MSTO1_HUMAN
ID MSTO1_HUMAN Reviewed; 570 AA.
AC Q9BUK6; Q53GR8; Q5CZ69; Q5T717; Q68CT6; Q7LBZ8; Q7Z3M7; Q7Z558; Q8TE05;
AC Q9NQX2; Q9NVU4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Protein misato homolog 1;
GN Name=MSTO1; ORFNames=LST005, SLTP005;
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 6).
RC TISSUE=Aorta;
RA Hui R.T., Liu B., Zhao B., Wang X.Y.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RC TISSUE=Testis;
RA Gu A.H., Xu Z.Y., Wang H., Xu M., Yin L.L.;
RT "Identification and characterization of a gene coding an alternative splice
RT of FLJ10504 in testis.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 7).
RC TISSUE=Spleen, and Teratocarcinoma;
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 2).
RC TISSUE=Liver;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Cerebellum, Endometrium, and Hippocampus;
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [MRNA] OF 16-570 (ISOFORM 1).
RC TISSUE=Heart;
RA Fong K.S.K., Fukushima D., de Couet H.G.;
RT "Human homologue of the Drosophila Misato gene.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17349998; DOI=10.1016/j.yexcr.2007.02.004;
RA Kimura M., Okano Y.;
RT "Human Misato regulates mitochondrial distribution and morphology.";
RL Exp. Cell Res. 313:1393-1404(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN MMYAT, VARIANT MMYAT MET-8,
RP AND CHARACTERIZATION OF VARIANT MMYAT MET-8.
RX PubMed=28554942; DOI=10.15252/emmm.201607058;
RA Gal A., Balicza P., Weaver D., Naghdi S., Joseph S.K., Varnai P.,
RA Gyuris T., Horvath A., Nagy L., Seifert E.L., Molnar M.J., Hajnoczky G.;
RT "MSTO1 is a cytoplasmic pro-mitochondrial fusion protein, whose mutation
RT induces myopathy and ataxia in humans.";
RL EMBO Mol. Med. 9:967-984(2017).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND VARIANTS MMYAT ILE-324; CYS-345 AND
RP LEU-376.
RX PubMed=28544275; DOI=10.1002/humu.23262;
RA Nasca A., Scotton C., Zaharieva I., Neri M., Selvatici R., Magnusson O.T.,
RA Gal A., Weaver D., Rossi R., Armaroli A., Pane M., Phadke R., Sarkozy A.,
RA Muntoni F., Hughes I., Cecconi A., Hajnoczky G., Donati A., Mercuri E.,
RA Zeviani M., Ferlini A., Ghezzi D.;
RT "Recessive mutations in MSTO1 cause mitochondrial dynamics impairment,
RT leading to myopathy and ataxia.";
RL Hum. Mutat. 38:970-977(2017).
CC -!- FUNCTION: Involved in the regulation of mitochondrial distribution and
CC morphology (PubMed:17349998, PubMed:28554942, PubMed:28544275).
CC Required for mitochondrial fusion and mitochondrial network formation
CC (PubMed:28554942, PubMed:28544275). {ECO:0000269|PubMed:17349998,
CC ECO:0000269|PubMed:28544275, ECO:0000269|PubMed:28554942}.
CC -!- INTERACTION:
CC Q9BUK6; Q8N4P3-2: HDDC3; NbExp=3; IntAct=EBI-2340176, EBI-12037393;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:17349998, ECO:0000269|PubMed:28554942}. Cytoplasm
CC {ECO:0000269|PubMed:28544275, ECO:0000269|PubMed:28554942}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q9BUK6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BUK6-2; Sequence=VSP_028056;
CC Name=3;
CC IsoId=Q9BUK6-3; Sequence=VSP_028054;
CC Name=4;
CC IsoId=Q9BUK6-4; Sequence=VSP_028051, VSP_028052;
CC Name=5;
CC IsoId=Q9BUK6-5; Sequence=VSP_028050, VSP_028056;
CC Name=6;
CC IsoId=Q9BUK6-6; Sequence=VSP_028049;
CC Name=7;
CC IsoId=Q9BUK6-7; Sequence=VSP_028053, VSP_028055;
CC -!- TISSUE SPECIFICITY: Present in all cell lines tested (at protein
CC level). Widely expressed. {ECO:0000269|PubMed:17349998}.
CC -!- DISEASE: Myopathy, mitochondrial, and ataxia (MMYAT) [MIM:617675]: A
CC neuromuscular disorder characterized by muscle weakness and atrophy,
CC ataxia, poor growth, delayed motor development, dysdiadochokinesia,
CC dysmetria and additional neurologic features. Some patients show
CC skeletal and endocrine anomalies, as well as behavioral psychiatric
CC manifestations. MMYAT transmission pattern is consistent with autosomal
CC dominant inheritance in some families, and autosomal recessive
CC inheritance in others. {ECO:0000269|PubMed:28544275,
CC ECO:0000269|PubMed:28554942}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the misato family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM12424.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF111708; AAM12424.1; ALT_FRAME; mRNA.
DR EMBL; AY334564; AAP94730.1; -; mRNA.
DR EMBL; AK001366; BAA91651.1; -; mRNA.
DR EMBL; AK092950; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK222863; BAD96583.1; -; mRNA.
DR EMBL; BX537684; CAD97810.1; -; mRNA.
DR EMBL; CR749791; CAH18652.1; -; mRNA.
DR EMBL; CR936872; CAI59784.1; -; Transcribed_RNA.
DR EMBL; AL353807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002535; AAH02535.1; -; mRNA.
DR EMBL; AF272833; AAF81794.1; -; mRNA.
DR CCDS; CCDS1114.1; -. [Q9BUK6-1]
DR RefSeq; NP_001243461.1; NM_001256532.1. [Q9BUK6-2]
DR RefSeq; NP_001243462.1; NM_001256533.1. [Q9BUK6-3]
DR RefSeq; NP_060586.2; NM_018116.3. [Q9BUK6-1]
DR RefSeq; XP_011508010.1; XM_011509708.1. [Q9BUK6-5]
DR RefSeq; XP_016857098.1; XM_017001609.1.
DR AlphaFoldDB; Q9BUK6; -.
DR BioGRID; 120457; 55.
DR IntAct; Q9BUK6; 25.
DR MINT; Q9BUK6; -.
DR STRING; 9606.ENSP00000245564; -.
DR GlyGen; Q9BUK6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BUK6; -.
DR PhosphoSitePlus; Q9BUK6; -.
DR BioMuta; MSTO1; -.
DR DMDM; 74752357; -.
DR EPD; Q9BUK6; -.
DR jPOST; Q9BUK6; -.
DR MassIVE; Q9BUK6; -.
DR MaxQB; Q9BUK6; -.
DR PaxDb; Q9BUK6; -.
DR PeptideAtlas; Q9BUK6; -.
DR PRIDE; Q9BUK6; -.
DR ProteomicsDB; 79098; -. [Q9BUK6-1]
DR ProteomicsDB; 79099; -. [Q9BUK6-2]
DR ProteomicsDB; 79100; -. [Q9BUK6-3]
DR ProteomicsDB; 79101; -. [Q9BUK6-4]
DR ProteomicsDB; 79102; -. [Q9BUK6-5]
DR ProteomicsDB; 79103; -. [Q9BUK6-6]
DR ProteomicsDB; 79104; -. [Q9BUK6-7]
DR Antibodypedia; 35210; 114 antibodies from 23 providers.
DR DNASU; 55154; -.
DR Ensembl; ENST00000245564.8; ENSP00000245564.3; ENSG00000125459.17. [Q9BUK6-1]
DR Ensembl; ENST00000368341.8; ENSP00000357325.4; ENSG00000125459.17. [Q9BUK6-7]
DR Ensembl; ENST00000490743.5; ENSP00000476353.1; ENSG00000125459.17. [Q9BUK6-4]
DR GeneID; 55154; -.
DR KEGG; hsa:55154; -.
DR MANE-Select; ENST00000245564.8; ENSP00000245564.3; NM_018116.4; NP_060586.2.
DR UCSC; uc001fky.5; human. [Q9BUK6-1]
DR CTD; 55154; -.
DR DisGeNET; 55154; -.
DR GeneCards; MSTO1; -.
DR HGNC; HGNC:29678; MSTO1.
DR HPA; ENSG00000125459; Low tissue specificity.
DR MalaCards; MSTO1; -.
DR MIM; 617619; gene.
DR MIM; 617675; phenotype.
DR neXtProt; NX_Q9BUK6; -.
DR Orphanet; 502423; Mitochondrial myopathy-cerebellar ataxia-pigmentary retinopathy syndrome.
DR PharmGKB; PA142671313; -.
DR VEuPathDB; HostDB:ENSG00000125459; -.
DR eggNOG; KOG2530; Eukaryota.
DR GeneTree; ENSGT00530000064067; -.
DR HOGENOM; CLU_184878_0_0_1; -.
DR InParanoid; Q9BUK6; -.
DR OMA; EILTFQF; -.
DR OrthoDB; 1321917at2759; -.
DR PhylomeDB; Q9BUK6; -.
DR TreeFam; TF323669; -.
DR PathwayCommons; Q9BUK6; -.
DR SignaLink; Q9BUK6; -.
DR BioGRID-ORCS; 55154; 454 hits in 1074 CRISPR screens.
DR ChiTaRS; MSTO1; human.
DR GeneWiki; MSTO1; -.
DR GenomeRNAi; 55154; -.
DR Pharos; Q9BUK6; Tbio.
DR PRO; PR:Q9BUK6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BUK6; protein.
DR Bgee; ENSG00000125459; Expressed in left testis and 93 other tissues.
DR ExpressionAtlas; Q9BUK6; baseline and differential.
DR Genevisible; Q9BUK6; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0048311; P:mitochondrion distribution; IMP:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR029209; DML1/Misato_tubulin.
DR InterPro; IPR019605; Misato_II_tubulin-like.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR Pfam; PF10644; Misat_Tub_SegII; 1.
DR Pfam; PF14881; Tubulin_3; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Disease variant; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..570
FT /note="Protein misato homolog 1"
FT /id="PRO_0000304626"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..388
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_028049"
FT VAR_SEQ 1..178
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_028050"
FT VAR_SEQ 98..99
FT /note="QG -> EC (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_028051"
FT VAR_SEQ 100..570
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_028052"
FT VAR_SEQ 105..139
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028053"
FT VAR_SEQ 489..500
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_028054"
FT VAR_SEQ 489..499
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028055"
FT VAR_SEQ 499
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|Ref.2, ECO:0000303|Ref.4"
FT /id="VSP_028056"
FT VARIANT 8
FT /note="V -> M (in MMYAT; autosomal dominant; patient cells
FT show decreased mitochondrial fusion and mitochondrial
FT network formation; patient cells show increased
FT mitochondria aggregation and fragmentation;
FT dbSNP:rs762798018)"
FT /evidence="ECO:0000269|PubMed:28554942"
FT /id="VAR_079889"
FT VARIANT 324
FT /note="T -> I (in MMYAT; unknown pathological significance;
FT dbSNP:rs622288)"
FT /evidence="ECO:0000269|PubMed:28544275"
FT /id="VAR_035046"
FT VARIANT 345
FT /note="R -> C (in MMYAT; unknown pathological significance;
FT dbSNP:rs749922789)"
FT /evidence="ECO:0000269|PubMed:28544275"
FT /id="VAR_079890"
FT VARIANT 376
FT /note="F -> L (in MMYAT; unknown pathological significance;
FT dbSNP:rs1553295536)"
FT /evidence="ECO:0000269|PubMed:28544275"
FT /id="VAR_079891"
FT CONFLICT 389
FT /note="M -> V (in Ref. 3; BAA91651)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="F -> S (in Ref. 3; AK092950)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="Q -> P (in Ref. 5; CAI59784)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 570 AA; 61835 MW; A139748AF2798619 CRC64;
MAGGAREVLT LQLGHFAGFV GAHWWNQQDA ALGRATDSKE PPGELCPDVL YRTGRTLHGQ
ETYTPRLILM DLKGSLSSLK EEGGLYRDKQ LDAAIAWQGK LTTHKEELYP KNPYLQDFLS
AEGVLSSDGV WRVKSIPNGK GSSPLPTATT PKPLIPTEAS IRVWSDFLRV HLHPRSICMI
QKYNHDGEAG RLEAFGQGES VLKEPKYQEE LEDRLHFYVE ECDYLQGFQI LCDLHDGFSG
VGAKAAELLQ DEYSGRGIIT WGLLPGPYHR GEAQRNIYRL LNTAFGLVHL TAHSSLVCPL
SLGGSLGLRP EPPVSFPYLH YDATLPFHCS AILATALDTV TVPYRLCSSP VSMVHLADML
SFCGKKVVTA GAIIPFPLAP GQSLPDSLMQ FGGATPWTPL SACGEPSGTR CFAQSVVLRG
IDRACHTSQL TPGTPPPSAL HACTTGEEIL AQYLQQQQPG VMSSSHLLLT PCRVAPPYPH
LFSSCSPPGM VLDGSPKGAA VESIPVFGAL CSSSSLHQTL EALARDLTKL DLRRWASFMD
AGVEHDDVAE LLQELQSLAQ CYQGGDSLVD
