ID   MOGS_MOUSE              Reviewed;         834 AA.
AC   Q80UM7; Q9Z2W5;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 150.
DE   RecName: Full=Mannosyl-oligosaccharide glucosidase {ECO:0000305};
DE            EC=3.2.1.106 {ECO:0000250|UniProtKB:Q13724};
DE   AltName: Full=Endoplasmic reticulum alpha-glucosidase I {ECO:0000303|PubMed:21183079};
DE            Short=ER glu I {ECO:0000303|PubMed:21183079};
DE   AltName: Full=Glucosidase 1;
DE   AltName: Full=Glycoprotein-processing glucosidase I {ECO:0000305|PubMed:10406845};
GN   Name=Mogs {ECO:0000312|MGI:MGI:1929872};
GN   Synonyms=Gcs1 {ECO:0000312|MGI:MGI:1929872};
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] {ECO:0000312|EMBL:AAD00906.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10406845; DOI=10.1093/glycob/9.8.797;
RA   Khan F.A., Varma G.M., Vijay I.K.;
RT   "Genomic organization and promoter activity of glucosidase I gene.";
RL   Glycobiology 9:797-806(1999).
RN   [2] {ECO:0000312|EMBL:AAH51949.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Fetal brain;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
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   [4] {ECO:0007744|PDB:5MHF}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 59-834 IN COMPLEX WITH A
RP   DEOXYNOJIRIMYCIN DERIVATIVE INHIBITOR, FUNCTION (MICROBIAL INFECTION), AND
RP   ACTIVITY REGULATION.
RX   PubMed=32227946; DOI=10.1021/acs.jmedchem.0c00067;
RA   Warfield K.L., Alonzi D.S., Hill J.C., Caputo A.T., Roversi P.,
RA   Kiappes J.L., Sheets N., Duchars M., Dwek R.A., Biggins J., Barnard D.,
RA   Shresta S., Treston A.M., Zitzmann N.;
RT   "Targeting endoplasmic reticulum alpha-glucosidase I with a single-dose
RT   iminosugar treatment protects against lethal Influenza and Dengue virus
RT   infections.";
RL   J. Med. Chem. 63:4205-4214(2020).
CC   -!- FUNCTION: In the context of N-glycan degradation, cleaves the distal
CC       alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2)
CC       oligosaccharide precursor in a highly specific manner.
CC       {ECO:0000250|UniProtKB:Q13724}.
CC   -!- FUNCTION: (Microbial infection) Required for successful influenza or
CC       dengue virus infection; inhibition of its activity by a
CC       deoxynojirimycin derivative prevents death in mice infected with lethal
CC       doses of influenza or dengue viruses, even when administrated after
CC       infection. {ECO:0000269|PubMed:32227946}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(4)-(alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-
CC         (1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC         [alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC         Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC         (1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] = beta-D-glucose +
CC         N(4)-(alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-
CC         D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC         (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-
CC         beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-
CC         [protein]; Xref=Rhea:RHEA:55988, Rhea:RHEA-COMP:12806, Rhea:RHEA-
CC         COMP:14355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:59082,
CC         ChEBI:CHEBI:132537; EC=3.2.1.106;
CC         Evidence={ECO:0000250|UniProtKB:Q13724};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55989;
CC         Evidence={ECO:0000250|UniProtKB:Q13724};
CC   -!- ACTIVITY REGULATION: Inhibited by the deoxynojirimycin derivative N-9'-
CC       Methoxynonyl-1-Deoxynojirimycin. {ECO:0000269|PubMed:32227946}.
CC   -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC       {ECO:0000250|UniProtKB:Q13724}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q13724}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:O88941}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 63 family. {ECO:0000305}.
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DR   EMBL; AF001797; AAD00906.1; -; Genomic_DNA.
DR   EMBL; BC051949; AAH51949.1; -; mRNA.
DR   CCDS; CCDS20273.1; -.
DR   RefSeq; NP_065644.2; NM_020619.2.
DR   PDB; 5MHF; X-ray; 2.10 A; A/B/C/D=59-834.
DR   PDBsum; 5MHF; -.
DR   AlphaFoldDB; Q80UM7; -.
DR   SMR; Q80UM7; -.
DR   BioGRID; 208276; 8.
DR   IntAct; Q80UM7; 3.
DR   STRING; 10090.ENSMUSP00000032114; -.
DR   ChEMBL; CHEMBL4523366; -.
DR   CAZy; GH63; Glycoside Hydrolase Family 63.
DR   GlyCosmos; Q80UM7; 1 site, No reported glycans.
DR   GlyGen; Q80UM7; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q80UM7; -.
DR   PhosphoSitePlus; Q80UM7; -.
DR   SwissPalm; Q80UM7; -.
DR   EPD; Q80UM7; -.
DR   jPOST; Q80UM7; -.
DR   MaxQB; Q80UM7; -.
DR   PaxDb; 10090-ENSMUSP00000032114; -.
DR   ProteomicsDB; 295578; -.
DR   Pumba; Q80UM7; -.
DR   Antibodypedia; 2372; 198 antibodies from 25 providers.
DR   DNASU; 57377; -.
DR   Ensembl; ENSMUST00000032114.8; ENSMUSP00000032114.8; ENSMUSG00000030036.9.
DR   GeneID; 57377; -.
DR   KEGG; mmu:57377; -.
DR   UCSC; uc009cmn.1; mouse.
DR   AGR; MGI:1929872; -.
DR   CTD; 7841; -.
DR   MGI; MGI:1929872; Mogs.
DR   VEuPathDB; HostDB:ENSMUSG00000030036; -.
DR   eggNOG; KOG2161; Eukaryota.
DR   GeneTree; ENSGT00390000017452; -.
DR   HOGENOM; CLU_007380_1_0_1; -.
DR   InParanoid; Q80UM7; -.
DR   OMA; FNWYNTT; -.
DR   OrthoDB; 1571at2759; -.
DR   PhylomeDB; Q80UM7; -.
DR   TreeFam; TF300749; -.
DR   UniPathway; UPA00280; -.
DR   BioGRID-ORCS; 57377; 28 hits in 83 CRISPR screens.
DR   ChiTaRS; Mogs; mouse.
DR   PRO; PR:Q80UM7; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q80UM7; Protein.
DR   Bgee; ENSMUSG00000030036; Expressed in primitive streak and 266 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0004573; F:Glc3Man9GlcNAc2 oligosaccharide glucosidase activity; IBA:GO_Central.
DR   GO; GO:0009311; P:oligosaccharide metabolic process; IEA:InterPro.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.70.98.110; Glycosyl hydrolase family 63, N-terminal domain; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR031335; Glyco_hydro_63_C.
DR   InterPro; IPR031631; Glyco_hydro_63N.
DR   InterPro; IPR038518; Glyco_hydro_63N_sf.
DR   InterPro; IPR004888; Glycoside_hydrolase_63.
DR   PANTHER; PTHR10412; MANNOSYL-OLIGOSACCHARIDE GLUCOSIDASE; 1.
DR   PANTHER; PTHR10412:SF11; MANNOSYL-OLIGOSACCHARIDE GLUCOSIDASE; 1.
DR   Pfam; PF03200; Glyco_hydro_63; 1.
DR   Pfam; PF16923; Glyco_hydro_63N; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   Genevisible; Q80UM7; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Endoplasmic reticulum; Glycoprotein; Glycosidase; Hydrolase;
KW   Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..834
FT                   /note="Mannosyl-oligosaccharide glucosidase"
FT                   /id="PRO_0000057711"
FT   TOPO_DOM        1..43
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..64
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        65..834
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          74..136
FT                   /note="Required for endoplasmic reticulum targeting"
FT                   /evidence="ECO:0000250"
FT   MOTIF           3..9
FT                   /note="Endoplasmic reticulum targeting"
FT   COMPBIAS        1..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        580
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000305|PubMed:32227946"
FT   ACT_SITE        804
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000305|PubMed:32227946"
FT   CARBOHYD        654
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13724"
FT   CONFLICT        749
FT                   /note="G -> S (in Ref. 1; AAD00906)"
FT                   /evidence="ECO:0000305"
FT   HELIX           63..69
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   TURN            81..84
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   TURN            86..88
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           90..92
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          93..95
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          101..109
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          114..123
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          144..150
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          152..162
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          165..174
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   TURN            177..180
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          182..191
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          201..209
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          228..233
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   TURN            234..236
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          237..243
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          258..265
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           269..271
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           272..279
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          282..286
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          294..299
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          315..335
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   TURN            336..338
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           342..345
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           351..365
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   TURN            368..370
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           382..397
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          400..404
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          407..409
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          429..433
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           446..459
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           461..472
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          483..485
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           489..492
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           497..499
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           513..522
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           525..532
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           535..548
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           575..577
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           595..615
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           618..632
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           634..641
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   TURN            644..647
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          652..655
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          659..664
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   TURN            665..667
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          668..673
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          679..682
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           689..691
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           692..695
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           706..714
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   TURN            716..719
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          724..728
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          746..749
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           753..766
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           774..778
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           781..799
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          804..806
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   TURN            808..810
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   STRAND          813..818
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           822..825
FT                   /evidence="ECO:0007829|PDB:5MHF"
FT   HELIX           826..831
FT                   /evidence="ECO:0007829|PDB:5MHF"
SQ   SEQUENCE   834 AA;  91831 MW;  CB2728BE16EACD0E CRC64;
     MARGERRRRA AAAEGARPLE RARAAGRRDG RAGGARGSAS GAALAVVVLA LAFGLSGRWV
     LAWLRVRRAL TLHPAPSALP PDSSSPAVAP ELFWGTYRPH VYFGMKTRSP KPLLTGLMWA
     QQGATPGTPP KLRHTCEQGD GVGPYGWEFH DGRTFGRQHI HDGALRLTTE FVKRPGGQHG
     GDWSWRVTVE PQASGTPSFP LVSLFFYVVT DGQEVLLPEI GAKGQLKSIS GHTSELGDFR
     LTLLPPTSPG DTVPKHGSYN VFWSSNPGLP QLTDMVKSRL NSWFQHRPPG ASPDRYLGLP
     GSLKWEERGP SGQGQFLIQQ VTLKAPFSVE FVFESGSAAT GGNQASGRLV GSQLTQALES
     HAAAFKERFE KTFQLKEKGL SPEEQALGQV ALSGLLGGIG YFYGQGLVLP DTSMEGSEQK
     MDPALFPPVP LFSGVPSRSF FPRGFLWDEG FHQLVVQRWD PHLTREALGH WLGLLNADGW
     IGREQILGDE ARARVPPEFL VQRAAHANPP TLLLPVVHML EGHDPDDLAF LRKAFPRLHA
     WFSWLHQSQA GPVPLSYRWR GRDLALPTLL NPKTLPSGLD DYPRASHPST AERHLDLRCW
     VALGARVLSQ LAEQLGETEA AAELGPLAAS LEEPGSLDEL HWAPELGVFA DFGNHTKAVQ
     LKSRPPQGLV RVVGRPPPRL QYVDALGYVS LFPLLLQLLD PSSPRLGPLL DVLADSRHLW
     SPFGLRSLSA SSLFYKQRNT EHDPPYWRGA VWLNINYLAL GALHHYGHVE GPHKVQAAKL
     YHELRANVVR NVRQQYQATG FLWEQYSDQD GRGMGCRPFQ GWTSLVLLIM AEEY
//