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    YPC1 phytoceramidase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 852481, updated on 9-Dec-2024

    Summary

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    Official Symbol
    YPC1
    Official Full Name
    phytoceramidase
    Primary source
    SGD:S000000387
    Locus tag
    YBR183W
    See related
    AllianceGenome:SGD:S000000387; FungiDB:YBR183W; VEuPathDB:YBR183W
    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 N-acylsphingosine amidohydrolase activity and sphingosine N-acyltransferase activity. Involved in ceramide biosynthetic process and ceramide catabolic process. Located in cortical endoplasmic reticulum. Used to study leukodystrophy. Orthologous to human ACER3 (alkaline ceramidase 3). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See YPC1 in Genome Data Viewer
    Location:
    chromosome: II
    Exon count:
    1
    Sequence:
    Chromosome: II; NC_001134.8 (596115..597065)

    Chromosome II - NC_001134.8Genomic Context describing neighboring genes Neighboring gene Smp1p Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein Neighboring gene Mba1p

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001134.8

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Cloning of an alkaline ceramidase from Saccharomyces cerevisiae. An enzyme with reverse (CoA-independent) ceramide synthase activity. Mao C, et al. J Biol Chem, 2000 Mar 10. PMID 10702247
    2. Membrane topology of yeast alkaline ceramidase YPC1. Ramachandra N, et al. Biochem J, 2013 Jun 15. PMID 23445175
    3. Cloning and characterization of a Saccharomyces cerevisiae alkaline ceramidase with specificity for dihydroceramide. Mao C, et al. J Biol Chem, 2000 Oct 6. PMID 10900202
    4. Molecular cloning and characterization of OsCDase, a ceramidase enzyme from rice. Pata MO, et al. Plant J, 2008 Sep. PMID 18547394, Free PMC Article
    5. Sphingolipids function as downstream effectors of a fungal PAQR. Villa NY, et al. Mol Pharmacol, 2009 Apr. PMID 19066337, Free PMC Article

    See all (43) 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 N-acylsphingosine amidohydrolase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables N-acylsphingosine amidohydrolase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables sphingosine N-acyltransferase activity IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    enables sphingosine N-acyltransferase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in ceramide biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in ceramide biosynthetic process IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in ceramide catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in ceramide catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in ceramide metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in sphingolipid metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cortical endoplasmic reticulum IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in endoplasmic reticulum HDA PubMed 
    located_in endoplasmic reticulum IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in endoplasmic reticulum IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in endoplasmic reticulum membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in endoplasmic reticulum membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in membrane IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    phytoceramidase
    NP_009742.1
    • Alkaline ceramidase; also has reverse (CoA-independent) ceramide synthase activity; catalyzes both breakdown and synthesis of phytoceramide; overexpression confers fumonisin B1 resistance; YPC1 has a paralog, YDC1, that arose from the whole genome duplication

    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_001134.8 Reference assembly

      Range
      596115..597065
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001178531.1 → NP_009742.1  TPA: phytoceramidase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_009742.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VQH8, P38298
      UniProtKB/TrEMBL
      A6ZLC4, B3LMX8, C7GQ29, D3UES7, G2W9I5, N1P9J6
      Conserved Domains (1) summary
      pfam05875
      Location:15 → 285
      Ceramidase
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P38298.1

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