SYQ_RAT
ID SYQ_RAT Reviewed; 775 AA.
AC Q66H61; F1LPA0;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Glutamine--tRNA ligase;
DE EC=6.1.1.18 {ECO:0000250|UniProtKB:P47897};
DE AltName: Full=Glutaminyl-tRNA synthetase;
DE Short=GlnRS;
GN Name=Qars1; Synonyms=Qars {ECO:0000312|RGD:1359448};
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 {ECO:0000312|EMBL:AAH82002.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 TISSUE SPECIFICITY, AND INDUCTION BY PERIPHERAL NERVE INJURY.
RX PubMed=25467976; DOI=10.1007/s10735-014-9601-4;
RA Park B.S., Jo H.W., Jung J.;
RT "Expression profile of aminoacyl-tRNA synthetases in dorsal root ganglion
RT neurons after peripheral nerve injury.";
RL J. Mol. Histol. 46:115-122(2015).
CC -!- FUNCTION: Glutamine--tRNA ligase. Plays a critical role in brain
CC development. {ECO:0000250|UniProtKB:P47897}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-
CC glutaminyl-tRNA(Gln); Xref=Rhea:RHEA:20121, Rhea:RHEA-COMP:9662,
CC Rhea:RHEA-COMP:9681, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:78442, ChEBI:CHEBI:78521,
CC ChEBI:CHEBI:456215; EC=6.1.1.18;
CC Evidence={ECO:0000250|UniProtKB:P47897};
CC -!- SUBUNIT: Monomer. Part of a multisubunit complex that groups tRNA
CC ligases for Arg (RARS1), Asp (DARS1), Gln (QARS1), Ile (IARS1), Leu
CC (LARS1), Lys (KARS1), Met (MARS1) the bifunctional ligase for Glu and
CC Pro (EPRS1) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and
CC EEF1E1/p18. Interacts with RARS1. Part of a complex composed of RARS1,
CC QARS1 and AIMP1. {ECO:0000250|UniProtKB:P47897}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P47897}. Cytoplasm
CC {ECO:0000250|UniProtKB:P47897}.
CC -!- TISSUE SPECIFICITY: Detected in dorsal root ganglia (at protein level).
CC Detected in dorsal root ganglia. {ECO:0000269|PubMed:25467976}.
CC -!- INDUCTION: Down-regulated after peripheral nerve injury.
CC {ECO:0000269|PubMed:25467976}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|RuleBase:RU363037}.
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DR EMBL; AC107280; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC128721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC082002; AAH82002.1; -; mRNA.
DR EMBL; CH473954; EDL77164.1; -; Genomic_DNA.
DR RefSeq; NP_001007625.1; NM_001007624.1.
DR AlphaFoldDB; Q66H61; -.
DR SMR; Q66H61; -.
DR STRING; 10116.ENSRNOP00000060418; -.
DR iPTMnet; Q66H61; -.
DR PhosphoSitePlus; Q66H61; -.
DR jPOST; Q66H61; -.
DR PaxDb; Q66H61; -.
DR PRIDE; Q66H61; -.
DR GeneID; 290868; -.
DR KEGG; rno:290868; -.
DR CTD; 5859; -.
DR RGD; 1359448; Qars.
DR VEuPathDB; HostDB:ENSRNOG00000060912; -.
DR eggNOG; KOG1148; Eukaryota.
DR HOGENOM; CLU_001882_2_3_1; -.
DR InParanoid; Q66H61; -.
DR OMA; FAWRIMG; -.
DR OrthoDB; 809861at2759; -.
DR PhylomeDB; Q66H61; -.
DR TreeFam; TF105683; -.
DR PRO; PR:Q66H61; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Proteomes; UP000234681; Chromosome 8.
DR Bgee; ENSRNOG00000060912; Expressed in skeletal muscle tissue and 20 other tissues.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004819; F:glutamine-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0004860; F:protein kinase inhibitor activity; ISO:RGD.
DR GO; GO:0007420; P:brain development; ISO:RGD.
DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; ISS:UniProtKB.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:RGD.
DR GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR Gene3D; 1.10.10.2420; -; 1.
DR Gene3D; 1.10.8.1290; -; 1.
DR Gene3D; 2.40.240.10; -; 2.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR004514; Gln-tRNA-synth.
DR InterPro; IPR007638; Gln-tRNA-synth_Ib_RNA-bd_2.
DR InterPro; IPR007639; Gln-tRNA-synth_Ib_RNA-bd_N.
DR InterPro; IPR042558; Gln-tRNA-synth_Ib_RNA-bd_N_1.
DR InterPro; IPR042559; Gln-tRNA-synth_Ib_RNA-bd_N_2.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR Pfam; PF04558; tRNA_synt_1c_R1; 1.
DR Pfam; PF04557; tRNA_synt_1c_R2; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF50715; SSF50715; 1.
DR TIGRFAMs; TIGR00440; glnS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P47897"
FT CHAIN 2..775
FT /note="Glutamine--tRNA ligase"
FT /id="PRO_0000441173"
FT BINDING 271..273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 277..283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 303
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 438
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 457
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 486..487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT BINDING 494..496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00962"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P47897"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47897"
FT MOD_RES 309
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47897"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47897"
SQ SEQUENCE 775 AA; 87700 MW; C71804A23EA98DAD CRC64;
MATPDSLALF TGLGLSENKA RETLKNAALS TQLREAATQA QQTLGSTIDK ATGTLLYGLA
SRLRDTRRLS FLVGYIANKK IHTELQLSAA LEYVRSHPLD PIDTKDFEQE CGVGVVVTPE
QIEEAVEATI NRHRPQLLVE RYRFSMGLLM GEARAALRWA DGKMIKNEVD MQVLHLLGPK
MEADLEKKPK VAKARLEETD RKTAKDVVEN GEVAGQTLSL MEQLRGEALK FHKPGENYKT
PGYVTTPHTM DLLKQHLEIT GGQVRTRFPP EPNGILHIGH AKAINFNFGY AKANNGICFL
RFDDTNPEKE EAKFFTAIYD MVTWLGYTPY KVTYASDYFD QLYAWAVELI RRGQAYVCHQ
RGEELKGHNP LPSPWRDRPI EESLLLFEAM RKGKFAEGEA TLRMKLVMED GKMDPVAYRV
KYTPHHRTGD KWCIYPTYDY THCLCDSIEH ITHSLCTKEF QARRSSYFWL CNALDVYCPV
QWEYGRLNLH YAVVSKRKIL QLVAAGAVRD WDDPRLFTLT ALRRRGFPPE AINNFCARVG
VTVAQTTMEP HLLEACVRDV LNDTAPRAMA VLEPLQVVIT NFPAPKPLDI RVPNFPADET
KGFHQVPFAS TVFIERTDFK EESEPGYKRL AWGQPVGLRH TGYVIELQHV VRGSSGCVEC
LEVTCRRADA GEKPKAFIHW VSQPLVCEIR LYERLFQHKN PEDPVEVPGG FLSDLNPASL
QVIKGALVDC SVALAKPFDK FQFERLGYFS VDPDSHQGQV VFNRTVTLKE DPGKV
