ID   MOGS1_CAEEL             Reviewed;         796 AA.
AC   Q19426; A5JYS7; Q0G829; Q0G830;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=Mannosyl-oligosaccharide glucosidase {ECO:0000312|WormBase:F13H10.4a};
DE            EC=3.2.1.106 {ECO:0000250|UniProtKB:Q13724};
DE   AltName: Full=Processing A-glucosidase I {ECO:0000250|UniProtKB:Q13724};
GN   Name=mogs-1 {ECO:0000312|WormBase:F13H10.4a};
GN   Synonyms=agl-1 {ECO:0000303|PubMed:23836288};
GN   ORFNames=F13H10.4 {ECO:0000312|WormBase:F13H10.4a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-153, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA   Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT   "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT   elegans.";
RL   Glycobiology 15:952-964(2005).
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-517, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23836288; DOI=10.1093/glycob/cwt051;
RA   Katoh T., Takase J., Tani Y., Amamoto R., Aoshima N., Tiemeyer M.,
RA   Yamamoto K., Ashida H.;
RT   "Deficiency of alpha-glucosidase I alters glycoprotein glycosylation and
RT   lifespan in Caenorhabditis elegans.";
RL   Glycobiology 23:1142-1151(2013).
CC   -!- FUNCTION: Cleaves the distal alpha 1,2-linked glucose residue from the
CC       Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor highly specifically.
CC       {ECO:0000250|UniProtKB:Q13724, ECO:0000269|PubMed:23836288}.
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   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Single-pass type II membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=a;
CC         IsoId=Q19426-1; Sequence=Displayed;
CC       Name=b;
CC         IsoId=Q19426-2; Sequence=VSP_021635;
CC       Name=c {ECO:0000312|WormBase:F13H10.4c};
CC         IsoId=Q19426-3; Sequence=VSP_021635, VSP_057602;
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown reduces lifespan to less
CC       than half of that of controls. Reduced paucimannose and complex-type
CC       glycans and increased glucosylated oligomannose glycans and fucosylated
CC       N-glycans. Chronic endoplasmic reticulum stress response is believed to
CC       be due to the accumulation of triglucosylated free oligosaccharides as
CC       a result of impaired glycan processing. {ECO:0000269|PubMed:23836288}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 63 family. {ECO:0000305}.
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DR   EMBL; Z68748; CAL36499.1; -; Genomic_DNA.
DR   EMBL; Z68748; CAL36500.1; -; Genomic_DNA.
DR   EMBL; Z68748; CAN86588.1; -; Genomic_DNA.
DR   PIR; T20864; T20864.
DR   RefSeq; NP_001076681.1; NM_001083212.3. [Q19426-1]
DR   RefSeq; NP_001076682.1; NM_001083213.3. [Q19426-2]
DR   RefSeq; NP_001122771.1; NM_001129299.2. [Q19426-3]
DR   AlphaFoldDB; Q19426; -.
DR   SMR; Q19426; -.
DR   BioGRID; 43098; 1.
DR   STRING; 6239.F13H10.4a.1; -.
DR   CAZy; GH63; Glycoside Hydrolase Family 63.
DR   GlyCosmos; Q19426; 3 sites, No reported glycans.
DR   iPTMnet; Q19426; -.
DR   EPD; Q19426; -.
DR   PaxDb; 6239-F13H10-4a; -.
DR   PeptideAtlas; Q19426; -.
DR   EnsemblMetazoa; F13H10.4a.1; F13H10.4a.1; WBGene00008775. [Q19426-1]
DR   EnsemblMetazoa; F13H10.4b.1; F13H10.4b.1; WBGene00008775. [Q19426-2]
DR   EnsemblMetazoa; F13H10.4c.1; F13H10.4c.1; WBGene00008775. [Q19426-3]
DR   EnsemblMetazoa; F13H10.4c.2; F13H10.4c.2; WBGene00008775. [Q19426-3]
DR   GeneID; 177998; -.
DR   KEGG; cel:CELE_F13H10.4; -.
DR   UCSC; F13H10.4a.1; c. elegans.
DR   AGR; WB:WBGene00008775; -.
DR   WormBase; F13H10.4a; CE40354; WBGene00008775; mogs-1. [Q19426-1]
DR   WormBase; F13H10.4b; CE40355; WBGene00008775; mogs-1. [Q19426-2]
DR   WormBase; F13H10.4c; CE40940; WBGene00008775; mogs-1. [Q19426-3]
DR   eggNOG; KOG2161; Eukaryota.
DR   GeneTree; ENSGT00390000017452; -.
DR   InParanoid; Q19426; -.
DR   OMA; DQTGYIW; -.
DR   OrthoDB; 1571at2759; -.
DR   PhylomeDB; Q19426; -.
DR   PRO; PR:Q19426; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00008775; Expressed in germ line (C elegans) and 4 other cell types or tissues.
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.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endoplasmic reticulum; Glycoprotein; Glycosidase;
KW   Hydrolase; Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..796
FT                   /note="Mannosyl-oligosaccharide glucosidase"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000057715"
FT   TOPO_DOM        1..46
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..67
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        68..796
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          70..130
FT                   /note="Required for endoplasmic reticulum targeting"
FT                   /evidence="ECO:0000250"
FT   MOTIF           2..8
FT                   /note="Endoplasmic reticulum targeting"
FT   ACT_SITE        534
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q80UM7"
FT   ACT_SITE        764
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q80UM7"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15888633"
FT   CARBOHYD        340
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        517
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761667"
FT   VAR_SEQ         1..7
FT                   /note="Missing (in isoform b and isoform c)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_021635"
FT   VAR_SEQ         303
FT                   /note="Q -> HSFR (in isoform c)"
FT                   /id="VSP_057602"
SQ   SEQUENCE   796 AA;  92646 MW;  A9DB69788CBB1F09 CRC64;
     MHREHEEMHQ PSRRRRPPRE VERPSATIRY EPVAEPEPWC SFCSWDLILI LLVMLGAGCF
     ILLHLYLYPN LEKVAPLPNI DPENAPYTWG TYRPHMYFGL RTRSPMSPLF GMMWYEQPNT
     IQRPHIRHWC NQDDRLPGYY WYEADGRHFG KQNISEAHKG VIQTDWINDA NGFAARVKLN
     MAPGRRYNVI LYLSAQEIGT RFRLGKHLSD VFHGYNELLG KFTMSLRLKD NTKLQTSHSV
     MLTDEKIPID RYHDFVVDNT QAYNAPNQPL NYILNEKHND EEGKFIAVQL NLGSQAEFDI
     ILQTEKLKGM KPEEFTNILR IRSYNFNKKY ENVFQLAGKN YTKTQLKMAK VSLSNMLGSV
     GYWYGHNRVL FNGIVQPYGP HVLFSAVPSR PFFPRGFLWD EGFHQMLIRK MDSKMTLEAI
     ASWMNAMDTS GWIPREMIVG SEAEAKVPAE FIPQKNDVAN PPTLFYVMDK LVNDEKTVGR
     YAGILKLLYP RLEKWFHWIR ITQSGPTRTT YRWRGRNETI KTELNPKTLS SGLDDFPRAS
     HPSDLEYHLD LRCWLALASR VLNRLAKSYG TDADYQRTAK AMEELNNFDS LVKDHWSEEA
     QGFFDYGKHS FDVALSPVPT PGSPRQFEYQ RVTSRAPSYT LVSDAFGYNN LFPMMLKLIP
     SKSPILKSML DKIRDPKILW TNYGLRSISR SSPYYMARNT EHDPPYWRGY IWINVNYMVL
     SSLRHYADQP GPYRENAENI FSELRANLVK NLATQFQKTG FLWENYDDRT GEGRGCHPFT
     GWSSLILLIM SDNLDT
//