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Protein

Mannosyl-oligosaccharide glucosidase

Gene

mogs-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves the distal alpha 1,2-linked glucose residue from the Glc3Man9GlcNAc2 oligosaccharide precursor highly specifically.By similarity1 Publication

Catalytic activityi

Exohydrolysis of the non-reducing terminal glucose residues in the mannosyl-oligosaccharide Glc3Man9GlcNAc2.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

ReactomeiREACT_320893. N-glycan trimming in the ER and Calnexin/Calreticulin cycle.

Protein family/group databases

CAZyiGH63. Glycoside Hydrolase Family 63.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannosyl-oligosaccharide glucosidaseImported (EC:3.2.1.106By similarity)
Alternative name(s):
Processing A-glucosidase IBy similarity
Gene namesi
Name:mogs-1Imported
Synonyms:agl-11 Publication
ORF Names:F13H10.4Imported
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940 Componenti: Chromosome IV

Organism-specific databases

WormBaseiF13H10.4a; CE40354; WBGene00008775; mogs-1.
F13H10.4b; CE40355; WBGene00008775; mogs-1.
F13H10.4c; CE40940; WBGene00008775; mogs-1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4646CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei47 – 6721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini68 – 796729LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

RNAi-mediated knockdown reduces lifespan to less than half of that of controls. Reduced paucimannose and complex-type glycans and increased glucosylated oligomannose glycans and fucosylated N-glycans. Chronic endoplasmic reticulum stress response is believed to be due to the accumulation of triglucosylated free oligosaccharides as a result of impaired glycan processing.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 796796Mannosyl-oligosaccharide glucosidaseCuratedPRO_0000057715Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi153 – 1531N-linked (GlcNAc...)1 Publication
Glycosylationi340 – 3401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi517 – 5171N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ19426.

Expressioni

Gene expression databases

ExpressionAtlasiQ19426. baseline and differential.

Interactioni

Protein-protein interaction databases

STRINGi6239.F13H10.4a.2.

Structurei

3D structure databases

ProteinModelPortaliQ19426.
SMRiQ19426. Positions 84-790.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni70 – 13061Required for endoplasmic reticulum targetingBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi2 – 87Endoplasmic reticulum targeting

Sequence similaritiesi

Belongs to the glycosyl hydrolase 63 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG305138.
GeneTreeiENSGT00390000017452.
HOGENOMiHOG000201473.
InParanoidiQ19426.
KOiK01228.
OMAiGFAARVK.
PhylomeDBiQ19426.

Family and domain databases

InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR004888. Glycoside_hydrolase_63.
[Graphical view]
PANTHERiPTHR10412:SF1. PTHR10412:SF1. 1 hit.
PfamiPF03200. Glyco_hydro_63. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 2 hits.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform a (identifier: Q19426-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MHREHEEMHQ PSRRRRPPRE VERPSATIRY EPVAEPEPWC SFCSWDLILI
60 70 80 90 100
LLVMLGAGCF ILLHLYLYPN LEKVAPLPNI DPENAPYTWG TYRPHMYFGL
110 120 130 140 150
RTRSPMSPLF GMMWYEQPNT IQRPHIRHWC NQDDRLPGYY WYEADGRHFG
160 170 180 190 200
KQNISEAHKG VIQTDWINDA NGFAARVKLN MAPGRRYNVI LYLSAQEIGT
210 220 230 240 250
RFRLGKHLSD VFHGYNELLG KFTMSLRLKD NTKLQTSHSV MLTDEKIPID
260 270 280 290 300
RYHDFVVDNT QAYNAPNQPL NYILNEKHND EEGKFIAVQL NLGSQAEFDI
310 320 330 340 350
ILQTEKLKGM KPEEFTNILR IRSYNFNKKY ENVFQLAGKN YTKTQLKMAK
360 370 380 390 400
VSLSNMLGSV GYWYGHNRVL FNGIVQPYGP HVLFSAVPSR PFFPRGFLWD
410 420 430 440 450
EGFHQMLIRK MDSKMTLEAI ASWMNAMDTS GWIPREMIVG SEAEAKVPAE
460 470 480 490 500
FIPQKNDVAN PPTLFYVMDK LVNDEKTVGR YAGILKLLYP RLEKWFHWIR
510 520 530 540 550
ITQSGPTRTT YRWRGRNETI KTELNPKTLS SGLDDFPRAS HPSDLEYHLD
560 570 580 590 600
LRCWLALASR VLNRLAKSYG TDADYQRTAK AMEELNNFDS LVKDHWSEEA
610 620 630 640 650
QGFFDYGKHS FDVALSPVPT PGSPRQFEYQ RVTSRAPSYT LVSDAFGYNN
660 670 680 690 700
LFPMMLKLIP SKSPILKSML DKIRDPKILW TNYGLRSISR SSPYYMARNT
710 720 730 740 750
EHDPPYWRGY IWINVNYMVL SSLRHYADQP GPYRENAENI FSELRANLVK
760 770 780 790
NLATQFQKTG FLWENYDDRT GEGRGCHPFT GWSSLILLIM SDNLDT
Note: No experimental confirmation available.
Length:796
Mass (Da):92,646
Last modified:November 28, 2006 - v2
Checksum:iA9DB69788CBB1F09
GO
Isoform b (identifier: Q19426-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: Missing.

Note: No experimental confirmation available.
Show »
Length:789
Mass (Da):91,697
Checksum:i6A1A86F3F3752028
GO
Isoform cImported (identifier: Q19426-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: Missing.
     303-303: Q → HSFR

Note: No experimental confirmation available.
Show »
Length:792
Mass (Da):92,096
Checksum:iBBC7B82F261F31B0
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 77Missing in isoform b and isoform c. CuratedVSP_021635
Alternative sequencei303 – 3031Q → HSFR in isoform c. VSP_057602

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z68748 Genomic DNA. Translation: CAL36499.1.
Z68748 Genomic DNA. Translation: CAL36500.1.
Z68748 Genomic DNA. Translation: CAN86588.1.
PIRiT20864.
RefSeqiNP_001076681.1. NM_001083212.3. [Q19426-1]
NP_001076682.1. NM_001083213.3. [Q19426-2]
NP_001122771.1. NM_001129299.2. [Q19426-3]
UniGeneiCel.17548.

Genome annotation databases

EnsemblMetazoaiF13H10.4a; F13H10.4a; WBGene00008775. [Q19426-1]
F13H10.4c.1; F13H10.4c.1; WBGene00008775. [Q19426-3]
F13H10.4c.2; F13H10.4c.2; WBGene00008775. [Q19426-3]
GeneIDi177998.
KEGGicel:CELE_F13H10.4.
UCSCiF13H10.4a.1. c. elegans. [Q19426-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z68748 Genomic DNA. Translation: CAL36499.1.
Z68748 Genomic DNA. Translation: CAL36500.1.
Z68748 Genomic DNA. Translation: CAN86588.1.
PIRiT20864.
RefSeqiNP_001076681.1. NM_001083212.3. [Q19426-1]
NP_001076682.1. NM_001083213.3. [Q19426-2]
NP_001122771.1. NM_001129299.2. [Q19426-3]
UniGeneiCel.17548.

3D structure databases

ProteinModelPortaliQ19426.
SMRiQ19426. Positions 84-790.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.F13H10.4a.2.

Protein family/group databases

CAZyiGH63. Glycoside Hydrolase Family 63.

Proteomic databases

PaxDbiQ19426.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF13H10.4a; F13H10.4a; WBGene00008775. [Q19426-1]
F13H10.4c.1; F13H10.4c.1; WBGene00008775. [Q19426-3]
F13H10.4c.2; F13H10.4c.2; WBGene00008775. [Q19426-3]
GeneIDi177998.
KEGGicel:CELE_F13H10.4.
UCSCiF13H10.4a.1. c. elegans. [Q19426-1]

Organism-specific databases

CTDi177998.
WormBaseiF13H10.4a; CE40354; WBGene00008775; mogs-1.
F13H10.4b; CE40355; WBGene00008775; mogs-1.
F13H10.4c; CE40940; WBGene00008775; mogs-1.

Phylogenomic databases

eggNOGiNOG305138.
GeneTreeiENSGT00390000017452.
HOGENOMiHOG000201473.
InParanoidiQ19426.
KOiK01228.
OMAiGFAARVK.
PhylomeDBiQ19426.

Enzyme and pathway databases

ReactomeiREACT_320893. N-glycan trimming in the ER and Calnexin/Calreticulin cycle.

Miscellaneous databases

NextBioi899290.
PROiQ19426.

Gene expression databases

ExpressionAtlasiQ19426. baseline and differential.

Family and domain databases

InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR004888. Glycoside_hydrolase_63.
[Graphical view]
PANTHERiPTHR10412:SF1. PTHR10412:SF1. 1 hit.
PfamiPF03200. Glyco_hydro_63. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
    Strain: Bristol N2.
  2. "Identification of the hydrophobic glycoproteins of Caenorhabditis elegans."
    Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.
    Glycobiology 15:952-964(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-153, IDENTIFICATION BY MASS SPECTROMETRY.
  3. "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins."
    Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T.
    Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-517, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Bristol N2.
  4. "Deficiency of alpha-glucosidase I alters glycoprotein glycosylation and lifespan in Caenorhabditis elegans."
    Katoh T., Takase J., Tani Y., Amamoto R., Aoshima N., Tiemeyer M., Yamamoto K., Ashida H.
    Glycobiology 23:1142-1151(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiMOGS1_CAEEL
AccessioniPrimary (citable) accession number: Q19426
Secondary accession number(s): A5JYS7, Q0G829, Q0G830
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 28, 2006
Last modified: June 24, 2015
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.