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    VID28 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 854795, updated on 11-Sep-2024

    Summary

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    Official Symbol
    VID28
    Primary source
    SGD:S000001279
    Locus tag
    YIL017C
    See related
    AllianceGenome:SGD:S000001279; FungiDB:YIL017C; VEuPathDB:YIL017C
    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
    GID5; YIL017W
    Summary
    Involved in negative regulation of gluconeogenesis; proteasome-mediated ubiquitin-dependent protein catabolic process; and protein catabolic process in the vacuole. Located in cytoplasm and nucleus. Part of GID complex. Orthologous to human ARMC8 (armadillo repeat containing 8). [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    Location:
    chromosome: IX
    Exon count:
    1
    Sequence:
    Chromosome: IX; NC_001141.2 (318200..320965, complement)

    Chromosome IX - NC_001141.2Genomic Context describing neighboring genes Neighboring gene Faf1p Neighboring gene ribosomal 60S subunit protein L2B Neighboring gene Snl1p Neighboring gene aspartyl protease BAR1

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001141.2

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Vid28 protein is required for the association of vacuole import and degradation (Vid) vesicles with actin patches and the retention of Vid vesicle proteins in the intracellular fraction. Giardina BJ, et al. J Biol Chem, 2013 Apr 26. PMID 23393132, Free PMC Article
    2. Intracellular vesicle clusters are organelles that synthesize extracellular vesicle-associated cargo proteins in yeast. Winters CM, et al. J Biol Chem, 2020 Feb 28. PMID 31974164, Free PMC Article
    3. Regulation of the Gid ubiquitin ligase recognition subunit Gid4. Menssen R, et al. FEBS Lett, 2018 Oct. PMID 30136317
    4. Exploring the topology of the Gid complex, the E3 ubiquitin ligase involved in catabolite-induced degradation of gluconeogenic enzymes. Menssen R, et al. J Biol Chem, 2012 Jul 20. PMID 22645139, Free PMC Article
    5. Cryo-EM structures of Gid12-bound GID E3 reveal steric blockade as a mechanism inhibiting substrate ubiquitylation. Qiao S, et al. Nat Commun, 2022 Jun 1. PMID 35650207, Free PMC Article

    See all (49) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Vid28 protein is required for the association of vacuole import and degradation (Vid) vesicles with actin patches and the retention of Vid vesicle proteins in the intracellular fraction.
      Title: Vid28 protein is required for the association of vacuole import and degradation (Vid) vesicles with actin patches and the retention of Vid vesicle proteins in the intracellular fraction.
    2. Three members of the VID and GID gene families, VID30/GID1, GID2, and VID28/GID5 are needed for the rapamycin or nitrogen starvation-induced degradation of the high-affinity hexose transporter Hxt7p is shown here.
      Title: Components of the Vid30c are needed for the rapamycin-induced degradation of the high-affinity hexose transporter Hxt7p in Saccharomyces cerevisiae.
    Submit: New GeneRIF Correction

    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 molecular_function ND
    No biological Data available
    more info
    		  
    Process Evidence Code Pubs
    involved_in ascospore formation HMP PubMed 
    involved_in negative regulation of gluconeogenesis IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in proteasome-mediated ubiquitin-dependent protein catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in proteasome-mediated ubiquitin-dependent protein catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein catabolic process in the vacuole IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    part_of GID complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of GID complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasm HDA PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in nucleus HDA PubMed 
    located_in nucleus IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in vacuole IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    glucose-induced degradation complex subunit VID28
    NP_012247.3
    • GID Complex subunit, serves as adaptor for regulatory subunit Vid24p; protein involved in proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBPase); localized to the nucleus and the cytoplasm

    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_001141.2 Reference assembly

      Range
      318200..320965 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001179367.3 → NP_012247.3  TPA: glucose-induced degradation complex subunit VID28 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_012247.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VVR2, P40547
      UniProtKB/TrEMBL
      B3LTM5
      Conserved Domains (2) summary
      COG5369
      Location:1 → 918
      COG5369; Uncharacterized conserved protein [Function unknown]
      sd00044
      Location:586 → 610
      HEAT; HEAT repeat [structural motif]
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P40547.1

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