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Protein

Mannosyl-oligosaccharide glucosidase

Gene

Mogs

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Cleaves the distal alpha 1,2-linked glucose residue from the Glc3Man9GlcNAc2 oligosaccharide precursor.By similarity

Catalytic activityi

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

Pathwayi: N-glycan degradation

This protein is involved in the pathway N-glycan degradation, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway N-glycan degradation and in Glycan metabolism.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase

Enzyme and pathway databases

ReactomeiR-MMU-532668. N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
UniPathwayiUPA00280.

Protein family/group databases

CAZyiGH63. Glycoside Hydrolase Family 63.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannosyl-oligosaccharide glucosidase (EC:3.2.1.106)
Alternative name(s):
Glucosidase 1
Glycoprotein-processing glucosidase I
Gene namesi
Name:Mogs
Synonyms:Gcs1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1929872. Mogs.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 43CytoplasmicSequence analysisAdd BLAST43
Transmembranei44 – 64Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini65 – 834LumenalSequence analysisAdd BLAST770

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000577111 – 834Mannosyl-oligosaccharide glucosidaseAdd BLAST834

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi654N-linked (GlcNAc...) asparagineBy similarity1

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ80UM7.
MaxQBiQ80UM7.
PaxDbiQ80UM7.
PRIDEiQ80UM7.

PTM databases

iPTMnetiQ80UM7.
PhosphoSitePlusiQ80UM7.
SwissPalmiQ80UM7.

Expressioni

Gene expression databases

BgeeiENSMUSG00000030036.
CleanExiMM_GCS1.
GenevisibleiQ80UM7. MM.

Interactioni

Protein-protein interaction databases

BioGridi208276. 3 interactors.
IntActiQ80UM7. 6 interactors.
MINTiQ80UM7.
STRINGi10090.ENSMUSP00000032114.

Structurei

Secondary structure

1834
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi63 – 69Combined sources7
Turni81 – 84Combined sources4
Turni86 – 88Combined sources3
Helixi90 – 92Combined sources3
Beta strandi93 – 95Combined sources3
Beta strandi101 – 109Combined sources9
Beta strandi114 – 123Combined sources10
Beta strandi144 – 150Combined sources7
Beta strandi152 – 162Combined sources11
Beta strandi165 – 174Combined sources10
Turni177 – 180Combined sources4
Beta strandi182 – 191Combined sources10
Beta strandi201 – 209Combined sources9
Beta strandi228 – 233Combined sources6
Turni234 – 236Combined sources3
Beta strandi237 – 243Combined sources7
Beta strandi258 – 265Combined sources8
Helixi269 – 271Combined sources3
Helixi272 – 279Combined sources8
Beta strandi282 – 286Combined sources5
Beta strandi294 – 299Combined sources6
Beta strandi315 – 335Combined sources21
Turni336 – 338Combined sources3
Helixi342 – 345Combined sources4
Helixi351 – 365Combined sources15
Turni368 – 370Combined sources3
Helixi382 – 397Combined sources16
Beta strandi400 – 404Combined sources5
Beta strandi407 – 409Combined sources3
Beta strandi429 – 433Combined sources5
Helixi446 – 459Combined sources14
Helixi461 – 472Combined sources12
Beta strandi483 – 485Combined sources3
Helixi489 – 492Combined sources4
Helixi497 – 499Combined sources3
Helixi513 – 522Combined sources10
Helixi525 – 532Combined sources8
Helixi535 – 548Combined sources14
Helixi575 – 577Combined sources3
Helixi595 – 615Combined sources21
Helixi618 – 632Combined sources15
Helixi634 – 641Combined sources8
Turni644 – 647Combined sources4
Beta strandi652 – 655Combined sources4
Beta strandi659 – 664Combined sources6
Turni665 – 667Combined sources3
Beta strandi668 – 673Combined sources6
Beta strandi679 – 682Combined sources4
Helixi689 – 691Combined sources3
Helixi692 – 695Combined sources4
Helixi706 – 714Combined sources9
Turni716 – 719Combined sources4
Beta strandi724 – 728Combined sources5
Beta strandi746 – 749Combined sources4
Helixi753 – 766Combined sources14
Helixi774 – 778Combined sources5
Helixi781 – 799Combined sources19
Beta strandi804 – 806Combined sources3
Turni808 – 810Combined sources3
Beta strandi813 – 818Combined sources6
Helixi822 – 825Combined sources4
Helixi826 – 831Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5MHFX-ray2.10A/B/C/D59-834[»]
ProteinModelPortaliQ80UM7.
SMRiQ80UM7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni74 – 136Required for endoplasmic reticulum targetingBy similarityAdd BLAST63

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi3 – 9Endoplasmic reticulum targeting7

Sequence similaritiesi

Belongs to the glycosyl hydrolase 63 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2161. Eukaryota.
ENOG410XTHA. LUCA.
GeneTreeiENSGT00390000017452.
HOGENOMiHOG000201473.
InParanoidiQ80UM7.
KOiK01228.
OMAiENYWRSP.
OrthoDBiEOG091G07DR.
PhylomeDBiQ80UM7.
TreeFamiTF300749.

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
2.70.98.110. 1 hit.
InterProiView protein in InterPro
IPR008928. 6-hairpin_glycosidase_sf.
IPR012341. 6hp_glycosidase-like_sf.
IPR031335. Glyco_hydro_63_C.
IPR031631. Glyco_hydro_63N.
IPR038518. Glyco_hydro_63N_sf.
IPR004888. Glycoside_hydrolase_63.
PANTHERiPTHR10412. PTHR10412. 1 hit.
PfamiView protein in Pfam
PF03200. Glyco_hydro_63. 1 hit.
PF16923. Glyco_hydro_63N. 1 hit.
SUPFAMiSSF48208. SSF48208. 1 hit.

Sequencei

Sequence statusi: Complete.

Q80UM7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARGERRRRA AAAEGARPLE RARAAGRRDG RAGGARGSAS GAALAVVVLA
60 70 80 90 100
LAFGLSGRWV LAWLRVRRAL TLHPAPSALP PDSSSPAVAP ELFWGTYRPH
110 120 130 140 150
VYFGMKTRSP KPLLTGLMWA QQGATPGTPP KLRHTCEQGD GVGPYGWEFH
160 170 180 190 200
DGRTFGRQHI HDGALRLTTE FVKRPGGQHG GDWSWRVTVE PQASGTPSFP
210 220 230 240 250
LVSLFFYVVT DGQEVLLPEI GAKGQLKSIS GHTSELGDFR LTLLPPTSPG
260 270 280 290 300
DTVPKHGSYN VFWSSNPGLP QLTDMVKSRL NSWFQHRPPG ASPDRYLGLP
310 320 330 340 350
GSLKWEERGP SGQGQFLIQQ VTLKAPFSVE FVFESGSAAT GGNQASGRLV
360 370 380 390 400
GSQLTQALES HAAAFKERFE KTFQLKEKGL SPEEQALGQV ALSGLLGGIG
410 420 430 440 450
YFYGQGLVLP DTSMEGSEQK MDPALFPPVP LFSGVPSRSF FPRGFLWDEG
460 470 480 490 500
FHQLVVQRWD PHLTREALGH WLGLLNADGW IGREQILGDE ARARVPPEFL
510 520 530 540 550
VQRAAHANPP TLLLPVVHML EGHDPDDLAF LRKAFPRLHA WFSWLHQSQA
560 570 580 590 600
GPVPLSYRWR GRDLALPTLL NPKTLPSGLD DYPRASHPST AERHLDLRCW
610 620 630 640 650
VALGARVLSQ LAEQLGETEA AAELGPLAAS LEEPGSLDEL HWAPELGVFA
660 670 680 690 700
DFGNHTKAVQ LKSRPPQGLV RVVGRPPPRL QYVDALGYVS LFPLLLQLLD
710 720 730 740 750
PSSPRLGPLL DVLADSRHLW SPFGLRSLSA SSLFYKQRNT EHDPPYWRGA
760 770 780 790 800
VWLNINYLAL GALHHYGHVE GPHKVQAAKL YHELRANVVR NVRQQYQATG
810 820 830
FLWEQYSDQD GRGMGCRPFQ GWTSLVLLIM AEEY
Length:834
Mass (Da):91,831
Last modified:June 1, 2003 - v1
Checksum:iCB2728BE16EACD0E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti749G → S in AAD00906 (PubMed:10406845).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF001797 Genomic DNA. Translation: AAD00906.1.
BC051949 mRNA. Translation: AAH51949.1.
CCDSiCCDS20273.1.
RefSeqiNP_065644.2. NM_020619.2.
UniGeneiMm.28188.

Genome annotation databases

EnsembliENSMUST00000032114; ENSMUSP00000032114; ENSMUSG00000030036.
GeneIDi57377.
KEGGimmu:57377.
UCSCiuc009cmn.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiMOGS_MOUSE
AccessioniPrimary (citable) accession number: Q80UM7
Secondary accession number(s): Q9Z2W5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2003
Last modified: March 28, 2018
This is version 122 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome