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    VMA11 H(+)-transporting V0 sector ATPase subunit c' [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855842, updated on 9-Dec-2024

    Summary

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    Official Symbol
    VMA11
    Official Full Name
    H(+)-transporting V0 sector ATPase subunit c'
    Primary source
    SGD:S000006155
    Locus tag
    YPL234C
    See related
    AllianceGenome:SGD:S000006155; FungiDB:YPL234C; VEuPathDB:YPL234C
    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
    CLS9; TFP3
    Summary
    Predicted to enable proton-transporting ATPase activity, rotational mechanism. Predicted to be involved in vacuolar acidification. Located in fungal-type vacuole and membrane. [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See VMA11 in Genome Data Viewer
    Location:
    chromosome: XVI
    Exon count:
    1
    Sequence:
    Chromosome: XVI; NC_001148.4 (104946..105440, complement)

    Chromosome XVI - NC_001148.4Genomic Context describing neighboring genes Neighboring gene putative serine/threonine protein kinase ENV7 Neighboring gene RuvB family ATP-dependent DNA helicase reptin Neighboring gene MIND complex subunit NSL1 Neighboring gene syntaxin

    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. VMA11, a novel gene that encodes a putative proteolipid, is indispensable for expression of yeast vacuolar membrane H(+)-ATPase activity. Umemoto N, et al. J Biol Chem, 1991 Dec 25. PMID 1837023
    2. Genome-Wide Identification of Genes Involved in General Acid Stress and Fluoride Toxicity in Saccharomyces cerevisiae. Johnston NR, et al. Front Microbiol, 2020. PMID 32670247, Free PMC Article
    3. Expression of a proteolipid gene from a high-copy-number plasmid confers trifluoperazine resistance to Saccharomyces cerevisiae. Shih CK, et al. Mol Cell Biol, 1990 Jul. PMID 2192255, Free PMC Article
    4. Interacting helical surfaces of the transmembrane segments of subunits a and c' of the yeast V-ATPase defined by disulfide-mediated cross-linking. Kawasaki-Nishi S, et al. J Biol Chem, 2003 Oct 24. PMID 12917411
    5. Genome-wide analysis reveals the vacuolar pH-stat of Saccharomyces cerevisiae. Brett CL, et al. PLoS One, 2011 Mar 14. PMID 21423800, Free PMC Article

    See all (86) 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 proton-transporting ATPase activity, rotational mechanism IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables proton-transporting ATPase activity, rotational mechanism TAS
    Traceable Author Statement
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in proton transmembrane transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in vacuolar acidification TAS
    Traceable Author Statement
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cell periphery HDA PubMed 
    located_in fungal-type vacuole IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in fungal-type vacuole membrane HDA PubMed 
    is_active_in membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of proton-transporting V-type ATPase, V0 domain IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in vacuolar membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of vacuolar proton-transporting V-type ATPase, V0 domain TAS
    Traceable Author Statement
    more info
    		 PubMed 
    located_in vacuole IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    H(+)-transporting V0 sector ATPase subunit c'
    NP_015090.1
    • Vacuolar ATPase V0 domain subunit c'; involved in proton transport activity; hydrophobic integral membrane protein (proteolipid) containing four transmembrane segments; N and C termini are in the vacuolar lumen

    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
      104946..105440 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001184048.1 → NP_015090.1  TPA: H(+)-transporting V0 sector ATPase subunit c' [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_015090.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W3D6, P32365, P32842
      UniProtKB/TrEMBL
      A6ZW21, B3LKJ7, B5VSU8, C7GU73, C8ZIE5, G2WNV1, N1NW63
      Conserved Domains (2) summary
      cd18176
      Location:92 → 159
      ATP-synt_Vo_c_ATP6C_rpt2; V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar proteins
      cl00466
      Location:17 → 124
      ATP-synt_C; ATP synthase subunit C
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P32842.1

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