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    PLB3 lysophospholipase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 854151, updated on 2-Nov-2024

    Summary

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    Official Symbol
    PLB3
    Official Full Name
    lysophospholipase
    Primary source
    SGD:S000005371
    Locus tag
    YOL011W
    See related
    AllianceGenome:SGD:S000005371; FungiDB:YOL011W; VEuPathDB:YOL011W
    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 lysophospholipase activity. Involved in phosphatidylinositol metabolic process and phosphatidylserine catabolic process. Located in extracellular region. Orthologous to several human genes including PLA2G4C (phospholipase A2 group IVC) and PLA2G4F (phospholipase A2 group IVF). [provided by Alliance of Genome Resources, Nov 2024]
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    Genomic context

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    See PLB3 in Genome Data Viewer
    Location:
    chromosome: XV
    Exon count:
    1
    Sequence:
    Chromosome: XV; NC_001147.6 (305349..307409)

    Chromosome XV - NC_001147.6Genomic Context describing neighboring genes Neighboring gene E3 ubiquitin-protein ligase HRD1 Neighboring gene histone H2AZ Neighboring gene rRNA-processing endoribonuclease Neighboring gene ERMES complex subunit MDM12

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001147.6

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Lysophospholipids Facilitate COPII Vesicle Formation. Melero A, et al. Curr Biol, 2018 Jun 18. PMID 29887313, Free PMC Article
    2. Regulation of activity in vitro and in vivo of three phospholipases B from Saccharomyces cerevisiae. Merkel O, et al. Biochem J, 2005 Apr 15. PMID 15588231, Free PMC Article
    3. Cloning of CnLYSO1, a novel extracellular lysophospholipase of the pathogenic fungus Cryptococcus neoformans. Coe JG, et al. Gene, 2003 Oct 16. PMID 14563553
    4. Characterization and function in vivo of two novel phospholipases B/lysophospholipases from Saccharomyces cerevisiae. Merkel O, et al. J Biol Chem, 1999 Oct 1. PMID 10497163
    5. Development and validation of a hydrophilic interaction liquid chromatography-tandem mass spectrometry method for the quantification of lipid-related extracellular metabolites in Saccharomyces cerevisiae. Sun T, et al. J Chromatogr B Analyt Technol Biomed Life Sci, 2012 May 15. PMID 22541168

    See all (36) citations in PubMed

    GeneRIFs: Gene References Into Functions

    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 lysophospholipase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables lysophospholipase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables phospholipase A2 activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables phospholipase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in glycerophospholipid catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in lipid catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in phosphatidylinositol metabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in phosphatidylinositol metabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in phosphatidylserine catabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in phosphatidylserine catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in phospholipid catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    is_active_in endoplasmic reticulum IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    is_active_in extracellular region IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in extracellular region IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in fungal-type vacuole HDA PubMed 
    is_active_in plasma membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in side of membrane IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    lysophospholipase
    NP_014632.1
    • Phospholipase B (lysophospholipase) involved in lipid metabolism; hydrolyzes phosphatidylinositol and phosphatidylserine and displays transacylase activity in vitro; PLB3 has a paralog, PLB1, 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_001147.6 Reference assembly

      Range
      305349..307409
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001183265.1 → NP_014632.1  TPA: lysophospholipase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_014632.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W256, Q08108
      UniProtKB/TrEMBL
      A6ZNJ5, B3LJ45
      Conserved Domains (1) summary
      cd07203
      Location:35 → 595
      cPLA2_Fungal_PLB; Fungal Phospholipase B-like; cPLA2 GrpIVA homologs; catalytic domain
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q08108.1

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