ID SYVM_HUMAN Reviewed; 1063 AA. AC Q5ST30; A2ABL7; B4DET4; B4E3P5; F5GXJ0; F5H323; Q2M2A0; Q59FI1; Q5SQ96; AC Q5SS98; Q6DKJ5; Q6ZV24; Q96GN2; Q96H77; Q96Q02; Q9H6R2; Q9UFH7; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 24-JAN-2024, entry version 171. DE RecName: Full=Valine--tRNA ligase, mitochondrial; DE EC=6.1.1.9 {ECO:0000269|PubMed:24827421}; DE AltName: Full=Valyl-tRNA synthetase; DE Short=ValRS; DE AltName: Full=Valyl-tRNA synthetase-like; DE Flags: Precursor; GN Name=VARS2; Synonyms=KIAA1885, VARS2L, VARSL; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-1049. RC TISSUE=Brain; RX PubMed=11572484; DOI=10.1093/dnares/8.4.179; RA Nagase T., Kikuno R., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XXI. The RT complete sequences of 60 new cDNA clones from brain which code for large RT proteins."; RL DNA Res. 8:179-187(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 416-1063 (ISOFORM 1), AND VARIANTS ARG-449; RP LEU-680; GLN-917 AND THR-965. RC TISSUE=Cerebellum, Thalamus, and Uterus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ARG-449; RP LEU-680 AND THR-965. RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS ARG-449; RP LEU-680; GLN-917; THR-965 AND GLN-1049. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ARG-449; RP LEU-680; GLN-917; THR-965 AND GLN-1049. RC TISSUE=Brain, Eye, and Skin; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 748-1063 (ISOFORM 1), AND VARIANT RP THR-965. RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] RP INVOLVEMENT IN COXPD20, VARIANT COXPD20 ILE-337, CHARACTERIZATION OF RP VARIANT COXPD20 ILE-337, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=24827421; DOI=10.1002/humu.22590; RA Diodato D., Melchionda L., Haack T.B., Dallabona C., Baruffini E., RA Donnini C., Granata T., Ragona F., Balestri P., Margollicci M., RA Lamantea E., Nasca A., Powell C.A., Minczuk M., Strom T.M., Meitinger T., RA Prokisch H., Lamperti C., Zeviani M., Ghezzi D.; RT "VARS2 and TARS2 mutations in patients with mitochondrial RT encephalomyopathies."; RL Hum. Mutat. 35:983-989(2014). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [10] RP VARIANTS COXPD20 THR-349 AND ASP-596. RX PubMed=25058219; DOI=10.1001/jama.2014.7184; RA Taylor R.W., Pyle A., Griffin H., Blakely E.L., Duff J., He L., RA Smertenko T., Alston C.L., Neeve V.C., Best A., Yarham J.W., Kirschner J., RA Schara U., Talim B., Topaloglu H., Baric I., Holinski-Feder E., Abicht A., RA Czermin B., Kleinle S., Morris A.A., Vassallo G., Gorman G.S., Ramesh V., RA Turnbull D.M., Santibanez-Koref M., McFarland R., Horvath R., RA Chinnery P.F.; RT "Use of whole-exome sequencing to determine the genetic basis of multiple RT mitochondrial respiratory chain complex deficiencies."; RL JAMA 312:68-77(2014). CC -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val) in a two-step CC reaction: valine is first activated by ATP to form Val-AMP and then CC transferred to the acceptor end of tRNA(Val). CC {ECO:0000269|PubMed:24827421}. 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 Evidence={ECO:0000269|PubMed:24827421}; CC -!- INTERACTION: CC Q5ST30; Q8IZP0-5: ABI1; NbExp=3; IntAct=EBI-2116622, EBI-11743294; CC Q5ST30; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-2116622, EBI-11096309; CC Q5ST30; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-2116622, EBI-742038; CC Q5ST30; O43639: NCK2; NbExp=3; IntAct=EBI-2116622, EBI-713635; CC Q5ST30; O60504: SORBS3; NbExp=3; IntAct=EBI-2116622, EBI-741237; CC Q5ST30-3; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-10244969, EBI-2548702; CC Q5ST30-3; Q969L2: MAL2; NbExp=3; IntAct=EBI-10244969, EBI-944295; CC Q5ST30-4; Q9NYB9: ABI2; NbExp=3; IntAct=EBI-10244997, EBI-743598; CC Q5ST30-4; O43639: NCK2; NbExp=3; IntAct=EBI-10244997, EBI-713635; CC Q5ST30-4; O60504: SORBS3; NbExp=3; IntAct=EBI-10244997, EBI-741237; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q5ST30-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5ST30-2; Sequence=VSP_034032; CC Name=3; CC IsoId=Q5ST30-3; Sequence=VSP_045483; CC Name=4; CC IsoId=Q5ST30-4; Sequence=VSP_046102; CC -!- DISEASE: Combined oxidative phosphorylation deficiency 20 (COXPD20) CC [MIM:615917]: A disorder due to mitochondrial respiratory chain complex CC defects. Clinical features are variable and include muscle weakness CC with hypotonia, central neurological disease with progressive external CC ophthalmoplegia, ptosis and ataxia, delayed psychomotor development, CC cardiomyopathy, abnormal liver function, facial dysmorphism, CC microcephaly and epilepsy. {ECO:0000269|PubMed:24827421, CC ECO:0000269|PubMed:25058219}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB15191.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB67778.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAD92716.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB067472; BAB67778.1; ALT_INIT; mRNA. DR EMBL; AK025618; BAB15191.1; ALT_INIT; mRNA. DR EMBL; AK125069; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK293780; BAG57195.1; -; mRNA. DR EMBL; AK304807; BAG65557.1; -; mRNA. DR EMBL; AB209479; BAD92716.1; ALT_SEQ; Transcribed_RNA. DR EMBL; AL662854; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL669830; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL773541; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX927194; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759747; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR936875; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC008844; AAH08844.2; -; mRNA. DR EMBL; BC009355; AAH09355.2; -; mRNA. DR EMBL; BC073838; AAH73838.1; -; mRNA. DR EMBL; BC112054; AAI12055.1; -; mRNA. DR EMBL; BC113605; AAI13606.1; -; mRNA. DR EMBL; AL122037; CAB59177.1; -; mRNA. DR CCDS; CCDS34387.1; -. [Q5ST30-1] DR CCDS; CCDS54981.1; -. [Q5ST30-3] DR RefSeq; NP_001161205.1; NM_001167733.2. [Q5ST30-3] DR RefSeq; NP_001161206.1; NM_001167734.1. [Q5ST30-4] DR RefSeq; NP_065175.4; NM_020442.5. [Q5ST30-1] DR AlphaFoldDB; Q5ST30; -. DR SMR; Q5ST30; -. DR BioGRID; 121426; 115. DR IntAct; Q5ST30; 22. DR MINT; Q5ST30; -. DR STRING; 9606.ENSP00000441000; -. DR iPTMnet; Q5ST30; -. DR PhosphoSitePlus; Q5ST30; -. DR BioMuta; VARS2; -. DR DMDM; 296452917; -. DR EPD; Q5ST30; -. DR jPOST; Q5ST30; -. DR MassIVE; Q5ST30; -. DR MaxQB; Q5ST30; -. DR PaxDb; 9606-ENSP00000441000; -. DR PeptideAtlas; Q5ST30; -. DR ProteomicsDB; 24437; -. DR ProteomicsDB; 26145; -. DR ProteomicsDB; 63892; -. [Q5ST30-1] DR ProteomicsDB; 63893; -. [Q5ST30-2] DR Pumba; Q5ST30; -. DR Antibodypedia; 45126; 66 antibodies from 17 providers. DR DNASU; 57176; -. DR Ensembl; ENST00000321897.9; ENSP00000316092.5; ENSG00000137411.19. [Q5ST30-1] DR Ensembl; ENST00000415079.6; ENSP00000400867.2; ENSG00000223494.11. [Q5ST30-1] DR Ensembl; ENST00000541562.6; ENSP00000441000.2; ENSG00000137411.19. [Q5ST30-1] DR Ensembl; ENST00000546854.5; ENSP00000446839.1; ENSG00000223494.11. [Q5ST30-4] DR Ensembl; ENST00000625423.2; ENSP00000485818.1; ENSG00000137411.19. [Q5ST30-3] DR Ensembl; ENST00000676266.1; ENSP00000502585.1; ENSG00000137411.19. [Q5ST30-1] DR GeneID; 57176; -. DR KEGG; hsa:57176; -. DR MANE-Select; ENST00000676266.1; ENSP00000502585.1; NM_020442.6; NP_065175.4. DR UCSC; uc003nsc.3; human. [Q5ST30-1] DR AGR; HGNC:21642; -. DR CTD; 57176; -. DR DisGeNET; 57176; -. DR GeneCards; VARS2; -. DR HGNC; HGNC:21642; VARS2. DR HPA; ENSG00000137411; Low tissue specificity. DR MalaCards; VARS2; -. DR MIM; 612802; gene. DR MIM; 615917; phenotype. DR neXtProt; NX_Q5ST30; -. DR OpenTargets; ENSG00000137411; -. DR PharmGKB; PA164742816; -. DR VEuPathDB; HostDB:ENSG00000137411; -. DR eggNOG; KOG0432; Eukaryota. DR GeneTree; ENSGT00940000159890; -. DR InParanoid; Q5ST30; -. DR OMA; RQWYIRN; -. DR OrthoDB; 5473263at2759; -. DR PhylomeDB; Q5ST30; -. DR TreeFam; TF354250; -. DR PathwayCommons; Q5ST30; -. DR Reactome; R-HSA-379726; Mitochondrial tRNA aminoacylation. DR SignaLink; Q5ST30; -. DR SIGNOR; Q5ST30; -. DR BioGRID-ORCS; 57176; 438 hits in 1160 CRISPR screens. DR ChiTaRS; VARS2; human. DR GenomeRNAi; 57176; -. DR Pharos; Q5ST30; Tbio. DR PRO; PR:Q5ST30; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q5ST30; Protein. DR Bgee; ENSG00000137411; Expressed in right hemisphere of cerebellum and 96 other cell types or tissues. DR ExpressionAtlas; Q5ST30; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. 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; IMP:UniProtKB. DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central. DR CDD; cd07962; Anticodon_Ia_Val; 1. DR CDD; cd00817; ValRS_core; 1. DR Gene3D; 3.40.50.620; HUPs; 2. DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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 NCBIfam; TIGR00422; valS; 1. DR PANTHER; PTHR11946:SF71; VALINE--TRNA LIGASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 1. DR PRINTS; PR00986; TRNASYNTHVAL. DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. DR Genevisible; Q5ST30; HS. PE 1: Evidence at protein level; KW Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding; KW Disease variant; Ligase; Mitochondrion; Nucleotide-binding; KW Primary mitochondrial disease; Protein biosynthesis; Reference proteome; KW Transit peptide. FT TRANSIT 1..26 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 27..1063 FT /note="Valine--tRNA ligase, mitochondrial" FT /id="PRO_0000338000" FT REGION 25..53 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 146..156 FT /note="'HIGH' region" FT MOTIF 658..662 FT /note="'KMSKS' region" FT COMPBIAS 38..53 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 661 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT VAR_SEQ 1..644 FT /note="MPHLPLASFRPPFWGLRHSRGLPRFHSVSTQSEPHGSPISRRNREAKQKRLR FT EKQATLEAEIAGESKSPAESIKAWRPKELVLYEIPTKPGEKKDVSGPLPPAYSPRYVEA FT AWYPWWVREGFFKPEYQARLPQATGETFSMCIPPPNVTGSLHIGHALTVAIQDALVRWH FT RMRGDQVLWVPGSDHAGIATQAVVEKQLWKERGVRRHELSREAFLREVWQWKEAKGGEI FT CEQLRALGASLDWDRECFTMDVGSSVAVTEAFVRLYKAGLLYRNHQLVNWSCALRSAIS FT DIEVENRPLPGHTQLRLPGCPTPVSFGLLFSVAFPVDGEPDAEVVVGTTRPETLPGDVA FT VAVHPDDSRYTHLHGRQLRHPLMGQPLPLITDYAVQPHVGTGAVKVTPAHSPADAEMGA FT RHGLSPLNVIAEDGTMTSLCGDWLQGLHRFVAREKIMSVLSEWGLFRGLQNHPMVLPIC FT SRSGDVIEYLLKNQWFVRCQEMGARAAKAVESGALELSPSFHQKNWQHWFSHIGDWCVS FT RQLWWGHQIPAYLVVEDHAQGEEDCWVVGRSEAEAREVAAELTGRPGAELTLERDPDVL FT DTWFSSALFPFSALGWPQETPDLARFYPLSLLETGSDLLLFWVGRMVMLGTQLTGQLPF FT SK -> MVFFCPVPLFCPGLAPRDPRPCSFLPPVTFGNGQRPSAVLGGPHGHVGDPAHR FT AAALQQVWRPEIPRHLQGNPPLLTPPCPQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_034032" FT VAR_SEQ 1..140 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045483" FT VAR_SEQ 1 FT /note="M -> MGGKAWPRRAVGTAGGPCAEQISAPFQTLLM (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046102" FT VARIANT 26 FT /note="H -> Y (in dbSNP:rs6926224)" FT /id="VAR_052651" FT VARIANT 64 FT /note="G -> R (in dbSNP:rs6926723)" FT /id="VAR_043730" FT VARIANT 337 FT /note="T -> I (in COXPD20; decreased levels of the protein; FT decreased valine-tRNA ligase activity; dbSNP:rs587777585)" FT /evidence="ECO:0000269|PubMed:24827421" FT /id="VAR_071850" FT VARIANT 349 FT /note="A -> T (in COXPD20; dbSNP:rs587777583)" FT /evidence="ECO:0000269|PubMed:25058219" FT /id="VAR_071851" FT VARIANT 449 FT /note="W -> R (in dbSNP:rs2249464)" FT /evidence="ECO:0000269|PubMed:14574404, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334, FT ECO:0000269|Ref.3" FT /id="VAR_043731" FT VARIANT 596 FT /note="A -> D (in COXPD20; dbSNP:rs587777584)" FT /evidence="ECO:0000269|PubMed:25058219" FT /id="VAR_071852" FT VARIANT 680 FT /note="V -> L (in dbSNP:rs2074506)" FT /evidence="ECO:0000269|PubMed:14574404, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334, FT ECO:0000269|Ref.3" FT /id="VAR_043732" FT VARIANT 765 FT /note="V -> M (in dbSNP:rs55865499)" FT /id="VAR_061910" FT VARIANT 917 FT /note="R -> Q (in dbSNP:rs9394021)" FT /evidence="ECO:0000269|PubMed:14574404, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334" FT /id="VAR_043733" FT VARIANT 965 FT /note="A -> T (in dbSNP:rs2252863)" FT /evidence="ECO:0000269|PubMed:14574404, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:17974005, ECO:0000269|Ref.3" FT /id="VAR_043734" FT VARIANT 1049 FT /note="R -> Q (in dbSNP:rs4678)" FT /evidence="ECO:0000269|PubMed:11572484, FT ECO:0000269|PubMed:14574404, ECO:0000269|PubMed:15489334" FT /id="VAR_043735" FT CONFLICT 25 FT /note="F -> S (in Ref. 2; BAG65557)" FT /evidence="ECO:0000305" FT CONFLICT 156 FT /note="H -> R (in Ref. 2; BAG57195)" FT /evidence="ECO:0000305" FT CONFLICT 985 FT /note="E -> G (in Ref. 2; BAB15191)" FT /evidence="ECO:0000305" FT CONFLICT 1060 FT /note="S -> G (in Ref. 2; BAG65557)" FT /evidence="ECO:0000305" SQ SEQUENCE 1063 AA; 118490 MW; 0212C6361A87DF8B CRC64; MPHLPLASFR PPFWGLRHSR GLPRFHSVST QSEPHGSPIS RRNREAKQKR LREKQATLEA EIAGESKSPA ESIKAWRPKE LVLYEIPTKP GEKKDVSGPL PPAYSPRYVE AAWYPWWVRE GFFKPEYQAR LPQATGETFS MCIPPPNVTG SLHIGHALTV AIQDALVRWH RMRGDQVLWV PGSDHAGIAT QAVVEKQLWK ERGVRRHELS REAFLREVWQ WKEAKGGEIC EQLRALGASL DWDRECFTMD VGSSVAVTEA FVRLYKAGLL YRNHQLVNWS CALRSAISDI EVENRPLPGH TQLRLPGCPT PVSFGLLFSV AFPVDGEPDA EVVVGTTRPE TLPGDVAVAV HPDDSRYTHL HGRQLRHPLM GQPLPLITDY AVQPHVGTGA VKVTPAHSPA DAEMGARHGL SPLNVIAEDG TMTSLCGDWL QGLHRFVARE KIMSVLSEWG LFRGLQNHPM VLPICSRSGD VIEYLLKNQW FVRCQEMGAR AAKAVESGAL ELSPSFHQKN WQHWFSHIGD WCVSRQLWWG HQIPAYLVVE DHAQGEEDCW VVGRSEAEAR EVAAELTGRP GAELTLERDP DVLDTWFSSA LFPFSALGWP QETPDLARFY PLSLLETGSD LLLFWVGRMV MLGTQLTGQL PFSKVLLHPM VRDRQGRKMS KSLGNVLDPR DIISGVEMQV LQEKLRSGNL DPAELAIVAA AQKKDFPHGI PECGTDALRF TLCSHGVQAG DLHLSVSEVQ SCRHFCNKIW NALRFILNAL GEKFVPQPAE ELSPSSPMDA WILSRLALAA QECERGFLTR ELSLVTHALH HFWLHNLCDV YLEAVKPVLW HSPRPLGPPQ VLFSCADLGL RLLAPLMPFL AEELWQRLPP RPGCPPAPSI SVAPYPSACS LEHWRQPELE RRFSRVQEVV QVLRALRATY QLTKARPRVL LQSSEPGDQG LFEAFLEPLG TLGYCGAVGL LPPGAAAPSG WAQAPLSDTA QVYMELQGLV DPQIQLPLLA ARRYKLQKQL DSLTARTPSE GEAGTQRQQK LSSLQLELSK LDKAASHLRQ LMDEPPAPGS PEL //