MTO1_HUMAN
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 03-AUG-2022, entry version 187.
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; 88.
DR IntAct; Q9Y2Z2; 25.
DR MINT; Q9Y2Z2; -.
DR STRING; 9606.ENSP00000402038; -.
DR iPTMnet; Q9Y2Z2; -.
DR PhosphoSitePlus; Q9Y2Z2; -.
DR BioMuta; MTO1; -.
DR DMDM; 20981712; -.
DR EPD; Q9Y2Z2; -.
DR jPOST; Q9Y2Z2; -.
DR MassIVE; Q9Y2Z2; -.
DR MaxQB; Q9Y2Z2; -.
DR PeptideAtlas; Q9Y2Z2; -.
DR PRIDE; 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 Antibodypedia; 31347; 98 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 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; FRPGYAI; -.
DR OrthoDB; 1437708at2759; -.
DR PhylomeDB; Q9Y2Z2; -.
DR TreeFam; TF354240; -.
DR BioCyc; MetaCyc:ENSG00000135297-MON; -.
DR PathwayCommons; Q9Y2Z2; -.
DR Reactome; R-HSA-6787450; tRNA modification in the mitochondrion.
DR SignaLink; Q9Y2Z2; -.
DR BioGRID-ORCS; 25821; 91 hits in 1082 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 193 other tissues.
DR ExpressionAtlas; Q9Y2Z2; baseline and differential.
DR Genevisible; Q9Y2Z2; HS.
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 GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
DR Gene3D; 1.10.150.570; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR004416; MnmG.
DR InterPro; IPR002218; MnmG-rel.
DR InterPro; IPR020595; MnmG-rel_CS.
DR InterPro; IPR026904; MnmG_C.
DR InterPro; IPR044920; MnmG_C_subdom.
DR InterPro; IPR040131; MnmG_N.
DR PANTHER; PTHR11806; PTHR11806; 1.
DR PANTHER; PTHR11806:SF0; PTHR11806:SF0; 1.
DR Pfam; PF01134; GIDA; 1.
DR Pfam; PF13932; GIDA_C; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS01280; GIDA_1; 1.
DR PROSITE; PS01281; GIDA_2; 1.
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