SYWM_HUMAN
ID SYWM_HUMAN Reviewed; 360 AA.
AC Q9UGM6; B1ALR1; B2R9D4; Q53FT4; Q5VUD2; Q86TQ0;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Tryptophan--tRNA ligase, mitochondrial;
DE EC=6.1.1.2;
DE AltName: Full=(Mt)TrpRS;
DE AltName: Full=Tryptophanyl-tRNA synthetase;
DE Short=TrpRS;
DE Flags: Precursor;
GN Name=WARS2;
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 [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
RX PubMed=10828066; DOI=10.1074/jbc.275.22.16820;
RA Jorgensen R., Soegaard T.M.M., Rossing A.B., Martensen P.M., Justesen J.;
RT "Identification and characterization of human mitochondrial tryptophanyl-
RT tRNA synthetase.";
RL J. Biol. Chem. 275:16820-16826(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
RC TISSUE=Kidney proximal tubule;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP SER-50.
RC 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 [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 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 [9] {ECO:0007744|PDB:5EKD}
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 18-360 IN COMPLEX WITH ATP;
RP MANGANESE AND SUBSTRATE ANALOG.
RA Williams T.L., Carter C.W.;
RT "Binding of Mg2+ATP Enhances Inhibition of Human Mitochondrial
RT Tryptophanyl-tRNA Synthetase by Indolmycin.";
RL Submitted (NOV-2015) to the PDB data bank.
RN [10]
RP FUNCTION, INVOLVEMENT IN NEMMLAS, AND VARIANTS NEMMLAS LEU-100 DEL AND
RP MET-313.
RX PubMed=28650581; DOI=10.1002/ajmg.a.38339;
RA Theisen B.E., Rumyantseva A., Cohen J.S., Alcaraz W.A., Shinde D.N.,
RA Tang S., Srivastava S., Pevsner J., Trifunovic A., Fatemi A.;
RT "Deficiency of WARS2, encoding mitochondrial tryptophanyl tRNA synthetase,
RT causes severe infantile onset leukoencephalopathy.";
RL Am. J. Med. Genet. A 173:2505-2510(2017).
RN [11]
RP INVOLVEMENT IN NEMMLAS, AND VARIANTS NEMMLAS VAL-45; GLN-77; LEU-178;
RP MET-313; LEU-349 AND LYS-352.
RX PubMed=28905505; DOI=10.1002/humu.23340;
RA Wortmann S.B., Timal S., Venselaar H., Wintjes L.T., Kopajtich R.,
RA Feichtinger R.G., Onnekink C., Muehlmeister M., Brandt U., Smeitink J.A.,
RA Veltman J.A., Sperl W., Lefeber D., Pruijn G., Stojanovic V.,
RA Freisinger P., V Spronsen F., Derks T.G., Veenstra-Knol H.E., Mayr J.A.,
RA Roetig A., Tarnopolsky M., Prokisch H., Rodenburg R.J.;
RT "Biallelic variants in WARS2 encoding mitochondrial tryptophanyl-tRNA
RT synthase in six individuals with mitochondrial encephalopathy.";
RL Hum. Mutat. 38:1786-1795(2017).
RN [12]
RP VARIANT NEMMLAS GLY-13, CHARACTERIZATION OF VARIANT NEMMLAS GLY-13,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INVOLVEMENT IN NEMMLAS.
RX PubMed=28236339; DOI=10.1002/humu.23205;
RA Musante L., Puettmann L., Kahrizi K., Garshasbi M., Hu H., Stehr H.,
RA Lipkowitz B., Otto S., Jensen L.R., Tzschach A., Jamali P., Wienker T.,
RA Najmabadi H., Ropers H.H., Kuss A.W.;
RT "Mutations of the aminoacyl-tRNA-synthetases SARS and WARS2 are implicated
RT in the aetiology of autosomal recessive intellectual disability.";
RL Hum. Mutat. 38:621-636(2017).
CC -!- FUNCTION: Mitochondrial aminoacyl-tRNA synthetase that activate and
CC transfer the amino acids to their corresponding tRNAs during the
CC translation of mitochondrial genes and protein synthesis.
CC {ECO:0000305|PubMed:28650581}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-
CC tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671,
CC Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:28236339}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UGM6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UGM6-2; Sequence=VSP_041414, VSP_041415;
CC -!- TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:28236339}.
CC -!- DISEASE: Neurodevelopmental disorder, mitochondrial, with abnormal
CC movements and lactic acidosis, with or without seizures (NEMMLAS)
CC [MIM:617710]: An autosomal recessive, mitochondrial disorder with a
CC broad phenotypic spectrum ranging from severe neonatal lactic acidosis,
CC encephalomyopathy and early death to an attenuated course with milder
CC manifestations. Clinical features include delayed psychomotor
CC development, intellectual disability, hypotonia, dystonia, ataxia, and
CC spasticity. Severe combined respiratory chain deficiency may be found
CC in severely affected individuals. {ECO:0000269|PubMed:28236339,
CC ECO:0000269|PubMed:28650581, ECO:0000269|PubMed:28905505}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AJ242739; CAB63107.1; -; mRNA.
DR EMBL; AK223197; BAD96917.1; -; mRNA.
DR EMBL; AK313740; BAG36481.1; -; mRNA.
DR EMBL; AL359823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56693.1; -; Genomic_DNA.
DR EMBL; BC044575; AAH44575.1; -; mRNA.
DR EMBL; BC039889; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS30817.1; -. [Q9UGM6-2]
DR CCDS; CCDS900.1; -. [Q9UGM6-1]
DR RefSeq; NP_056651.1; NM_015836.3. [Q9UGM6-1]
DR RefSeq; NP_957715.1; NM_201263.2. [Q9UGM6-2]
DR PDB; 5EKD; X-ray; 1.82 A; A/B=18-360.
DR PDBsum; 5EKD; -.
DR AlphaFoldDB; Q9UGM6; -.
DR SMR; Q9UGM6; -.
DR BioGRID; 115633; 29.
DR IntAct; Q9UGM6; 6.
DR STRING; 9606.ENSP00000235521; -.
DR DrugBank; DB00150; Tryptophan.
DR GlyGen; Q9UGM6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UGM6; -.
DR PhosphoSitePlus; Q9UGM6; -.
DR BioMuta; WARS2; -.
DR DMDM; 21362967; -.
DR EPD; Q9UGM6; -.
DR jPOST; Q9UGM6; -.
DR MassIVE; Q9UGM6; -.
DR MaxQB; Q9UGM6; -.
DR PaxDb; Q9UGM6; -.
DR PeptideAtlas; Q9UGM6; -.
DR PRIDE; Q9UGM6; -.
DR ProteomicsDB; 84244; -. [Q9UGM6-1]
DR ProteomicsDB; 84245; -. [Q9UGM6-2]
DR Antibodypedia; 33903; 74 antibodies from 27 providers.
DR DNASU; 10352; -.
DR Ensembl; ENST00000235521.5; ENSP00000235521.4; ENSG00000116874.12. [Q9UGM6-1]
DR Ensembl; ENST00000369426.9; ENSP00000358434.5; ENSG00000116874.12. [Q9UGM6-2]
DR GeneID; 10352; -.
DR KEGG; hsa:10352; -.
DR MANE-Select; ENST00000235521.5; ENSP00000235521.4; NM_015836.4; NP_056651.1.
DR UCSC; uc001ehm.4; human. [Q9UGM6-1]
DR CTD; 10352; -.
DR DisGeNET; 10352; -.
DR GeneCards; WARS2; -.
DR HGNC; HGNC:12730; WARS2.
DR HPA; ENSG00000116874; Low tissue specificity.
DR MalaCards; WARS2; -.
DR MIM; 604733; gene.
DR MIM; 617710; phenotype.
DR neXtProt; NX_Q9UGM6; -.
DR OpenTargets; ENSG00000116874; -.
DR Orphanet; 572798; WARS2-related combined oxidative phosphorylation defect.
DR PharmGKB; PA37341; -.
DR VEuPathDB; HostDB:ENSG00000116874; -.
DR eggNOG; KOG2713; Eukaryota.
DR GeneTree; ENSGT00940000153724; -.
DR HOGENOM; CLU_029244_3_0_1; -.
DR InParanoid; Q9UGM6; -.
DR OMA; GWGQFKP; -.
DR OrthoDB; 1298726at2759; -.
DR PhylomeDB; Q9UGM6; -.
DR TreeFam; TF314321; -.
DR BRENDA; 6.1.1.2; 2681.
DR PathwayCommons; Q9UGM6; -.
DR Reactome; R-HSA-379726; Mitochondrial tRNA aminoacylation.
DR SignaLink; Q9UGM6; -.
DR BioGRID-ORCS; 10352; 229 hits in 1105 CRISPR screens.
DR ChiTaRS; WARS2; human.
DR GeneWiki; WARS2; -.
DR GenomeRNAi; 10352; -.
DR Pharos; Q9UGM6; Tbio.
DR PRO; PR:Q9UGM6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UGM6; protein.
DR Bgee; ENSG00000116874; Expressed in bronchial epithelial cell and 143 other tissues.
DR Genevisible; Q9UGM6; HS.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0070183; P:mitochondrial tryptophanyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR CDD; cd00806; TrpRS_core; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00140_B; Trp_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002306; Trp-tRNA-ligase.
DR InterPro; IPR024109; Trp-tRNA-ligase_bac-type.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01039; TRNASYNTHTRP.
DR TIGRFAMs; TIGR00233; trpS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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..18
FT /note="Mitochondrion"
FT CHAIN 19..360
FT /note="Tryptophan--tRNA ligase, mitochondrial"
FT /id="PRO_0000035828"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:5EKD"
FT BINDING 48..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:5EKD"
FT BINDING 167
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0007744|PDB:5EKD"
FT BINDING 179..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:5EKD"
FT BINDING 217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:5EKD"
FT BINDING 226..230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:5EKD"
FT VAR_SEQ 212..220
FT /note="TSMKKVKSL -> SMCVLVFLT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041414"
FT VAR_SEQ 221..360
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041415"
FT VARIANT 13
FT /note="W -> G (in NEMMLAS; impaired mitochondrial
FT localization; dbSNP:rs139548132)"
FT /evidence="ECO:0000269|PubMed:28236339"
FT /id="VAR_078435"
FT VARIANT 45
FT /note="G -> V (in NEMMLAS; dbSNP:rs1553241795)"
FT /evidence="ECO:0000269|PubMed:28905505"
FT /id="VAR_079734"
FT VARIANT 50
FT /note="G -> S (in dbSNP:rs11552864)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_028848"
FT VARIANT 77
FT /note="H -> Q (in NEMMLAS; unknown pathological
FT significance; dbSNP:rs766501807)"
FT /evidence="ECO:0000269|PubMed:28905505"
FT /id="VAR_079735"
FT VARIANT 100
FT /note="Missing (in NEMMLAS; dbSNP:rs772867219)"
FT /evidence="ECO:0000269|PubMed:28650581"
FT /id="VAR_079736"
FT VARIANT 178
FT /note="V -> L (in NEMMLAS; dbSNP:rs912133959)"
FT /evidence="ECO:0000269|PubMed:28905505"
FT /id="VAR_079737"
FT VARIANT 267
FT /note="A -> P (in dbSNP:rs3790549)"
FT /id="VAR_020217"
FT VARIANT 313
FT /note="K -> M (in NEMMLAS; dbSNP:rs145867327)"
FT /evidence="ECO:0000269|PubMed:28650581,
FT ECO:0000269|PubMed:28905505"
FT /id="VAR_079738"
FT VARIANT 349
FT /note="V -> L (in NEMMLAS; dbSNP:rs1170780314)"
FT /evidence="ECO:0000269|PubMed:28905505"
FT /id="VAR_079739"
FT VARIANT 352
FT /note="E -> K (in NEMMLAS; unknown pathological
FT significance; dbSNP:rs563341344)"
FT /evidence="ECO:0000269|PubMed:28905505"
FT /id="VAR_079740"
FT VARIANT 360
FT /note="L -> P (in dbSNP:rs17023101)"
FT /id="VAR_052407"
FT CONFLICT 151
FT /note="H -> R (in Ref. 3; BAD96917)"
FT /evidence="ECO:0000305"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:5EKD"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:5EKD"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:5EKD"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:5EKD"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:5EKD"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:5EKD"
FT HELIX 85..102
FT /evidence="ECO:0007829|PDB:5EKD"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:5EKD"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:5EKD"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:5EKD"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:5EKD"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:5EKD"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:5EKD"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:5EKD"
FT HELIX 155..169
FT /evidence="ECO:0007829|PDB:5EKD"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:5EKD"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:5EKD"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:5EKD"
FT HELIX 183..200
FT /evidence="ECO:0007829|PDB:5EKD"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:5EKD"
FT TURN 213..216
FT /evidence="ECO:0007829|PDB:5EKD"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:5EKD"
FT HELIX 244..253
FT /evidence="ECO:0007829|PDB:5EKD"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:5EKD"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:5EKD"
FT HELIX 287..293
FT /evidence="ECO:0007829|PDB:5EKD"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:5EKD"
FT HELIX 299..324
FT /evidence="ECO:0007829|PDB:5EKD"
FT HELIX 328..357
FT /evidence="ECO:0007829|PDB:5EKD"
SQ SEQUENCE 360 AA; 40147 MW; 8C80DF6FCA214A91 CRC64;
MALHSMRKAR ERWSFIRALH KGSAAAPALQ KDSKKRVFSG IQPTGILHLG NYLGAIESWV
RLQDEYDSVL YSIVDLHSIT VPQDPAVLRQ SILDMTAVLL ACGINPEKSI LFQQSQVSEH
TQLSWILSCM VRLPRLQHLH QWKAKTTKQK HDGTVGLLTY PVLQAADILL YKSTHVPVGE
DQVQHMELVQ DLAQGFNKKY GEFFPVPESI LTSMKKVKSL RDPSAKMSKS DPDKLATVRI
TDSPEEIVQK FRKAVTDFTS EVTYDPAGRA GVSNIVAVHA AVTGLSVEEV VRRSAGMNTA
RYKLAVADAV IEKFAPIKRE IEKLKLDKDH LEKVLQIGSA KAKELAYTVC QEVKKLVGFL
