ID   MTO1_HUMAN              Reviewed;         717 AA.
AC   Q9Y2Z2; B3KQB5; Q5SWL2; Q5SWL3; Q5SWL4; Q8NDN7; Q8WZ57; Q96FE6; Q9BS06;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2002, sequence version 2.
DT   27-MAR-2024, entry version 196.
DE   RecName: Full=Protein MTO1 homolog, mitochondrial;
DE   Flags: Precursor;
GN   Name=MTO1; ORFNames=CGI-02;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3 AND 5),
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12011058; DOI=10.1074/jbc.m203267200;
RA   Li X.M., Li R.H., Lin X., Guan M.-X.;
RT   "Isolation and characterization of the putative nuclear modifier gene MTO1
RT   involved in the pathogenesis of deafness-associated mitochondrial 12 S rRNA
RT   A1555G mutation.";
RL   J. Biol. Chem. 277:27256-27264(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RX   PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA   Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT   "Identification of novel human genes evolutionarily conserved in
RT   Caenorhabditis elegans by comparative proteomics.";
RL   Genome Res. 10:703-713(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   TISSUE=Embryo;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC   TISSUE=Spleen;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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   [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6).
RC   TISSUE=Lymph, and Placenta;
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-717 (ISOFORM 5).
RC   TISSUE=Uterus;
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   [9]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT LYS-533, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Colon carcinoma;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [10]
RP   VARIANT COXPD10 THR-453.
RX   PubMed=22608499; DOI=10.1016/j.ajhg.2012.04.011;
RA   Ghezzi D., Baruffini E., Haack T.B., Invernizzi F., Melchionda L.,
RA   Dallabona C., Strom T.M., Parini R., Burlina A.B., Meitinger T.,
RA   Prokisch H., Ferrero I., Zeviani M.;
RT   "Mutations of the mitochondrial-tRNA modifier MTO1 cause hypertrophic
RT   cardiomyopathy and lactic acidosis.";
RL   Am. J. Hum. Genet. 90:1079-1087(2012).
CC   -!- FUNCTION: Involved in the 5-carboxymethylaminomethyl modification
CC       (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs.
CC       {ECO:0000269|PubMed:12011058}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=3; Synonyms=4;
CC         IsoId=Q9Y2Z2-1; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q9Y2Z2-2; Sequence=VSP_001749, VSP_001751;
CC       Name=2;
CC         IsoId=Q9Y2Z2-3; Sequence=VSP_001750;
CC       Name=5;
CC         IsoId=Q9Y2Z2-4; Sequence=VSP_001751;
CC       Name=6;
CC         IsoId=Q9Y2Z2-5; Sequence=VSP_001748;
CC       Name=7;
CC         IsoId=Q9Y2Z2-6; Sequence=VSP_040985, VSP_040986;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed in various tissues, but with
CC       a markedly elevated expression in tissues of high metabolic rates
CC       including cochlea. {ECO:0000269|PubMed:12011058}.
CC   -!- DISEASE: Combined oxidative phosphorylation deficiency 10 (COXPD10)
CC       [MIM:614702]: An autosomal recessive disorder resulting in variable
CC       defects of mitochondrial oxidative respiration. Affected individuals
CC       present in infancy with hypertrophic cardiomyopathy and lactic
CC       acidosis. The severity is variable, but can be fatal in the most severe
CC       cases. {ECO:0000269|PubMed:22608499}. Note=The disease is caused by
CC       variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the MnmG family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD27712.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAH05808.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF469110; AAL82394.1; -; mRNA.
DR   EMBL; AF469111; AAL82395.1; -; mRNA.
DR   EMBL; AF442963; AAL35894.1; -; Genomic_DNA.
DR   EMBL; AF319422; AAG42814.3; -; mRNA.
DR   EMBL; AY078986; AAL85491.1; -; mRNA.
DR   EMBL; AY078985; AAL85490.1; -; mRNA.
DR   EMBL; AF132937; AAD27712.1; ALT_FRAME; mRNA.
DR   EMBL; AK074625; BAG51977.1; -; mRNA.
DR   EMBL; AK225828; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AL603910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471051; EAW48762.1; -; Genomic_DNA.
DR   EMBL; BC005808; AAH05808.2; ALT_INIT; mRNA.
DR   EMBL; BC011051; AAH11051.2; -; mRNA.
DR   EMBL; AL833823; CAD38685.1; -; mRNA.
DR   CCDS; CCDS34485.1; -. [Q9Y2Z2-4]
DR   CCDS; CCDS47452.1; -. [Q9Y2Z2-6]
DR   CCDS; CCDS4979.1; -. [Q9Y2Z2-1]
DR   RefSeq; NP_001116698.1; NM_001123226.1. [Q9Y2Z2-6]
DR   RefSeq; NP_036255.2; NM_012123.3. [Q9Y2Z2-4]
DR   RefSeq; NP_598400.1; NM_133645.2. [Q9Y2Z2-1]
DR   AlphaFoldDB; Q9Y2Z2; -.
DR   SMR; Q9Y2Z2; -.
DR   BioGRID; 117349; 92.
DR   IntAct; Q9Y2Z2; 26.
DR   MINT; Q9Y2Z2; -.
DR   STRING; 9606.ENSP00000402038; -.
DR   GlyGen; Q9Y2Z2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9Y2Z2; -.
DR   PhosphoSitePlus; Q9Y2Z2; -.
DR   SwissPalm; Q9Y2Z2; -.
DR   BioMuta; MTO1; -.
DR   DMDM; 20981712; -.
DR   EPD; Q9Y2Z2; -.
DR   jPOST; Q9Y2Z2; -.
DR   MassIVE; Q9Y2Z2; -.
DR   MaxQB; Q9Y2Z2; -.
DR   PaxDb; 9606-ENSP00000402038; -.
DR   PeptideAtlas; Q9Y2Z2; -.
DR   ProteomicsDB; 85942; -. [Q9Y2Z2-1]
DR   ProteomicsDB; 85943; -. [Q9Y2Z2-2]
DR   ProteomicsDB; 85944; -. [Q9Y2Z2-3]
DR   ProteomicsDB; 85945; -. [Q9Y2Z2-4]
DR   ProteomicsDB; 85946; -. [Q9Y2Z2-5]
DR   ProteomicsDB; 85947; -. [Q9Y2Z2-6]
DR   Pumba; Q9Y2Z2; -.
DR   Antibodypedia; 31347; 117 antibodies from 24 providers.
DR   DNASU; 25821; -.
DR   Ensembl; ENST00000370300.8; ENSP00000359323.4; ENSG00000135297.17. [Q9Y2Z2-1]
DR   Ensembl; ENST00000370305.5; ENSP00000359328.1; ENSG00000135297.17. [Q9Y2Z2-5]
DR   Ensembl; ENST00000415954.6; ENSP00000402038.2; ENSG00000135297.17. [Q9Y2Z2-6]
DR   Ensembl; ENST00000498286.6; ENSP00000419561.2; ENSG00000135297.17. [Q9Y2Z2-4]
DR   GeneID; 25821; -.
DR   KEGG; hsa:25821; -.
DR   MANE-Select; ENST00000498286.6; ENSP00000419561.2; NM_012123.4; NP_036255.2. [Q9Y2Z2-4]
DR   UCSC; uc003pgy.5; human. [Q9Y2Z2-1]
DR   AGR; HGNC:19261; -.
DR   CTD; 25821; -.
DR   DisGeNET; 25821; -.
DR   GeneCards; MTO1; -.
DR   HGNC; HGNC:19261; MTO1.
DR   HPA; ENSG00000135297; Low tissue specificity.
DR   MalaCards; MTO1; -.
DR   MIM; 614667; gene.
DR   MIM; 614702; phenotype.
DR   neXtProt; NX_Q9Y2Z2; -.
DR   OpenTargets; ENSG00000135297; -.
DR   Orphanet; 314637; Mitochondrial hypertrophic cardiomyopathy with lactic acidosis due to MTO1 deficiency.
DR   PharmGKB; PA134974199; -.
DR   VEuPathDB; HostDB:ENSG00000135297; -.
DR   eggNOG; KOG2311; Eukaryota.
DR   GeneTree; ENSGT00390000011297; -.
DR   HOGENOM; CLU_007831_2_2_1; -.
DR   InParanoid; Q9Y2Z2; -.
DR   OMA; CNPAMGG; -.
DR   OrthoDB; 5486689at2759; -.
DR   PhylomeDB; Q9Y2Z2; -.
DR   TreeFam; TF354240; -.
DR   BioCyc; MetaCyc:ENSG00000135297-MONOMER; -.
DR   PathwayCommons; Q9Y2Z2; -.
DR   Reactome; R-HSA-6787450; tRNA modification in the mitochondrion.
DR   SignaLink; Q9Y2Z2; -.
DR   BioGRID-ORCS; 25821; 94 hits in 1161 CRISPR screens.
DR   ChiTaRS; MTO1; human.
DR   GeneWiki; MTO1; -.
DR   GenomeRNAi; 25821; -.
DR   Pharos; Q9Y2Z2; Tbio.
DR   PRO; PR:Q9Y2Z2; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9Y2Z2; Protein.
DR   Bgee; ENSG00000135297; Expressed in germinal epithelium of ovary and 195 other cell types or tissues.
DR   ExpressionAtlas; Q9Y2Z2; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0070899; P:mitochondrial tRNA wobble uridine modification; IBA:GO_Central.
DR   GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR   Gene3D; 2.40.30.260; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 1.10.150.570; GidA associated domain, C-terminal subdomain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR049312; GIDA_C_N.
DR   InterPro; IPR002218; MnmG-rel.
DR   InterPro; IPR020595; MnmG-rel_CS.
DR   InterPro; IPR026904; MnmG_C.
DR   InterPro; IPR047001; MnmG_C_subdom.
DR   InterPro; IPR044920; MnmG_C_subdom_sf.
DR   InterPro; IPR040131; MnmG_N.
DR   PANTHER; PTHR11806; GLUCOSE INHIBITED DIVISION PROTEIN A; 1.
DR   PANTHER; PTHR11806:SF0; PROTEIN MTO1 HOMOLOG, MITOCHONDRIAL; 1.
DR   Pfam; PF01134; GIDA; 1.
DR   Pfam; PF13932; GIDA_C; 1.
DR   Pfam; PF21680; GIDA_C_1st; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SMART; SM01228; GIDA_assoc_3; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS01280; GIDA_1; 1.
DR   PROSITE; PS01281; GIDA_2; 1.
DR   Genevisible; Q9Y2Z2; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cardiomyopathy; Disease variant; FAD; Flavoprotein;
KW   Methylation; Mitochondrion; Primary mitochondrial disease;
KW   Reference proteome; Transit peptide; tRNA processing.
FT   TRANSIT         1..25
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..717
FT                   /note="Protein MTO1 homolog, mitochondrial"
FT                   /id="PRO_0000042688"
FT   BINDING         43..48
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         533
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   VAR_SEQ         1..74
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_001748"
FT   VAR_SEQ         179..275
FT                   /note="Missing (in isoform 1)"
FT                   /evidence="ECO:0000303|PubMed:12011058"
FT                   /id="VSP_001749"
FT   VAR_SEQ         314..717
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12011058"
FT                   /id="VSP_001750"
FT   VAR_SEQ         376..400
FT                   /note="Missing (in isoform 7)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_040985"
FT   VAR_SEQ         377..401
FT                   /note="Missing (in isoform 1 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:10810093,
FT                   ECO:0000303|PubMed:12011058, ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT                   /id="VSP_001751"
FT   VAR_SEQ         444
FT                   /note="A -> AQTECCSVARLECSDMISQLQAILLPQPSLVAGTAGMHHNT (in
FT                   isoform 7)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_040986"
FT   VARIANT         453
FT                   /note="A -> T (in COXPD10; dbSNP:rs143747297)"
FT                   /evidence="ECO:0000269|PubMed:22608499"
FT                   /id="VAR_068693"
FT   CONFLICT        300
FT                   /note="H -> Q (in Ref. 1; AAL82394/AAL82395 and 2;
FT                   AAD27712)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        586..587
FT                   /note="LA -> CT (in Ref. 1; AAL35894)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   717 AA;  79964 MW;  78F84D8833BC0ED3 CRC64;
     MFYFRGCGRW VAVSFTKQQF PLARLSSDSA APRTPHFDVI VIGGGHAGTE AATAAARCGS
     RTLLLTHRVD TIGQMSCNPS FGGIGKGHLM REVDALDGLC SRICDQSGVH YKVLNRRKGP
     AVWGLRAQID RKLYKQNMQK EILNTPLLTV QEGAVEDLIL TEPEPEHTGK CRVSGVVLVD
     GSTVYAESVI LTTGTFLRGM IVIGLETHPA GRLGDQPSIG LAQTLEKLGF VVGRLKTGTP
     PRIAKESINF SILNKHIPDN PSIPFSFTNE TVWIKPEDQL PCYLTHTNPR VDEIVLKNLH
     LNSHVKETTR GPRYCPSIES KVLRFPNRLH QVWLEPEGMD SDLIYPQGLS MTLPAELQEK
     MITCIRGLEK AKVIQPDGVL LLLPRMECNG AISAHHNLPL PGYGVQYDYL DPRQITPSLE
     THLVQRLFFA GQINGTTGYE EAAAQGVIAG INASLRVSRK PPFVVSRTEG YIGVLIDDLT
     TLGTSEPYRM FTSRVEFRLS LRPDNADSRL TLRGYKDAGC VSQQRYERAC WMKSSLEEGI
     SVLKSIEFLS SKWKKLIPEA SISTSRSLPV RALDVLKYEE VDMDSLAKAV PEPLKKYTKC
     RELAERLKIE ATYESVLFHQ LQEIKGVQQD EALQLPKDLD YLTIRDVSLS HEVREKLHFS
     RPQTIGAASR IPGVTPAAII NLLRFVKTTQ RRQSAMNESS KTDQYLCDAD RLQEREL
//