MYORG_MOUSE
ID MYORG_MOUSE Reviewed; 716 AA.
AC Q69ZQ1; A2ANN6; B2RU42;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Myogenesis-regulating glycosidase;
DE EC=3.2.1.-;
DE AltName: Full=Nuclear envelope transmembrane protein 37 {ECO:0000303|PubMed:17062158};
DE AltName: Full=Uncharacterized family 31 glucosidase KIAA1161;
GN Name=Myorg; Synonyms=Kiaa1161, Net37 {ECO:0000303|PubMed:17062158};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Testis;
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 [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-239 AND ASN-249.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17062158; DOI=10.1186/1471-2121-7-38;
RA Chen I.-H., Huber M., Guan T., Bubeck A., Gerace L.;
RT "Nuclear envelope transmembrane proteins (NETs) that are up-regulated
RT during myogenesis.";
RL BMC Cell Biol. 7:38-38(2006).
RN [6]
RP TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION, TOPOLOGY, FUNCTION,
RP AND INTERACTION WITH IGF2.
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Putative glycosidase. Promotes myogenesis by activating AKT
CC signaling through the maturation and secretion of IGF2
CC (PubMed:19706595). {ECO:0000269|PubMed:19706595}.
CC -!- SUBUNIT: Interacts with IGF2; this interaction is required for IGF2
CC secretion (PubMed:19706595). {ECO:0000269|PubMed:19706595}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:17062158,
CC ECO:0000269|PubMed:19706595}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:19706595}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19706595}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:19706595}. Note=Only a minor fraction is present in
CC the peripheral endoplasmic reticulum (PubMed:19706595).
CC {ECO:0000269|PubMed:19706595}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, liver, spleen, skeletal muscle,
CC heart, lung and kidney (PubMed:29910000). High expression is observed
CC in the cerebellum, specifically in astrocytes (PubMed:29910000). Highly
CC expressed in skeletal muscle (at protein level) (PubMed:19706595).
CC {ECO:0000269|PubMed:19706595, ECO:0000269|PubMed:29910000}.
CC -!- INDUCTION: Up-regulated during C2C12 myogenic differentiation.
CC {ECO:0000269|PubMed:17062158, ECO:0000269|PubMed:19706595}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice develop bilateral calcifications in
CC the thalamus, due to the formation of calcium phosphate deposits.
CC {ECO:0000269|PubMed:29910000}.
CC -!- MISCELLANEOUS: The requirement of the predicted catalytic residue Asp-
CC 462 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32395.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK173117; BAD32395.1; ALT_INIT; mRNA.
DR EMBL; AL831723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC137640; AAI37641.1; -; mRNA.
DR EMBL; BC140956; AAI40957.1; -; mRNA.
DR CCDS; CCDS38716.1; -.
DR RefSeq; NP_001078984.1; NM_001085515.2.
DR RefSeq; XP_006538073.1; XM_006538010.2.
DR AlphaFoldDB; Q69ZQ1; -.
DR SMR; Q69ZQ1; -.
DR BioGRID; 236844; 2.
DR STRING; 10090.ENSMUSP00000059038; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR GlyConnect; 2810; 4 N-Linked glycans (2 sites).
DR GlyGen; Q69ZQ1; 4 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q69ZQ1; -.
DR PhosphoSitePlus; Q69ZQ1; -.
DR SwissPalm; Q69ZQ1; -.
DR MaxQB; Q69ZQ1; -.
DR PaxDb; Q69ZQ1; -.
DR PeptideAtlas; Q69ZQ1; -.
DR PRIDE; Q69ZQ1; -.
DR ProteomicsDB; 287536; -.
DR Antibodypedia; 55615; 50 antibodies from 12 providers.
DR Ensembl; ENSMUST00000054920; ENSMUSP00000059038; ENSMUSG00000046312.
DR GeneID; 329828; -.
DR KEGG; mmu:329828; -.
DR UCSC; uc008sit.2; mouse.
DR CTD; 57462; -.
DR MGI; MGI:2140300; Myorg.
DR VEuPathDB; HostDB:ENSMUSG00000046312; -.
DR eggNOG; KOG1065; Eukaryota.
DR GeneTree; ENSGT00940000161008; -.
DR HOGENOM; CLU_008294_0_0_1; -.
DR InParanoid; Q69ZQ1; -.
DR OMA; ETATQYW; -.
DR OrthoDB; 238940at2759; -.
DR PhylomeDB; Q69ZQ1; -.
DR TreeFam; TF324266; -.
DR BioGRID-ORCS; 329828; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q69ZQ1; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q69ZQ1; protein.
DR Bgee; ENSMUSG00000046312; Expressed in hindlimb stylopod muscle and 208 other tissues.
DR ExpressionAtlas; Q69ZQ1; baseline and differential.
DR Genevisible; Q69ZQ1; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IDA:MGI.
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; IMP:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:MGI.
DR GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
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 Endoplasmic reticulum; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW Nucleus; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..716
FT /note="Myogenesis-regulating glycosidase"
FT /id="PRO_0000295753"
FT TOPO_DOM 1..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..716
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 462
FT /evidence="ECO:0000250"
FT ACT_SITE 465
FT /evidence="ECO:0000250"
FT ACT_SITE 527
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 2
FT /note="S -> P (in Ref. 3; AAI40957/AAI37641)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 716 AA; 81362 MW; 5691CCD1D6515D17 CRC64;
MSQNLQETSQ AYPRHRPGSH AGPKSLKVTP RATMYTFLPD NFSPAKPKPT KELRPLLCSA
VLGLLLVLAA VVAWCYYSAS LRKAERLRAE LLDLNRGGFS IRNQKGEQVF RLAFRSGALD
LDSCSRDGAL LGCSRAADGR PLHFFIQTVR PKDTVMCYRV RWEEAVPGRA VEHAMFLGDA
AAHWYGGAEM RTQHWPIRLD GQQEPQPFVT SDVYSSDAAF GGILERYWLS SRAAAIKVND
SVPFHLGWNS TERSMRLQAR YHDTSYKPPA GRTAAPELSY RVCVGSDVTS IHKYMVRRYF
NKPSRVPASE AFRDPIWSTW ALHGRAVDQN KVLQFAQQIR QHRFNSSHLE IDDMYTPAYG
DFNFDEGKFP NASDMFRRLR DAGFRVTLWV HPFVNYNSSS FGEGVERELF VREPTGRLPA
LVRWWNGIGA VLDFTHPEAR EWFQGHLRRL RLRYNVTSFK FDAGEVSYLP RDFSTYRPLS
DPSVWSRRYT EMAEPFFSLA EVRVGYQSQN ISCFFRLVDR DSVWGYDLGL RSLIPAVLTV
SMLGYPFILP DMIGGNAVPE RTAGRQDGPG PERELYVRWL EVAAFMPAMQ FSIPPWQYDA
EVVAIAHKFA ALRASLVAPL LLELAGEITD TGDPIVRPLW WIAPGDETAH RIDSQFLIGD
TLLVAPVLEP GKQERDVYLP AGKWRSYKGE LFDKTPVLLT DYPVDLDEVA YFTWAS
