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PNG1 peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase [ Saccharomyces cerevisiae S288C ]

Gene ID: 856009, updated on 28-Oct-2024

Summary

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Official Symbol
PNG1
Official Full Name
peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase
Primary source
SGD:S000006017
Locus tag
YPL096W
See related
AllianceGenome:SGD:S000006017; FungiDB:YPL096W; VEuPathDB:YPL096W
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary
Enables peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity. Involved in protein deglycosylation; protein quality control for misfolded or incompletely synthesized proteins; and ubiquitin-dependent glycoprotein ERAD pathway. Located in cytosol and nucleus. Used to study congenital disorder of deglycosylation 1. Human ortholog(s) of this gene implicated in congenital disorder of deglycosylation 1. Orthologous to human NGLY1 (N-glycanase 1). [provided by Alliance of Genome Resources, Oct 2024]
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Genomic context

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See PNG1 in Genome Data Viewer
Location:
chromosome: XVI
Exon count:
1
Sequence:
Chromosome: XVI; NC_001148.4 (366927..368018)

Chromosome XVI - NC_001148.4Genomic Context describing neighboring genes Neighboring gene tyrosine--tRNA ligase MSY1 Neighboring gene Eri1p Neighboring gene medium-chain fatty acid ethyl ester synthase/esterase Neighboring gene Sec63 complex subunit SEC62

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_001148.4

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Influence of substrate conformation on the deglycosylation of ribonuclease B by recombinant yeast peptide:N-glycanase. Wang S, et al. Acta Biochim Biophys Sin (Shanghai), 2007 Jan. PMID 17213953
  2. A simple, sensitive in vitro assay for cytoplasmic deglycosylation by peptide: N-glycanase. Suzuki T. Methods, 2005 Apr. PMID 15804608
  3. Fluorescently labeled inhibitor for profiling cytoplasmic peptide:N-glycanase. Hagihara S, et al. Glycobiology, 2007 Oct. PMID 17640972
  4. Site-directed mutagenesis study of yeast peptide:N-glycanase. Insight into the reaction mechanism of deglycosylation. Katiyar S, et al. J Biol Chem, 2002 Apr 12. PMID 11812789
  5. Structural and mutational studies on the importance of oligosaccharide binding for the activity of yeast PNGase. Zhao G, et al. Glycobiology, 2009 Feb. PMID 18854368, Free PMC Article

See all (55) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Dynamic simulations of the wild type and N-terminal H1 deletion mutant implied that Png1p-DeltaH1 is more flexible than wild type Png1p.
    Title: N-terminal deletion of peptide:N-glycanase results in enhanced deglycosylation activity.
  2. the crystal structure of yeast PNGase in complex with N,N'-diacetylchitobiose (chitobiose).
    Title: Structural and mutational studies on the importance of oligosaccharide binding for the activity of yeast PNGase.
  3. Data demonstrate that the efficient degradation of glycosylated ricin A chain requires the Png1-Rad23 complex, suggesting that this complex couples protein deglycosylation and degradation.
    Title: The Png1-Rad23 complex regulates glycoprotein turnover.
  4. analysis of peptide:N-glycanase-Rad23 complex structure
    Title: Structure of a peptide:N-glycanase-Rad23 complex: insight into the deglycosylation for denatured glycoproteins.
Submit: New GeneRIF Correction

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Homology

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity IEA
Inferred from Electronic Annotation
more info
  
enables zinc ion binding RCA
inferred from Reviewed Computational Analysis
more info
 PubMed 
Process Evidence Code Pubs
involved_in ERAD pathway IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in protein deglycosylation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in protein deglycosylation IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in protein quality control for misfolded or incompletely synthesized proteins IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in ubiquitin-dependent glycoprotein ERAD pathway IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
located_in mitochondrion HDA PubMed 
located_in nucleus IDA
Inferred from Direct Assay
more info
 PubMed 
located_in nucleus IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase
NP_015229.1
  • Conserved peptide N-glycanase; deglycosylating enzyme that cleaves N-glycans that are attached to misfolded ERAD substrate glycoproteins prior to proteasome-dependent degradation; localizes to the cytoplasm and nucleus; activity is enhanced by interaction with Rad23p; human ortholog NGLY1 is associated with a syndrome characterized by developmental delays, epilepsy, absence of tears and liver disease

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_001148.4 Reference assembly

    Range
    366927..368018
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001183910.1 → NP_015229.1  TPA: peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_015229.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6W3S1, Q02890
    UniProtKB/TrEMBL
    A6ZWF5, B3LKX7, C7GJ50, C8ZIT4, N1NX60
    Conserved Domains (2) summary
    smart00460
    Location:183 → 237
    TGc; Transglutaminase/protease-like homologues
    cl10615
    Location:220 → 274
    sm_acid_XPC-like; small acidic domain of Xeroderma pigmentosum group C complementing protein and similar proteins
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
Q02890.1

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