ID   MYORG_HUMAN             Reviewed;         714 AA.
AC   Q6NSJ0; Q5T587; Q5T588; Q9ULQ9;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Myogenesis-regulating glycosidase {ECO:0000312|HGNC:HGNC:19918};
DE            EC=3.2.1.-;
DE   AltName: Full=Uncharacterized family 31 glucosidase KIAA1161;
GN   Name=MYORG {ECO:0000312|HGNC:HGNC:19918}; Synonyms=KIAA1161;
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 GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ILE-4 AND GLU-53.
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-714, AND VARIANT GLU-53.
RC   TISSUE=Brain;
RX   PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA   Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT   "Characterization of cDNA clones selected by the GeneMark analysis from
RT   size-fractionated cDNA libraries from human brain.";
RL   DNA Res. 6:329-336(1999).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-250.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [5]
RP   SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF ASP-463.
RX   PubMed=19706595; DOI=10.1074/jbc.m109.034041;
RA   Datta K., Guan T., Gerace L.;
RT   "NET37, a nuclear envelope transmembrane protein with glycosidase homology,
RT   is involved in myoblast differentiation.";
RL   J. Biol. Chem. 284:29666-29676(2009).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [7]
RP   SUBCELLULAR LOCATION, INVOLVEMENT IN IBGC7, AND VARIANTS IBGC7 VAL-35;
RP   75-TRP--SER-714 DEL; LEU-ALA-PHE-ARG-116 INS; 203-GLN--SER-714 DEL;
RP   LEU-232; LEU-261; 365-PHE-ASP-366 DEL; GLY-441 AND 443-TRP--SER-714 DEL.
RX   PubMed=29910000; DOI=10.1016/j.neuron.2018.05.037;
RA   Yao X.P., Cheng X., Wang C., Zhao M., Guo X.X., Su H.Z., Lai L.L.,
RA   Zou X.H., Chen X.J., Zhao Y., Dong E.L., Lu Y.Q., Wu S., Li X., Fan G.,
RA   Yu H., Xu J., Wang N., Xiong Z.Q., Chen W.J.;
RT   "Biallelic mutations in MYORG cause autosomal recessive primary familial
RT   brain calcification.";
RL   Neuron 98:1116-1123(2018).
RN   [8]
RP   INVOLVEMENT IN IBGC7, AND VARIANT IBGC7 ASP-354 DEL.
RX   PubMed=30656188; DOI=10.1002/acn3.684;
RA   Arkadir D., Lossos A., Rahat D., Abu Snineh M., Schueler-Furman O.,
RA   Nitschke S., Minassian B.A., Sadaka Y., Lerer I., Tabach Y., Meiner V.;
RT   "MYORG is associated with recessive primary familial brain calcification.";
RL   Ann. Clin. Transl. Neurol. 6:106-113(2019).
RN   [9]
RP   INVOLVEMENT IN IBGC7, AND VARIANTS IBGC7 GLU-64; ARG-113;
RP   LEU-ALA-PHE-ARG-116 INS; ALA-236 INS; CYS-249; ASP-373; HIS-434;
RP   445-GLN--SER-714 DEL; ASN-476; SER-513 DEL; TRP-611; PRO-622; THR-656 AND
RP   GLN-660.
RX   PubMed=31009047; DOI=10.1093/brain/awz095;
RG   French PFBC study group;
RA   Grangeon L., Wallon D., Charbonnier C., Quenez O., Richard A.C.,
RA   Rousseau S., Budowski C., Lebouvier T., Corbille A.G., Vidailhet M.,
RA   Meneret A., Roze E., Anheim M., Tranchant C., Favrole P., Antoine J.C.,
RA   Defebvre L., Ayrignac X., Labauge P., Pariente J., Clanet M., Maltete D.,
RA   Rovelet-Lecrux A., Boland A., Deleuze J.F., Frebourg T., Hannequin D.,
RA   Campion D., Nicolas G.;
RT   "Biallelic MYORG mutation carriers exhibit primary brain calcification with
RT   a distinct phenotype.";
RL   Brain 142:1573-1586(2019).
RN   [10]
RP   INVOLVEMENT IN IBGC7, AND VARIANT IBGC7 445-GLN--SER-714 DEL.
RX   PubMed=30460687; DOI=10.1111/cge.13467;
RA   Peng Y., Wang P., Chen Z., Jiang H.;
RT   "A novel mutation in MYORG causes primary familial brain calcification with
RT   central neuropathic pain.";
RL   Clin. Genet. 95:433-435(2019).
RN   [11]
RP   INVOLVEMENT IN IBGC7, AND VARIANTS IBGC7 LEU-ALA-PHE-ARG-116 INS;
RP   143-LEU--ILE-147 DEL; CYS-229 AND 477-TYR--SER-714 DEL.
RX   PubMed=30589467; DOI=10.1002/mds.27582;
RA   Chen Y., Fu F., Chen S., Cen Z., Tang H., Huang J., Xie F., Zheng X.,
RA   Yang D., Wang H., Huang X., Zhang Y., Zhou Y., Liu J.Y., Luo W.;
RT   "Evaluation of MYORG mutations as a novel cause of primary familial brain
RT   calcification.";
RL   Mov. Disord. 34:291-297(2019).
RN   [12]
RP   INVOLVEMENT IN IBGC7.
RX   PubMed=30895394; DOI=10.1007/s10048-019-00571-8;
RA   Ramos E.M., Roca A., Chumchim N., Dokuru D.R., Van Berlo V., De Michele G.,
RA   Lieto M., Tedeschi E., De Michele G., Coppola G.;
RT   "Primary familial brain calcification caused by a novel homozygous MYORG
RT   mutation in a consanguineous Italian family.";
RL   Neurogenetics 20:99-102(2019).
CC   -!- FUNCTION: Putative glycosidase. Promotes myogenesis by activating AKT
CC       signaling through the maturation and secretion of IGF2.
CC       {ECO:0000250|UniProtKB:Q69ZQ1}.
CC   -!- SUBUNIT: Interacts with IGF2; this interaction is required for IGF2
CC       secretion. {ECO:0000250|UniProtKB:Q69ZQ1}.
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:Q69ZQ1};
CC       Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q69ZQ1}.
CC       Endoplasmic reticulum membrane {ECO:0000269|PubMed:29910000}; Single-
CC       pass type II membrane protein {ECO:0000250|UniProtKB:Q69ZQ1}. Note=Only
CC       a minor fraction is present in the peripheral endoplasmic reticulum.
CC       {ECO:0000250|UniProtKB:Q69ZQ1}.
CC   -!- DISEASE: Basal ganglia calcification, idiopathic, 7, autosomal
CC       recessive (IBGC7) [MIM:618317]: A form of basal ganglia calcification,
CC       a genetically heterogeneous condition characterized by symmetric
CC       calcification in the basal ganglia and other brain regions. Affected
CC       individuals can either be asymptomatic or show a wide spectrum of
CC       neuropsychiatric symptoms, including parkinsonism, dystonia, tremor,
CC       ataxia, dementia, psychosis, seizures, and chronic headache. Serum
CC       levels of calcium, phosphate, alkaline phosphatase and parathyroid
CC       hormone are normal. The neuropathological hallmark of the disease is
CC       vascular and pericapillary calcification, mainly of calcium phosphate,
CC       in the affected brain areas. {ECO:0000269|PubMed:29910000,
CC       ECO:0000269|PubMed:30460687, ECO:0000269|PubMed:30589467,
CC       ECO:0000269|PubMed:30656188, ECO:0000269|PubMed:30895394,
CC       ECO:0000269|PubMed:31009047}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: The requirement of the predicted catalytic residue Asp-
CC       463 to support myogenic function strongly suggests that MYORG is an
CC       enzymatically active glycosidase in vivo, even if concrete experimental
CC       proof for enzymatic activity is still missing.
CC       {ECO:0000305|PubMed:19706595}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR   EMBL; AL356494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC070098; AAH70098.1; -; mRNA.
DR   EMBL; BC110493; AAI10494.1; -; mRNA.
DR   EMBL; AB032987; BAA86475.2; -; mRNA.
DR   CCDS; CCDS78391.1; -.
DR   RefSeq; NP_065753.2; NM_020702.4.
DR   RefSeq; XP_011516268.1; XM_011517966.2.
DR   RefSeq; XP_016870419.1; XM_017014930.1.
DR   PDB; 7QQF; X-ray; 2.43 A; A/B/C/D=80-714.
DR   PDB; 7QQG; X-ray; 2.43 A; A/B/C/D=80-714.
DR   PDB; 7QQH; X-ray; 2.25 A; A/B/C/D=80-714.
DR   PDBsum; 7QQF; -.
DR   PDBsum; 7QQG; -.
DR   PDBsum; 7QQH; -.
DR   AlphaFoldDB; Q6NSJ0; -.
DR   SMR; Q6NSJ0; -.
DR   BioGRID; 121532; 58.
DR   IntAct; Q6NSJ0; 12.
DR   STRING; 9606.ENSP00000297625; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   GlyConnect; 1882; 2 N-Linked glycans (1 site).
DR   GlyCosmos; Q6NSJ0; 3 sites, 2 glycans.
DR   GlyGen; Q6NSJ0; 5 sites, 2 N-linked glycans (1 site).
DR   iPTMnet; Q6NSJ0; -.
DR   PhosphoSitePlus; Q6NSJ0; -.
DR   SwissPalm; Q6NSJ0; -.
DR   BioMuta; MYORG; -.
DR   DMDM; 158563982; -.
DR   EPD; Q6NSJ0; -.
DR   jPOST; Q6NSJ0; -.
DR   MassIVE; Q6NSJ0; -.
DR   MaxQB; Q6NSJ0; -.
DR   PaxDb; 9606-ENSP00000297625; -.
DR   PeptideAtlas; Q6NSJ0; -.
DR   ProteomicsDB; 66636; -.
DR   Pumba; Q6NSJ0; -.
DR   Antibodypedia; 55615; 61 antibodies from 12 providers.
DR   DNASU; 57462; -.
DR   Ensembl; ENST00000297625.8; ENSP00000297625.8; ENSG00000164976.9.
DR   GeneID; 57462; -.
DR   KEGG; hsa:57462; -.
DR   MANE-Select; ENST00000297625.8; ENSP00000297625.8; NM_020702.5; NP_065753.2.
DR   UCSC; uc033cpb.2; human.
DR   AGR; HGNC:19918; -.
DR   CTD; 57462; -.
DR   DisGeNET; 57462; -.
DR   GeneCards; MYORG; -.
DR   HGNC; HGNC:19918; MYORG.
DR   HPA; ENSG00000164976; Tissue enhanced (skeletal).
DR   MalaCards; MYORG; -.
DR   MIM; 618255; gene.
DR   MIM; 618317; phenotype.
DR   neXtProt; NX_Q6NSJ0; -.
DR   OpenTargets; ENSG00000164976; -.
DR   Orphanet; 1980; Bilateral striopallidodentate calcinosis.
DR   PharmGKB; PA134929853; -.
DR   VEuPathDB; HostDB:ENSG00000164976; -.
DR   eggNOG; KOG1065; Eukaryota.
DR   GeneTree; ENSGT00940000161008; -.
DR   HOGENOM; CLU_008294_0_0_1; -.
DR   InParanoid; Q6NSJ0; -.
DR   OMA; AFFTWVH; -.
DR   OrthoDB; 2725689at2759; -.
DR   PhylomeDB; Q6NSJ0; -.
DR   TreeFam; TF324266; -.
DR   PathwayCommons; Q6NSJ0; -.
DR   SignaLink; Q6NSJ0; -.
DR   BioGRID-ORCS; 57462; 9 hits in 392 CRISPR screens.
DR   ChiTaRS; MYORG; human.
DR   GenomeRNAi; 57462; -.
DR   Pharos; Q6NSJ0; Tbio.
DR   PRO; PR:Q6NSJ0; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q6NSJ0; Protein.
DR   Bgee; ENSG00000164976; Expressed in ventricular zone and 122 other cell types or tissues.
DR   ExpressionAtlas; Q6NSJ0; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:UniProtKB.
DR   GO; GO:0048741; P:skeletal muscle fiber development; IMP:UniProtKB.
DR   CDD; cd06592; GH31_NET37; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR43053; GLYCOSIDASE FAMILY 31; 1.
DR   PANTHER; PTHR43053:SF7; MYOGENESIS-REGULATING GLYCOSIDASE; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 2.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   Genevisible; Q6NSJ0; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Disease variant; Endoplasmic reticulum; Glycoprotein;
KW   Glycosidase; Hydrolase; Membrane; Nucleus; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..714
FT                   /note="Myogenesis-regulating glycosidase"
FT                   /id="PRO_0000295752"
FT   TOPO_DOM        1..56
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        57..77
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        78..714
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        463
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        466
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        528
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        240
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        250
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
FT   CARBOHYD        511
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         4
FT                   /note="N -> I (in dbSNP:rs2297776)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_033359"
FT   VARIANT         35
FT                   /note="M -> V (in IBGC7; dbSNP:rs765483979)"
FT                   /evidence="ECO:0000269|PubMed:29910000"
FT                   /id="VAR_081940"
FT   VARIANT         53
FT                   /note="D -> E (in dbSNP:rs4879781)"
FT                   /evidence="ECO:0000269|PubMed:10574461,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_033360"
FT   VARIANT         64
FT                   /note="G -> E (in IBGC7; uncertain significance;
FT                   dbSNP:rs756514041)"
FT                   /evidence="ECO:0000269|PubMed:31009047"
FT                   /id="VAR_081941"
FT   VARIANT         75..714
FT                   /note="Missing (in IBGC7)"
FT                   /evidence="ECO:0000269|PubMed:29910000"
FT                   /id="VAR_081942"
FT   VARIANT         113
FT                   /note="L -> R (in IBGC7; uncertain significance;
FT                   dbSNP:rs753277260)"
FT                   /evidence="ECO:0000269|PubMed:31009047"
FT                   /id="VAR_081943"
FT   VARIANT         116
FT                   /note="R -> RLAFR (in IBGC7)"
FT                   /evidence="ECO:0000269|PubMed:29910000,
FT                   ECO:0000269|PubMed:30589467, ECO:0000269|PubMed:31009047"
FT                   /id="VAR_081944"
FT   VARIANT         143..147
FT                   /note="Missing (in IBGC7; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:30589467"
FT                   /id="VAR_081945"
FT   VARIANT         199
FT                   /note="R -> S (in dbSNP:rs12377)"
FT                   /id="VAR_033361"
FT   VARIANT         203..714
FT                   /note="Missing (in IBGC7)"
FT                   /evidence="ECO:0000269|PubMed:29910000"
FT                   /id="VAR_081946"
FT   VARIANT         229
FT                   /note="W -> C (in IBGC7; uncertain significance;
FT                   dbSNP:rs1588004637)"
FT                   /evidence="ECO:0000269|PubMed:30589467"
FT                   /id="VAR_081947"
FT   VARIANT         232
FT                   /note="S -> L (in IBGC7; uncertain significance;
FT                   dbSNP:rs757434146)"
FT                   /evidence="ECO:0000269|PubMed:29910000"
FT                   /id="VAR_081948"
FT   VARIANT         236
FT                   /note="A -> AA (in IBGC7; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:31009047"
FT                   /id="VAR_081949"
FT   VARIANT         249
FT                   /note="W -> C (in IBGC7; uncertain significance;
FT                   dbSNP:rs1356560096)"
FT                   /evidence="ECO:0000269|PubMed:31009047"
FT                   /id="VAR_081950"
FT   VARIANT         261
FT                   /note="R -> L (in IBGC7; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:29910000"
FT                   /id="VAR_081951"
FT   VARIANT         354
FT                   /note="Missing (in IBGC7; uncertain significance;
FT                   dbSNP:rs1180204613)"
FT                   /evidence="ECO:0000269|PubMed:30656188"
FT                   /id="VAR_081952"
FT   VARIANT         365..366
FT                   /note="Missing (in IBGC7; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:29910000"
FT                   /id="VAR_081953"
FT   VARIANT         373
FT                   /note="A -> D (in IBGC7; uncertain significance;
FT                   dbSNP:rs1588004082)"
FT                   /evidence="ECO:0000269|PubMed:31009047"
FT                   /id="VAR_081954"
FT   VARIANT         385
FT                   /note="F -> Y (in dbSNP:rs7852399)"
FT                   /id="VAR_033362"
FT   VARIANT         434
FT                   /note="D -> H (in IBGC7; uncertain significance;
FT                   dbSNP:rs916933188)"
FT                   /evidence="ECO:0000269|PubMed:31009047"
FT                   /id="VAR_081955"
FT   VARIANT         441
FT                   /note="R -> G (in IBGC7; dbSNP:rs749427106)"
FT                   /evidence="ECO:0000269|PubMed:29910000"
FT                   /id="VAR_081956"
FT   VARIANT         443..714
FT                   /note="Missing (in IBGC7)"
FT                   /evidence="ECO:0000269|PubMed:29910000"
FT                   /id="VAR_081957"
FT   VARIANT         445..714
FT                   /note="Missing (in IBGC7)"
FT                   /evidence="ECO:0000269|PubMed:30460687,
FT                   ECO:0000269|PubMed:31009047"
FT                   /id="VAR_081958"
FT   VARIANT         476
FT                   /note="T -> N (in IBGC7; uncertain significance;
FT                   dbSNP:rs769099047)"
FT                   /evidence="ECO:0000269|PubMed:31009047"
FT                   /id="VAR_081959"
FT   VARIANT         477..714
FT                   /note="Missing (in IBGC7)"
FT                   /evidence="ECO:0000269|PubMed:30589467"
FT                   /id="VAR_081960"
FT   VARIANT         513
FT                   /note="Missing (in IBGC7; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:31009047"
FT                   /id="VAR_081961"
FT   VARIANT         611
FT                   /note="R -> W (in IBGC7; uncertain significance;
FT                   dbSNP:rs536187898)"
FT                   /evidence="ECO:0000269|PubMed:31009047"
FT                   /id="VAR_081962"
FT   VARIANT         622
FT                   /note="L -> P (in IBGC7; uncertain significance;
FT                   dbSNP:rs1239594469)"
FT                   /evidence="ECO:0000269|PubMed:31009047"
FT                   /id="VAR_081963"
FT   VARIANT         656
FT                   /note="I -> T (in IBGC7; uncertain significance;
FT                   dbSNP:rs370944350)"
FT                   /evidence="ECO:0000269|PubMed:31009047"
FT                   /id="VAR_081964"
FT   VARIANT         660
FT                   /note="L -> Q (in IBGC7; uncertain significance;
FT                   dbSNP:rs1588002920)"
FT                   /evidence="ECO:0000269|PubMed:31009047"
FT                   /id="VAR_081965"
FT   MUTAGEN         463
FT                   /note="D->A: Does not change nuclear membrane localization.
FT                   Does not rescue the myogenetic defect induced by depletion
FT                   of endogenous MYORG."
FT                   /evidence="ECO:0000269|PubMed:19706595"
FT   STRAND          93..96
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          99..103
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          109..117
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   HELIX           122..124
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          125..128
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          131..137
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          142..153
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          156..164
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          166..168
FT                   /evidence="ECO:0007829|PDB:7QQF"
FT   STRAND          172..177
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          185..189
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          202..208
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   HELIX           214..216
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          218..220
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          223..231
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          234..239
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          245..250
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   TURN            251..254
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          255..260
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          263..266
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          278..285
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   HELIX           289..300
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   HELIX           310..313
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          317..320
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   HELIX           321..324
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   HELIX           325..327
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   HELIX           330..342
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          350..352
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          357..359
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   TURN            367..369
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   HELIX           373..382
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          387..391
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          393..396
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   HELIX           402..408
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          417..420
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          423..425
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          428..433
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   HELIX           438..455
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          459..462
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   HELIX           467..469
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   HELIX           485..491
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   HELIX           492..500
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          502..504
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          506..508
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          514..517
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          523..526
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   HELIX           531..533
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   HELIX           534..543
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          548..550
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   TURN            564..567
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   HELIX           571..581
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          584..586
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          588..591
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   HELIX           593..595
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   HELIX           598..613
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   HELIX           615..629
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          633..635
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   HELIX           637..639
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   HELIX           645..649
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          654..656
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   TURN            657..659
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          660..663
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          671..677
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          679..684
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          694..701
FT                   /evidence="ECO:0007829|PDB:7QQH"
FT   STRAND          708..713
FT                   /evidence="ECO:0007829|PDB:7QQH"
SQ   SEQUENCE   714 AA;  81087 MW;  D17E4A75A81DBB46 CRC64;
     MLQNPQEKSQ AYPRRRRPGC YAYRQNPEAI AAAAMYTFLP DNFSPAKPKP SKDLKPLLGS
     AVLGLLLVLA AVVAWCYYSV SLRKAERLRA ELLDLKAGGF SIRNQKGEQV FRLAFRSGAL
     DLDSCSRDGA LLGCSLTADG LPLHFFIQTV RPKDTVMCYR VRWEEAAPGR AVEHAMFLGD
     AAAHWYGGAE MRTQHWPIRL DGQQEPQPFV TSDVYSSDAA FGGILERYWL SSRAAAIKVN
     DSVPFHLGWN STERSLRLQA RYHDTPYKPP AGRAAAPELS YRVCVGSDVT SIHKYMVRRY
     FNKPSRVPAP EAFRDPIWST WALYGRAVDQ DKVLRFAQQI RLHHFNSSHL EIDDMYTPAY
     GDFDFDEVKF PNASDMFRRL RDAGFRVTLW VHPFVNYNSS RFGEGVEREL FVREPTGRLP
     ALVRWWNGIG AVLDFTHPKA RDWFQGHLRR LRSRYSVASF KFDAGEVSYL PRDFSTYRPL
     PDPSVWSRRY TEMALPFFSL AEVRVGYQSQ NISCFFRLVD RDSVWGYDLG LRSLIPAVLT
     VSMLGYPFIL PDMVGGNAVP QRTAGGDVPE RELYIRWLEV AAFMPAMQFS IPPWRYDAEV
     VAIAQKFAAL RASLVAPLLL ELAGEVTDTG DPIVRPLWWI APGDETAHRI DSQFLIGDTL
     LVAPVLEPGK QERDVYLPAG KWRSYKGELF DKTPVLLTDY PVDLDEIAYF TWAS
//