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    FAS2 trifunctional fatty acid synthase subunit FAS2 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855845, updated on 9-Dec-2024

    Summary

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    Official Symbol
    FAS2
    Official Full Name
    trifunctional fatty acid synthase subunit FAS2
    Primary source
    SGD:S000006152
    Locus tag
    YPL231W
    See related
    AllianceGenome:SGD:S000006152; FungiDB:YPL231W; VEuPathDB:YPL231W
    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 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; 3-oxoacyl-[acyl-carrier-protein] synthase activity; and holo-[acyl-carrier-protein] synthase activity. Contributes to fatty acid synthase activity. Involved in long-chain fatty acid biosynthetic process. Located in cytosol. Part of fatty acid synthase complex. [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See FAS2 in Genome Data Viewer
    Location:
    chromosome: XVI
    Exon count:
    1
    Sequence:
    Chromosome: XVI; NC_001148.4 (108652..114315)

    Chromosome XVI - NC_001148.4Genomic Context describing neighboring genes Neighboring gene MIND complex subunit NSL1 Neighboring gene syntaxin Neighboring gene Usv1p Neighboring gene uncharacterized protein

    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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    Related articles in PubMed

    1. Pantetheine-free mutants of the yeast fatty-acid-synthetase complex. Schweizer E, et al. Eur J Biochem, 1973 Nov 15. PMID 4590449
    2. Isolation of a spontaneous cerulenin-resistant sake yeast with both high ethyl caproate-producing ability and normal checkpoint integrity. Tamura H, et al. Biosci Biotechnol Biochem, 2015. PMID 25787154
    3. Interactions of the acyl chain with the Saccharomyces cerevisiae acyl carrier protein. Perez DR, et al. Biochemistry, 2015 Apr 7. PMID 25774789
    4. Engineering of Saccharomyces cerevisiae for the synthesis of short chain fatty acids. Leber C, et al. Biotechnol Bioeng, 2014 Feb. PMID 23928901
    5. The construction and application of diploid sake yeast with a homozygous mutation in the FAS2 gene. Kotaka A, et al. J Biosci Bioeng, 2010 Dec. PMID 20708434

    See all (168) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Genotypic analysis of the FAS2-F1279Y (3836T>A) polymorphism conferring high ethyl caprylate productivity in industrial sake yeast strains.
      Title: Genotypic analysis of the FAS2-F1279Y (3836T>A) polymorphism conferring high ethyl caprylate productivity in industrial sake yeast strains.
    2. Analysis of the co-translational assembly of the fungal fatty acid synthase (FAS).
      Title: Analysis of the co-translational assembly of the fungal fatty acid synthase (FAS).
    3. FAS2 molecular structure shows how acyl chain interacts with the hydrophobic cavity and gives it stability.
      Title: Interactions of the acyl chain with the Saccharomyces cerevisiae acyl carrier protein.
    4. The major ubiquitin ligase targeting the superfluous Fas2 subunit to the proteasome is Ubr1. The ubiquitin-conjugating enzymes Ubc2 and Ubc4 assist the degradation process.
      Title: Quality control of a cytoplasmic protein complex: chaperone motors and the ubiquitin-proteasome system govern the fate of orphan fatty acid synthase subunit Fas2 of yeast.
    5. Overexpression of FAS1, FAS2 and Acc1 leads to accumulation of sterols.
      Title: Overexpression of genes of the fatty acid biosynthetic pathway leads to accumulation of sterols in Saccharomyces cerevisiae.
    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 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables 3-oxoacyl-[acyl-carrier-protein] synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables 3-oxoacyl-[acyl-carrier-protein] synthase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables fatty acid synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    contributes_to fatty acid synthase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables fatty-acyl-CoA synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables holo-[acyl-carrier-protein] synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables holo-[acyl-carrier-protein] synthase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables magnesium ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidoreductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables transferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in fatty acid biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in long-chain fatty acid biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in long-chain fatty acid biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytosol HDA PubMed 
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of fatty acid synthase complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of fatty acid synthase complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in mitochondrion HDA PubMed 

    General protein information

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    Preferred Names
    trifunctional fatty acid synthase subunit FAS2
    NP_015093.1
    • Alpha subunit of fatty acid synthetase; complex catalyzes the synthesis of long-chain saturated fatty acids; contains the acyl-carrier protein domain and beta-ketoacyl reductase, beta-ketoacyl synthase and self-pantetheinylation activities

    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
      108652..114315
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001184045.1 → NP_015093.1  TPA: trifunctional fatty acid synthase subunit FAS2 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_015093.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W3D9, P19097, Q12533
      UniProtKB/TrEMBL
      A0A140KF01, G2WNV4, N1NWL3
      Conserved Domains (4) summary
      COG4982
      Location:93 → 1169
      FabG2; 3-oxoacyl-ACP reductase domain of yeast-type FAS1 [Lipid transport and metabolism]
      cd00828
      Location:1135 → 1655
      elong_cond_enzymes; "elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as ...
      TIGR00556
      Location:1765 → 1886
      pantethn_trn; phosphopantetheine--protein transferase domain
      cl08282
      Location:4 → 85
      Acyl_transf_1; Acyl transferase domain
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P19097.2

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