SYVM_MOUSE
ID SYVM_MOUSE Reviewed; 1060 AA.
AC Q3U2A8; E9QMJ4; Q69Z78; Q6PGG3; Q6ZQL7; Q8BIN9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Valine--tRNA ligase, mitochondrial;
DE EC=6.1.1.9;
DE AltName: Full=Valyl-tRNA synthetase;
DE Short=ValRS;
DE Flags: Precursor;
GN Name=Vars2; Synonyms=Kiaa1885, Vars2l;
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 [LARGE SCALE MRNA].
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kanehori K., Ishibashi T., Chiba Y., Fujimori K., Hiraoka S., Tanai H.,
RA Watanabe S., Ishida S., Ono Y., Hotuta T., Watanabe M., Sugiyama T.,
RA Irie R., Otsuki T., Sato H., Ota T., Wakamatsu A., Ishii S., Yamamoto J.,
RA Isono Y., Kawai-Hio Y., Saito K., Nishikawa T., Kimura K., Matsuo K.,
RA Nakamura Y., Sekine M., Kikuchi H., Kanda K., Wagatsuma M.,
RA Takahashi-Fujii A., Oshima A., Sugiyama A., Kawakami B., Suzuki Y.,
RA Sugano S., Nagahari K., Masuho Y., Nagai K., Isogai T.;
RT "NEDO cDNA sequencing project.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 395-1060.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-548, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC29932.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD32566.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD32566.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA.; Evidence={ECO:0000305};
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DR EMBL; AK173288; BAD32566.1; ALT_SEQ; Transcribed_RNA.
DR EMBL; AK038117; BAC29932.1; ALT_INIT; mRNA.
DR EMBL; AK155386; BAE33234.1; -; mRNA.
DR EMBL; AK129008; BAC87668.1; -; mRNA.
DR EMBL; CR974483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057036; AAH57036.2; -; mRNA.
DR CCDS; CCDS37602.1; -.
DR RefSeq; NP_780346.3; NM_175137.4.
DR AlphaFoldDB; Q3U2A8; -.
DR SMR; Q3U2A8; -.
DR BioGRID; 213111; 5.
DR STRING; 10090.ENSMUSP00000047917; -.
DR iPTMnet; Q3U2A8; -.
DR PhosphoSitePlus; Q3U2A8; -.
DR EPD; Q3U2A8; -.
DR MaxQB; Q3U2A8; -.
DR PaxDb; Q3U2A8; -.
DR PeptideAtlas; Q3U2A8; -.
DR PRIDE; Q3U2A8; -.
DR ProteomicsDB; 262924; -.
DR Antibodypedia; 45126; 61 antibodies from 17 providers.
DR DNASU; 68915; -.
DR Ensembl; ENSMUST00000043674; ENSMUSP00000047917; ENSMUSG00000038838.
DR GeneID; 68915; -.
DR KEGG; mmu:68915; -.
DR UCSC; uc008cie.2; mouse.
DR CTD; 57176; -.
DR MGI; MGI:1916165; Vars2.
DR VEuPathDB; HostDB:ENSMUSG00000038838; -.
DR eggNOG; KOG0432; Eukaryota.
DR GeneTree; ENSGT00940000159890; -.
DR HOGENOM; CLU_001493_0_1_1; -.
DR InParanoid; Q3U2A8; -.
DR OMA; HNIKSHF; -.
DR OrthoDB; 229591at2759; -.
DR PhylomeDB; Q3U2A8; -.
DR TreeFam; TF354250; -.
DR BioGRID-ORCS; 68915; 27 hits in 74 CRISPR screens.
DR PRO; PR:Q3U2A8; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q3U2A8; protein.
DR Bgee; ENSMUSG00000038838; Expressed in animal zygote and 192 other tissues.
DR ExpressionAtlas; Q3U2A8; baseline and differential.
DR Genevisible; Q3U2A8; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033705; Anticodon_Ia_Val.
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; 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; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00422; valS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..15
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 16..1060
FT /note="Valine--tRNA ligase, mitochondrial"
FT /id="PRO_0000338002"
FT REGION 25..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 146..156
FT /note="'HIGH' region"
FT MOTIF 659..663
FT /note="'KMSKS' region"
FT BINDING 662
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 548
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 57
FT /note="A -> V (in Ref. 1; BAD32566 and 3; BAC87668)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="M -> V (in Ref. 1; BAD32566 and 3; BAC87668/
FT BAE33234)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="E -> L (in Ref. 1; BAD32566 and 3; BAC87668)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="R -> H (in Ref. 1; BAD32566 and 3; BAC87668)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="Q -> R (in Ref. 3; BAC87668)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="I -> M (in Ref. 1; BAD32566 and 3; BAC87668)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="H -> R (in Ref. 3; BAC87668)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="Q -> R (in Ref. 1; BAD32566 and 3; BAC87668)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="L -> R (in Ref. 1; BAD32566 and 3; BAC87668/
FT BAE33234)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="H -> R (in Ref. 1; BAD32566 and 3; BAC87668)"
FT /evidence="ECO:0000305"
FT CONFLICT 889
FT /note="T -> A (in Ref. 1; BAD32566 and 3; BAC87668/
FT BAE33234)"
FT /evidence="ECO:0000305"
FT CONFLICT 896
FT /note="R -> H (in Ref. 3; BAC87668)"
FT /evidence="ECO:0000305"
FT CONFLICT 944
FT /note="Missing (in Ref. 3; BAC87668)"
FT /evidence="ECO:0000305"
FT CONFLICT 975
FT /note="T -> A (in Ref. 1; BAD32566 and 3; BAC87668/
FT BAE33234)"
FT /evidence="ECO:0000305"
FT CONFLICT 1019
FT /note="M -> V (in Ref. 3; BAE33234)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1060 AA; 118461 MW; C0CBFF593F54E657 CRC64;
MPHLPLASFR PPLWGLRPSW GLSRPQALCT QPEPHGSPVS RRNREAKQKR LREKQAALEA
GLAEKSKIPA VPTKAWSHKE VVLYEIPTGP GEKKDVSGPL PPAYSPQYVE AAWYQWWVRE
GFFKPEYQAR LPQATGETFS MCIPPPNVTG SLHIGHALTV AIQDALVRWH RMRGDRVLWI
PGSDHAGIAT QAMVEKQLWK EQRVRRHELS REDFLRAVWQ WKHEKGGEIY EQLCALGASL
DWDRECFTMD AGSSAAVTEA FVRLYNSGLL YRNRQLVNWS CTLRSAISDI EVESRPLPGR
TVLQLPGCPT PVSFGLLASV AFPVDGEPDT EIVVGTTRPE TLPGDVAVAV HPDDPRYTHL
HGRQLRHPLT GQLLPLITDT TVQPHVGTGA VKVTPAHSPI DAEIGTRHGL TPLSVIAEDG
TMTSLCGDWL QGLHRFVARE KIMCTLREQG LFRGLQEHPM VLPICSRSGD VVEYLLKSQW
FVRCQEMGDL AAKAVESGAL ELWPSFHQKS WQHWFAHIGD WCVSRQLWWG HQIPAYRVIG
ENAEDDRKEC WVVGRSEAEA RAVAAKRTGR PEAELTLERD PDVLDTWFSS ALFPFSALGW
PRETPDLAHF YPLTLLETGS DLLMFWVGRM VMLGTQLTGQ LPFSKVLLHS MVRDRQGRKM
SKSLGNVLDP RDIISGQELQ VLQAKLRDGN LDPGELAVAA AAQKKDFPYG IPECGTDALR
FALCSHGILG GDLHLSVSEV LNYRHFCNKL WNALRFVLRA LGDNFVPQPA EEVTPSSPMD
AWILSRLAFA ASECERGFLS RELSLVTHTL YHFWLHNLCD VYLEAVKPVL SSVPRPPGPP
QVLFSCADVG LRLLAPLMPF LAEELWQRLP PRPGGPLAPS ICVAPYPSTR SLEFWRQPEL
ERCFSRVQEV VQALRALRAT YQLTKARPQV LLQCSDPGEQ GLVQPFLEPL GILSHCGAVG
FLSPGAAAPS GWALTPLGDT MKIYMELQGL VDPQSQLPRL TARRQKLQKQ LDDLLNRTMS
EGLAERQQRI SSLHLELSKL DQAASYLQQL MDEAPSAREL
