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    TGL5 triacylglycerol lipase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 854248, updated on 18-Sep-2024

    Summary

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    Official Symbol
    TGL5
    Official Full Name
    triacylglycerol lipase
    Primary source
    SGD:S000005607
    Locus tag
    YOR081C
    See related
    AllianceGenome:SGD:S000005607; FungiDB:YOR081C; VEuPathDB:YOR081C
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Also known as
    STC2
    Summary
    Enables lysophosphatidic acid acyltransferase activity and triglyceride lipase activity. Involved in triglyceride mobilization. Located in lipid droplet. [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    See TGL5 in Genome Data Viewer
    Location:
    chromosome: XV
    Exon count:
    1
    Sequence:
    Chromosome: XV; NC_001147.6 (476939..479188, complement)

    Chromosome XV - NC_001147.6Genomic Context describing neighboring genes Neighboring gene Mn(2+) transporter ATX2 Neighboring gene DNA-binding SCF ubiquitin ligase subunit DIA2 Neighboring gene transcriptional repressor WHI5 Neighboring gene triglyceride lipase

    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. Janus-faced enzymes yeast Tgl3p and Tgl5p catalyze lipase and acyltransferase reactions. Rajakumari S, et al. Mol Biol Cell, 2010 Feb 15. PMID 20016004, Free PMC Article
    2. Tgl4p and Tgl5p, two triacylglycerol lipases of the yeast Saccharomyces cerevisiae are localized to lipid particles. Athenstaedt K, et al. J Biol Chem, 2005 Nov 11. PMID 16135509
    3. SUGAR-DEPENDENT1 encodes a patatin domain triacylglycerol lipase that initiates storage oil breakdown in germinating Arabidopsis seeds. Eastmond PJ. Plant Cell, 2006 Mar. PMID 16473965, Free PMC Article
    4. Triacylglycerol lipolysis is linked to sphingolipid and phospholipid metabolism of the yeast Saccharomyces cerevisiae. Rajakumari S, et al. Biochim Biophys Acta, 2010 Dec. PMID 20727985
    5. Obese yeast: triglyceride lipolysis is functionally conserved from mammals to yeast. Kurat CF, et al. J Biol Chem, 2006 Jan 6. PMID 16267052

    See all (39) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Results demonstrate that yeast Tgl3p and Tgl5p play a dual role in lipid metabolism contributing to both anabolic and catabolic processes.
      Title: Janus-faced enzymes yeast Tgl3p and Tgl5p catalyze lipase and acyltransferase reactions.
    2. The identification of Tgl4p and Tgl5p as additional TAG lipases of the yeast is reported.
      Title: Tgl4p and Tgl5p, two triacylglycerol lipases of the yeast Saccharomyces cerevisiae are localized to lipid particles.
    Submit: New GeneRIF Correction

    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 hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables lysophosphatidic acid acyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables triacylglycerol lipase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables triacylglycerol lipase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables triacylglycerol lipase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in lipid catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in lipid metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in sporulation resulting in formation of a cellular spore IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in triglyceride metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in triglyceride mobilization IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in triglyceride mobilization IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in lipid droplet HDA PubMed 
    located_in lipid droplet IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in lipid droplet IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    triacylglycerol lipase
    NP_014724.1
    • Bifunctional triacylglycerol lipase and LPA acyltransferase; lipid particle-localized triacylglycerol (TAG) lipase involved in triacylglycerol mobilization; catalyzes acylation of lysophosphatidic acid (LPA); potential Cdc28p substrate; TGL5 has a paralog, TGL4, 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
      476939..479188 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001183500.1 → NP_014724.1  TPA: triacylglycerol lipase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_014724.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W2E4, Q12043, Q7LH13
      UniProtKB/TrEMBL
      A6ZNT3, B3LJD0, C7GT34, C8ZI43, G2WMV9, N1NWI8
      Conserved Domains (2) summary
      cd07230
      Location:110 → 537
      Pat_TGL4-5_like; Triacylglycerol lipase 4 and 5
      pfam11815
      Location:40 → 176
      DUF3336; Domain of unknown function (DUF3336)
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q12043.1

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