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    NPY1 NAD(+) diphosphatase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 852813, updated on 9-Dec-2024

    Summary

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    Official Symbol
    NPY1
    Official Full Name
    NAD(+) diphosphatase
    Primary source
    SGD:S000003035
    Locus tag
    YGL067W
    See related
    AllianceGenome:SGD:S000003035; FungiDB:YGL067W; VEuPathDB:YGL067W
    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 NAD+ diphosphatase activity. Involved in NADH metabolic process. Acts upstream of or within NAD-cap decapping. Located in peroxisome. Orthologous to human NUDT12 (nudix hydrolase 12). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See NPY1 in Genome Data Viewer
    Location:
    chromosome: VII
    Exon count:
    1
    Sequence:
    Chromosome: VII; NC_001139.9 (376101..377255)

    Chromosome VII - NC_001139.9Genomic Context describing neighboring genes Neighboring gene DNA-directed RNA polymerase II core subunit RPB9 Neighboring gene mitochondrial 54S ribosomal protein MNP1 Neighboring gene deubiquitination module subunit SGF73 Neighboring gene GDP-Man:Man(1)GlcNAc(2)-PP-dolichol alpha-1,3-mannosyltransferase

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001139.9

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Structural insights into dpCoA-RNA decapping by NudC. Zhou W, et al. RNA Biol, 2021 Oct 15. PMID 34074215, Free PMC Article
    2. The NADH diphosphatase encoded by the Saccharomyces cerevisiae NPY1 nudix hydrolase gene is located in peroxisomes. AbdelRaheim SR, et al. Arch Biochem Biophys, 2001 Apr 1. PMID 11361135
    3. Extensive 5'-surveillance guards against non-canonical NAD-caps of nuclear mRNAs in yeast. Zhang Y, et al. Nat Commun, 2020 Nov 2. PMID 33139726, Free PMC Article
    4. Cloning and characterization of the NADH pyrophosphatases from Caenorhabditis elegans and Saccharomyces cerevisiae, members of a Nudix hydrolase subfamily. Xu W, et al. Biochem Biophys Res Commun, 2000 Jul 5. PMID 10873676
    5. Multiple Nudix family proteins possess mRNA decapping activity. Song MG, et al. RNA, 2013 Mar. PMID 23353937, Free PMC Article

    See all (25) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Pathways from PubChem

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    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 NAD+ diphosphatase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables NAD+ diphosphatase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables NADH pyrophosphatase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables NADH pyrophosphatase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables RNA NAD-cap (NMN-forming) hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding 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 NAD catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within NAD-cap decapping IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in NADH metabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in NADH metabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in NADP catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within RNA decapping IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    located_in cytosol HDA PubMed 
    is_active_in peroxisome IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in peroxisome IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in peroxisome IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    NAD(+) diphosphatase
    NP_011448.3
    • NADH diphosphatase (pyrophosphatase); hydrolyzes the pyrophosphate linkage in NADH and related nucleotides; localizes to peroxisomes; enzymatic component of one of several partly redundant surveillance pathways involved in decapping of non-canonical nicotinamide adenine dinucleotide (NAD) capped nuclear mRNAs (NAD-RNAs); also possesses deCoAping activity involved in the decapping of non-canonical dephospho-CoA capped RNA (dpCoA-RNA); nudix hydrolase family member

    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_001139.9 Reference assembly

      Range
      376101..377255
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001180932.3 → NP_011448.3  TPA: NAD(+) diphosphatase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_011448.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VU74, E9P928, P53164
      UniProtKB/TrEMBL
      A6ZUA9, B3LHD6, C8Z8H9, N1P372
      Conserved Domains (1) summary
      COG2816
      Location:13 → 371
      NPY1; NADH pyrophosphatase NudC, Nudix superfamily [Nucleotide transport and metabolism]
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P53164.1

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