MOGS_MOUSE
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 03-AUG-2022, entry version 142.
DE RecName: Full=Mannosyl-oligosaccharide glucosidase;
DE EC=3.2.1.106;
DE AltName: Full=Glucosidase 1;
DE AltName: Full=Glycoprotein-processing glucosidase I;
GN Name=Mogs; Synonyms=Gcs1;
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.
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]
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, Pancreas,
RC 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).
CC -!- FUNCTION: Cleaves the distal alpha 1,2-linked glucose residue from the
CC Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor. {ECO:0000250}.
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)-alpha-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)-alpha-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 -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}.
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; 7.
DR IntAct; Q80UM7; 3.
DR STRING; 10090.ENSMUSP00000032114; -.
DR ChEMBL; CHEMBL4523366; -.
DR CAZy; GH63; Glycoside Hydrolase Family 63.
DR GlyGen; Q80UM7; 1 site.
DR iPTMnet; Q80UM7; -.
DR PhosphoSitePlus; Q80UM7; -.
DR SwissPalm; Q80UM7; -.
DR EPD; Q80UM7; -.
DR jPOST; Q80UM7; -.
DR MaxQB; Q80UM7; -.
DR PaxDb; Q80UM7; -.
DR PRIDE; Q80UM7; -.
DR ProteomicsDB; 295578; -.
DR Antibodypedia; 2372; 186 antibodies from 25 providers.
DR DNASU; 57377; -.
DR Ensembl; ENSMUST00000032114; ENSMUSP00000032114; ENSMUSG00000030036.
DR GeneID; 57377; -.
DR KEGG; mmu:57377; -.
DR UCSC; uc009cmn.1; mouse.
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; YWKAPLY; -.
DR OrthoDB; 278028at2759; -.
DR PhylomeDB; Q80UM7; -.
DR TreeFam; TF300749; -.
DR UniPathway; UPA00280; -.
DR BioGRID-ORCS; 57377; 27 hits in 78 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 262 other tissues.
DR Genevisible; Q80UM7; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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; PTHR10412; 1.
DR Pfam; PF03200; Glyco_hydro_63; 1.
DR Pfam; PF16923; Glyco_hydro_63N; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
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 CARBOHYD 654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
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
