A0A139WB11 · A0A139WB11_TRICA

Function

function

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

Catalytic activity

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentendoplasmic reticulum membrane
Molecular FunctionGlc3Man9GlcNAc2 oligosaccharide glucosidase activity
Biological Processoligosaccharide metabolic process
Biological Processprotein N-linked glycosylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Mannosyl-oligosaccharide glucosidase
  • EC number

Gene names

    • Name
      AUGUSTUS-3.0.2_31384
    • ORF names
      TcasGA2_TC031384

Organism names

  • Taxonomic identifier
  • Strain
    • Georgia GA2
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Coleoptera > Polyphaga > Cucujiformia > Tenebrionidae > Tenebrionidae incertae sedis > Tribolium

Accessions

  • Primary accession
    A0A139WB11

Proteomes

Subcellular Location

Endoplasmic reticulum membrane
; Single-pass type II membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane41-62Helical

Keywords

PTM/Processing

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-32Disordered
Compositional bias10-32Polar residues
Domain88-272Glycosyl hydrolase family 63 N-terminal
Domain329-798Glycosyl hydrolase family 63 C-terminal
Domain858-1099MMS19 N-terminal
Domain1404-1653MMS19 C-terminal

Sequence similarities

Belongs to the MET18/MMS19 family.
Belongs to the glycosyl hydrolase 63 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,702
  • Mass (Da)
    193,322
  • Last updated
    2016-05-11 v1
  • Checksum
    591B3AB9190C5B0F
MARQRRTQGAADPNKGTNSSSSNGSNSTNNRSSKSTSLLSYWKQIIGCIVLGIAVSLGYMGYLETRVNTPFDDKKMVVKSGLQVPEQFWGTYRPGLYFGLKTRDPTSLVTGLMWYFPKRLRPGGDGIRHWCEQGDGLEKYGWVKHDGSNFGVQEIIDGGYNIDTSFVKRLGGSHGGDWTARISVTKPGASEDVSLIWYTALDEETKGFISLTNSATKFTGIKGETTGLGEFTIKFTNNSGVVSHESFLSTVAPGLHLLKETVVGSLRLAQDKPNSPRRIVLGGEILPETGTGKAQPNFVAVQLTGKVPFSIDVVFESGSFGTRQDTLVGETYSKALAWHVARFGQRFEDTFGLHKKGYGPKEVTFAQSALSNMLGGIGYFYGTSKVQSFYTKEPVHYWHAPLYTAVPSRSFFPRGFLWDEGFHGFLIATWDLDLELDIISHWFDLMNVEGWIPREQILGVEAIAKIPEEFIVQRNTNANPPTFFLTLQYILRKYYDKLSEGRLATLERLYPRLQAWFAWFNTTQKGAGPGMYRWRGRDATTNRELNPKTLTSGLDDYPRASHPTEAEYHVDLYCWIAIASDTLARLATLLDRDGYKYEQTADYLKDNFLLDNLHWSNYASRYADYGYHTDSVKLKRPKPLPRSQNQNMEMVRVTLKNPEYRLVDSTFGYVSLFPFLLQMIDSDSLKLGQILDDLRNPDLLWTKFGLRSLSKNSPLYMKRNTEHDPPYWRGQIWININFLAVRSLYFYANTEGPYRDKANAIYKDLRENVIKNVMTQYFKTGYLWEQYNDETGEGSGCYSRLFGACVVNYHLSKSLVMMASNLAKNFENVTIDDQEFAEKCHELAQALESGQVTLLRLVEDLGGLLIDTSPKGRELGMWVLTRVVETLPPDVLDENQLKFLNQFYTDRLKDNHFVLPAVLRGFLALIRCEGAPKGGPGPFLVQLFHNVSCQQQQENDRLAIYQIFETCLEKFWPELDEMGPDFVYGVISAVDGERSPKNLIFLFDWFPKFLRKVKLGHLAEDAFEILACYFPVDFRAPPQDENGITRNTLAEKLAFCLVAVPQFAEFSLQLALEKFDSSLEIAKLDSLRLIELSFVTFDISPTTVWPLIQKELFQTTNPAIEKACLTTMTAVIKHTRDPNLTETVKDICDTIKGNFLPDSKLFQPSARLIISVANASDSVANLVARETVPILTNMYNIANTTAEKTPFLRLLTDLYALASDLENLGEVPVLLVKSDSPIAFDCLRDISPKLPEKIRLLLYQNYVKLLQVPQEGAVLQCLEALARDYPNEVATHVVGNTENYTPCFLDALCVTLANQKFFTAHLIDLILKNCAIKTLQKVLIKFDDCDAIFDVLNAQNITHVLIEMALTGDTCHETIAFVLKIVIGRMSSEKQNEMIRNELSRIKIEDIFLLSGILTCLRRDVVINYEILSELIEFIIRERDNLRRNAAIELVANILNKCPNDDVIREFLERVDTKTDPILTSWLTKALIMRNHELGTFWTTKLIDYLDKDESIAPCFRTIMSNSESLSTKSHCNVAFLYQQKFFTIVTNKLSANYSPDKNSYLSGLGYLLEFAPKPAVLVQFRKISKLIISCLDHTTNHEILIVILRLIRDFITTKEQVIEENLGIFLARFLKLATYDKSMKVRILALQCLQEVTSKFPIFMLLPHKNDVLKVLGQVIDDKKRIVRREAVEARSMWFLLDFDK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias10-32Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KQ971379
EMBL· GenBank· DDBJ
KYB25099.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp