MOGS1_CAEEL
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 03-AUG-2022, entry version 143.
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)-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 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 STRING; 6239.F13H10.4a; -.
DR CAZy; GH63; Glycoside Hydrolase Family 63.
DR iPTMnet; Q19426; -.
DR EPD; Q19426; -.
DR PaxDb; Q19426; -.
DR PeptideAtlas; Q19426; -.
DR PRIDE; 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 CTD; 177998; -.
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; IAPDEFH; -.
DR OrthoDB; 278028at2759; -.
DR PhylomeDB; Q19426; -.
DR PRO; PR:Q19426; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00008775; Expressed in germ line (C elegans) and 4 other tissues.
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 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 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
