SYVC_MOUSE
ID SYVC_MOUSE Reviewed; 1263 AA.
AC Q9Z1Q9; Q9QUN2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Valine--tRNA ligase;
DE EC=6.1.1.9;
DE AltName: Full=Protein G7a;
DE AltName: Full=Valyl-tRNA synthetase;
DE Short=ValRS;
GN Name=Vars1; Synonyms=Bat6, G7a, Vars, Vars2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=BALB/cJ, and C57BL/RIJ; TISSUE=Brain;
RX PubMed=10199925; DOI=10.1007/s002510050522;
RA Snoek M., van Vugt H.;
RT "The sequence and organization of the mouse valyl-tRNA synthetase gene
RT G7a/Bat6 located in the MHC class III region.";
RL Immunogenetics 49:468-470(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129;
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-
CC tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-
CC COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
CC -!- ACTIVITY REGULATION: Can be regulated by protein kinase C-dependent
CC phosphorylation. {ECO:0000250}.
CC -!- SUBUNIT: Forms high-molecular-mass aggregates with elongation factor 1.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AF087680; AAD26532.1; -; mRNA.
DR EMBL; AF087141; AAD26531.1; -; Genomic_DNA.
DR EMBL; AF109905; AAC84151.1; -; Genomic_DNA.
DR EMBL; AF109906; AAC84172.1; -; Genomic_DNA.
DR CCDS; CCDS37593.1; -.
DR RefSeq; NP_035820.3; NM_011690.3.
DR RefSeq; XP_017172884.1; XM_017317395.1.
DR AlphaFoldDB; Q9Z1Q9; -.
DR SMR; Q9Z1Q9; -.
DR BioGRID; 204498; 24.
DR IntAct; Q9Z1Q9; 4.
DR STRING; 10090.ENSMUSP00000084572; -.
DR iPTMnet; Q9Z1Q9; -.
DR PhosphoSitePlus; Q9Z1Q9; -.
DR SwissPalm; Q9Z1Q9; -.
DR EPD; Q9Z1Q9; -.
DR jPOST; Q9Z1Q9; -.
DR MaxQB; Q9Z1Q9; -.
DR PaxDb; Q9Z1Q9; -.
DR PRIDE; Q9Z1Q9; -.
DR ProteomicsDB; 262923; -.
DR Antibodypedia; 51277; 188 antibodies from 27 providers.
DR DNASU; 22321; -.
DR Ensembl; ENSMUST00000087315; ENSMUSP00000084572; ENSMUSG00000007029.
DR GeneID; 22321; -.
DR KEGG; mmu:22321; -.
DR UCSC; uc008cez.2; mouse.
DR CTD; 22321; -.
DR MGI; MGI:90675; Vars.
DR VEuPathDB; HostDB:ENSMUSG00000007029; -.
DR eggNOG; KOG0432; Eukaryota.
DR eggNOG; KOG0867; Eukaryota.
DR GeneTree; ENSGT00940000157775; -.
DR HOGENOM; CLU_001493_0_1_1; -.
DR InParanoid; Q9Z1Q9; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 229591at2759; -.
DR PhylomeDB; Q9Z1Q9; -.
DR TreeFam; TF300648; -.
DR BioGRID-ORCS; 22321; 24 hits in 75 CRISPR screens.
DR ChiTaRS; Vars; mouse.
DR PRO; PR:Q9Z1Q9; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9Z1Q9; protein.
DR Bgee; ENSMUSG00000007029; Expressed in spermatid and 192 other tissues.
DR ExpressionAtlas; Q9Z1Q9; baseline and differential.
DR Genevisible; Q9Z1Q9; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004832; F:valine-tRNA ligase activity; ISO:MGI.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR Gene3D; 1.10.287.380; -; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_02004; Val_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033705; Anticodon_Ia_Val.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR PANTHER; PTHR11946; PTHR11946; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00422; valS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Ligase;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P26640"
FT CHAIN 2..1263
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106254"
FT DOMAIN 89..219
FT /note="GST C-terminal"
FT REGION 218..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 343..353
FT /note="'HIGH' region"
FT MOTIF 861..865
FT /note="'KMSKS' region"
FT COMPBIAS 233..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 864
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P26640"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26640"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26640"
FT MOD_RES 644
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26640"
FT CONFLICT 959
FT /note="A -> R (in Ref. 1; AAD26532/AAD26531)"
FT /evidence="ECO:0000305"
FT CONFLICT 1219
FT /note="E -> K (in Ref. 1; AAD26532/AAD26531)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1263 AA; 140215 MW; B510E73284FCE26D CRC64;
MSILYVSPHP DAFPSLRALI AARYGEAGDG PGWGGPHPRI CLQPPPSSRT PFPPPRLPAL
EQGPGGLWVW GAPAVAQLLW PAGLGGPGGS RAAVLVQQWV SYADTELIPA ACGATLPALG
LRGPGQDPQA ALGALGKALN PLEDWLRLHT YLAGDAPTLA DLAAVTALLL PFRYVLDPSA
RRIWGNVTRW FNTCVRQPEF RAVLGEVALY SGARSVTQQP GSEVIAPQKT PAQLKKEAKK
REKLEKFQQK QKTQQQPPHG EKKPKPEKKE KRDPGVITYD LPTPPGEKKD VSGAMPDSYS
PQYVEAAWYP WWERQGFFKP EYGRPSVSAP NPRGVFMMCI PPPNVTGSLH LGHALTNAIQ
DSLTRWHRMR GETTLWNPGC DHAGIATQVV VEKKLWKERG LNRHQLGREA FLEEVWKWKA
EKGDRIYHQL KKLGSSLDWD RACFTMDPKL SATVTEAFVR LHEEGVIYRS TRLVNWSCTL
NSAISDIEVD KKELTGRTLL PVPGYKEKVE FGVLVSFAYK VQGSDSDEEV VVATTRIETM
LGDVAVAVHP KDPRYQHLKG KCVVHPFLSR SLPIVFDDFV DMEFGTGAVK ITPAHDQNDY
EVGQRHRLEA ISIMDSKGAL INVPPPFLGL PRFEARKAVL AALKERGLFR GVKDNPMVVP
LCNRSKDVVE PLLRPQWYVR CGEMAQAASA AVTRGDLRIL PEAHQRTWHS WMDNIRDWCI
SRQLWWGHRI PAYFITVHDP AVPPGEDPDG RYWVSGRTEA EAREKAAREF GVSPDKISLQ
QDEDVLDTWF SSGLFPFSIF GWPNQSEDLS VFYPGTLLET GHDILFFWVA RMVMLGLKLT
GKLPFREVYL HAIVRDAHGR KMSKSLGNVI DPLDVIHGVS LQGLYDQLLN SNLDPSEVEK
AKEGQKADFP AGIPECGTDA LRFGLCAYTS QGRDINLDVN RILGYRHFCN KLWNATKFAL
RGLGKGFVPS ATSKPEGHES LVDRWIRSRL TEAVRLSNEG FQAYDFPAIT TAQYSFWLYE
LCDVYLECLK PVLNGVDQVA AECARQTLYT CLDVGLRLLS PFMPFVTEEL FQRLPRRTPK
APASLCVTPY PEPSECSWKD PEAEAALELA LSITRAVRSL RADYNLTRTR PDCFLEVADE
ATGALASAVS GYVQALASAG VVAVLALGAP APQGCAVAVA SDRCSIHLQL QGLVDPAREL
GKLQAKRSEA QRQAQRLQER RAASSYSAKV PLEVQEADEA KLQQTEAELR KVDEAIALFQ
KML
