MOGS_RAT
ID MOGS_RAT Reviewed; 834 AA.
AC O88941;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Mannosyl-oligosaccharide glucosidase;
DE EC=3.2.1.106;
DE AltName: Full=Glycoprotein-processing glucosidase I;
GN Name=Mogs; Synonyms=Gcs1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Varma G.M., Vijay I.K.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION AT ASN-654.
RX PubMed=1885588; DOI=10.1016/s0021-9258(18)55341-2;
RA Shailubhai K., Pukazhenthi B.S., Saxena E.S., Varma G.M., Vijay I.K.;
RT "Glucosidase I, a transmembrane endoplasmic reticular glycoprotein with a
RT luminal catalytic domain.";
RL J. Biol. Chem. 266:16587-16593(1991).
CC -!- FUNCTION: Cleaves the distal alpha 1,2-linked glucose residue from the
CC Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor in a highly specific
CC manner. {ECO:0000269|PubMed:1885588}.
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
CC {ECO:0000269|PubMed:1885588}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:1885588}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 63 family. {ECO:0000305}.
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DR EMBL; AF087431; AAC36477.1; -; mRNA.
DR RefSeq; NP_113937.1; NM_031749.2.
DR AlphaFoldDB; O88941; -.
DR SMR; O88941; -.
DR IntAct; O88941; 1.
DR CAZy; GH63; Glycoside Hydrolase Family 63.
DR GlyGen; O88941; 1 site.
DR iPTMnet; O88941; -.
DR PhosphoSitePlus; O88941; -.
DR jPOST; O88941; -.
DR PaxDb; O88941; -.
DR PRIDE; O88941; -.
DR GeneID; 78947; -.
DR KEGG; rno:78947; -.
DR UCSC; RGD:69240; rat.
DR CTD; 7841; -.
DR RGD; 69240; Mogs.
DR eggNOG; KOG2161; Eukaryota.
DR InParanoid; O88941; -.
DR OrthoDB; 278028at2759; -.
DR PhylomeDB; O88941; -.
DR UniPathway; UPA00280; -.
DR PRO; PR:O88941; -.
DR Proteomes; UP000002494; Unplaced.
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 Endoplasmic reticulum; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..834
FT /note="Mannosyl-oligosaccharide glucosidase"
FT /id="PRO_0000057712"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..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:0000269|PubMed:1885588"
SQ SEQUENCE 834 AA; 91872 MW; E6E1E0B58E74F178 CRC64;
MARGERRRRA AAAEGARPLE RARGAGRRDG RAGGARGSAG GAALAVVVLA LAFGLSGRWV
LAWLGVRRAL TLHPAPSALP PDSSSPAVAP EFFWGTYRPH VYFGMKTRSP KPLLTGLMWA
QQGATPGTPP KLRHTCEQGD GVGPYGWEFH DGLSFGRQHI YDGALRLTTE FVKRSGGHHG
GDWSWRVTVE PQASGTPSFP LVSLFFYVVT DGQEVLLPEV GAKGQLKFIS GHTSELGDFR
LTLLPPTTPG DTVPKHGSYN VFWSSNPGLP LLTDMVKSHL NSWFHHRPPG ASPERYLGLP
GSLKWEERGP SGQGQFLVQQ VTLKAPFSVE FVFESGSART GRDQASEQLV GGQLTRALES
HAAAFKERFE RTFQLKEKGL SPEEQALGQV ALSGLLGGIG YFYGQGLVLP DTGMEGSEQK
MDPSLFPPVP LFSGVPSRSF FPRGFLWDEG FHQLVVQRWD PHLTREALGH WLGLLNADGW
IGREQILGDE ARARVPPEFL VQRAAHANPP TLLLPVIHML EGRAPEDLAF LRRAFPRLHA
WFSWLHQSQA GPVPLSYRWR GRDLALPTLL NPKTLPSGLD DYPRASHPSA AERHLDLRCW
VTLGARVLSQ LAEELGETEA AAELGPLAAS LEAAGSLDEL HWAPELGVFA DFGNHTKAVQ
LKSRPPQGLV RVVGRPPARL QYVDALGYVS LFPLLLQLLE PSSPRLGPLL DVLADSRHLW
SPFGLRSLSA SSLFYKQRNT EHDPPYWRGA VWLNINYLAL GALHHYGRVE GPHKVQAAKL
YRELRANVVS NVRQQYQATG FLWEQYSDQD GRGMGCRPFQ GWTSLVLLIM AEEY
