.
DR CTD; 7453; -.
DR eggNOG; KOG2145; Eukaryota.
DR InParanoid; P23612; -.
DR OrthoDB; 817008at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:InterPro.
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..475
FT /note="Tryptophan--tRNA ligase, cytoplasmic"
FT /id="PRO_0000136741"
FT CHAIN 75..475
FT /note="T1-TrpRS"
FT /evidence="ECO:0000250"
FT /id="PRO_0000386467"
FT CHAIN 98..475
FT /note="T2-TrpRS"
FT /evidence="ECO:0000250"
FT /id="PRO_0000386468"
FT DOMAIN 12..68
FT /note="WHEP-TRS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00531"
FT REGION 61..87
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"
SQ SEQUENCE 475 AA; 53799 MW; 33BC9E718FF45DC4 CRC64;
MADVTNGERC ASPQELFSSI AAQGELVKSL KARKAPKEEI DSAVKMLLSL KTSYKEAMGE
DYKADCPPGN STPDSHGDPE AVDDKEDFVD PWTVRTSSAK GIDYDKLIVQ FGSSKIDKEL
VNRIERATGQ RPHRFLRRGI FFSHRDMNQV LDAYENKKPF YLYTGRGPSS EAMHVGHLIP
FIFTKWLQDV FDVPLVVQMS DDEKYLWKDL TLEQVYGYTL ENAKDIIACG FDVNKTFIFS
DLDYMGMSPG FYKNVVKIQK HVTFNQVKGI FGFTDSDCIG KISFPAIQAA PSFSNSFPQI
FHGQADIQCL IPCAIDQDPY FRMTRDVAPR IGYPKPALLH STFFPALQGA QTKMSASDPN
SSIFLTDTAK QIKTKVNKHA FSGGRDTIEE HRQFGGNCDV DVSFMYLTFF LEDDDKLEQI
RKDYSSGAML TGELKKELID VLQPLVAEHQ ARRKEVTDEM VKEFMTPRQL CFHYQ
