SYVM_HUMAN
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 03-AUG-2022, entry version 163.
DE RecName: Full=Valine--tRNA ligase, mitochondrial;
DE EC=6.1.1.9;
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, AND CHARACTERIZATION OF
RP VARIANT COXPD20 ILE-337.
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 -!- 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 -!- 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};
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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; CCDS54980.1; -. [Q5ST30-4]
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; 110.
DR IntAct; Q5ST30; 21.
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; Q5ST30; -.
DR PeptideAtlas; Q5ST30; -.
DR PRIDE; Q5ST30; -.
DR ProteomicsDB; 24437; -.
DR ProteomicsDB; 26145; -.
DR ProteomicsDB; 63892; -. [Q5ST30-1]
DR ProteomicsDB; 63893; -. [Q5ST30-2]
DR Antibodypedia; 45126; 61 antibodies from 17 providers.
DR DNASU; 57176; -.
DR Ensembl; ENST00000321897.9; ENSP00000316092.5; ENSG00000137411.19. [Q5ST30-1]
DR Ensembl; ENST00000541562.6; ENSP00000441000.2; ENSG00000137411.19. [Q5ST30-1]
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 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; HNIKSHF; -.
DR PhylomeDB; Q5ST30; -.
DR TreeFam; TF354250; -.
DR PathwayCommons; Q5ST30; -.
DR Reactome; R-HSA-379726; Mitochondrial tRNA aminoacylation.
DR SignaLink; Q5ST30; -.
DR BioGRID-ORCS; 57176; 407 hits in 1080 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 94 other tissues.
DR ExpressionAtlas; Q5ST30; baseline and differential.
DR Genevisible; Q5ST30; HS.
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; 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 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 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
