MYORG_HUMAN
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 03-AUG-2022, entry version 137.
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 AlphaFoldDB; Q6NSJ0; -.
DR SMR; Q6NSJ0; -.
DR BioGRID; 121532; 55.
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 GlyGen; Q6NSJ0; 5 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q6NSJ0; -.
DR PhosphoSitePlus; Q6NSJ0; -.
DR BioMuta; MYORG; -.
DR DMDM; 158563982; -.
DR EPD; Q6NSJ0; -.
DR jPOST; Q6NSJ0; -.
DR MassIVE; Q6NSJ0; -.
DR MaxQB; Q6NSJ0; -.
DR PaxDb; Q6NSJ0; -.
DR PeptideAtlas; Q6NSJ0; -.
DR PRIDE; Q6NSJ0; -.
DR ProteomicsDB; 66636; -.
DR Antibodypedia; 55615; 50 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 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; ETATQYW; -.
DR OrthoDB; 238940at2759; -.
DR PhylomeDB; Q6NSJ0; -.
DR TreeFam; TF324266; -.
DR PathwayCommons; Q6NSJ0; -.
DR SignaLink; Q6NSJ0; -.
DR BioGRID-ORCS; 57462; 8 hits in 320 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 121 other tissues.
DR ExpressionAtlas; Q6NSJ0; baseline and differential.
DR Genevisible; Q6NSJ0; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:0048741; P:skeletal muscle fiber development; IMP:UniProtKB.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Disease variant; Endoplasmic reticulum; Glycoprotein; Glycosidase;
KW Hydrolase; Membrane; Nucleus; Reference proteome; Signal-anchor;
KW 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; unknown pathological 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; unknown pathological 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; unknown pathological
FT 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; unknown pathological significance;
FT dbSNP:rs1588004637)"
FT /evidence="ECO:0000269|PubMed:30589467"
FT /id="VAR_081947"
FT VARIANT 232
FT /note="S -> L (in IBGC7; unknown pathological significance;
FT dbSNP:rs757434146)"
FT /evidence="ECO:0000269|PubMed:29910000"
FT /id="VAR_081948"
FT VARIANT 236
FT /note="A -> AA (in IBGC7; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31009047"
FT /id="VAR_081949"
FT VARIANT 249
FT /note="W -> C (in IBGC7; unknown pathological significance;
FT dbSNP:rs1356560096)"
FT /evidence="ECO:0000269|PubMed:31009047"
FT /id="VAR_081950"
FT VARIANT 261
FT /note="R -> L (in IBGC7; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:29910000"
FT /id="VAR_081951"
FT VARIANT 354
FT /note="Missing (in IBGC7; unknown pathological
FT significance; dbSNP:rs1180204613)"
FT /evidence="ECO:0000269|PubMed:30656188"
FT /id="VAR_081952"
FT VARIANT 365..366
FT /note="Missing (in IBGC7; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:29910000"
FT /id="VAR_081953"
FT VARIANT 373
FT /note="A -> D (in IBGC7; unknown pathological 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; unknown pathological 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; unknown pathological 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; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31009047"
FT /id="VAR_081961"
FT VARIANT 611
FT /note="R -> W (in IBGC7; unknown pathological significance;
FT dbSNP:rs536187898)"
FT /evidence="ECO:0000269|PubMed:31009047"
FT /id="VAR_081962"
FT VARIANT 622
FT /note="L -> P (in IBGC7; unknown pathological significance;
FT dbSNP:rs1239594469)"
FT /evidence="ECO:0000269|PubMed:31009047"
FT /id="VAR_081963"
FT VARIANT 656
FT /note="I -> T (in IBGC7; unknown pathological significance;
FT dbSNP:rs370944350)"
FT /evidence="ECO:0000269|PubMed:31009047"
FT /id="VAR_081964"
FT VARIANT 660
FT /note="L -> Q (in IBGC7; unknown pathological 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"
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
