A0A6I8Q741 · A0A6I8Q741_XENTR

Function

function

Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins.

Catalytic activity

  • Hydrolysis of an N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.
    EC:3.5.1.52 (UniProtKB | ENZYME | Rhea)

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionmetal ion binding
Molecular Functionpeptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity
Biological Processglycoprotein catabolic process

Keywords

  • Molecular function
  • Ligand
    • #Zinc

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase
  • EC number
  • Alternative names
    • N-glycanase 1
    • Peptide:N-glycanase

Gene names

    • Name
      ngly1

Organism names

Accessions

  • Primary accession
    A0A6I8Q741

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Expression

Gene expression databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region99-135Disordered
Compositional bias103-118Polar residues
Compositional bias119-135Pro residues
Domain435-635PAW

Sequence similarities

Belongs to the transglutaminase-like superfamily. PNGase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    635
  • Mass (Da)
    72,511
  • Last updated
    2021-06-02 v2
  • Checksum
    F4E278BF2DAFA6D1
MAALDSPAVAELCQNERQEFLDASQLLLTYADNILRSPNEEKYRSIRIGNTAFSTRLLPVRGAIECLFEMGFEEGETHLVFPKMASVEKLRKVRDHIATERNKRMSGANSTPQATPSTPPMSSRSPVPNPVPPSIPLQATEDISSFLASEVRYLKTLQSNSQHVLIYEQSELQQRALQEIPVLDLKTRAQQKLTEVKSIDSDTGVNIEDFLLLELLRWFKQDFFQWVNSLPCCLCGGETQGRDALSPSAEDLRWGANRVENHYCEKCKHSNRFPRYNHPEKLLETRRGRCGEWANCFTLCCRALGFEARYVWDSTDHVWTEVYSTSQNRWLHCDPCENACDKPLLYEVGWGKKLSYIIGFSKDEVVDVTWRYSCKHEDVIARRKEVRESWLRETITGLNKMRQVSLPENRKQELLGRLIVELVEFMSPKTPKPGELGGRVSGSLAWRMARGETSLQSNKSVVFIPSEREKIGKLFHLRYNVVEDAYTRVSNNNEVITGWENGVWKAESMCRKVENDWKMVYLARTEGSSSAAISWKIECASVGLQIESLSVRTSGQTFHSGKIKWKLTSPEVEVEVNSDTSLHSYPEFLNSSEVELKAELCDGDGNTAWQHTQLFRESLDCKQNSLEIIIMLKDV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias103-118Polar residues
Compositional bias119-135Pro residues

Keywords

Sequence databases

Genome annotation databases

Similar Proteins

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