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

    Gene ID: 856009, updated on 9-Dec-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, Dec 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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    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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