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VMA6 H(+)-transporting V0 sector ATPase subunit d [ Saccharomyces cerevisiae S288C ]

Gene ID: 851168, updated on 19-Jun-2024

Summary

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Gene symbol
VMA6
Gene description
H(+)-transporting V0 sector ATPase subunit d
Primary source
FungiDB:YLR447C
Locus tag
YLR447C
See related
SGD:S000004439; AllianceGenome:SGD:S000004439; VEuPathDB:YLR447C
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary
Contributes to proton-transporting ATPase activity, rotational mechanism. Involved in vacuolar transport. Located in fungal-type vacuole membrane. Orthologous to several human genes including ATP6V0D1 (ATPase H+ transporting V0 subunit d1). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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See VMA6 in Genome Data Viewer
Location:
chromosome: XII
Exon count:
1
Sequence:
Chromosome: XII; NC_001144.5 (1026856..1027893, complement)

Chromosome XII - NC_001144.5Genomic Context describing neighboring genes Neighboring gene Gmc2p Neighboring gene hexokinase Neighboring gene ribosomal 60S subunit protein L6B Neighboring gene peptidylprolyl isomerase FPR4

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_001144.5

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Assembly of subunit d (Vma6p) and G (Vma10p) and the NMR solution structure of subunit G (G(1-59)) of the Saccharomyces cerevisiae V(1)V(O) ATPase. Rishikesan S, et al. Biochim Biophys Acta, 2009 Apr. PMID 19344662
  2. The boxing glove shape of subunit d of the yeast V-ATPase in solution and the importance of disulfide formation for folding of this protein. Thaker YR, et al. J Bioenerg Biomembr, 2007 Aug. PMID 17896169
  3. Identification of a domain in the V0 subunit d that is critical for coupling of the yeast vacuolar proton-translocating ATPase. Owegi MA, et al. J Biol Chem, 2006 Oct 6. PMID 16891312
  4. Association of the eukaryotic V1VO ATPase subunits a with d and d with A. Thaker YR, et al. FEBS Lett, 2009 Apr 2. PMID 19289121
  5. VMA13 encodes a 54-kDa vacuolar H(+)-ATPase subunit required for activity but not assembly of the enzyme complex in Saccharomyces cerevisiae. Ho MN, et al. J Biol Chem, 1993 Aug 25. PMID 8349704

See all (107) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Solution NMR of the recombinant N- (G(1-59)) and C-terminal segment (G(61-114)) of subunit G, has been performed in the absence and presence of subunit d of the yeast V-ATPase.
    Title: Assembly of subunit d (Vma6p) and G (Vma10p) and the NMR solution structure of subunit G (G(1-59)) of the Saccharomyces cerevisiae V(1)V(O) ATPase.
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
contributes_to proton-transporting ATPase activity, rotational mechanism IDA
Inferred from Direct Assay
more info
 PubMed 
enables proton-transporting ATPase activity, rotational mechanism IEA
Inferred from Electronic Annotation
more info
  
contributes_to proton-transporting ATPase activity, rotational mechanism IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Process Evidence Code Pubs
involved_in proton transmembrane transport IEA
Inferred from Electronic Annotation
more info
  
involved_in vacuolar acidification IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in vacuolar transport IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in vacuolar transport IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in vacuolar transport IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
located_in fungal-type vacuole membrane HDA PubMed 
is_active_in fungal-type vacuole membrane IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in fungal-type vacuole 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 complex IBA
Inferred from Biological aspect of Ancestor
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 d
NP_013552.3
  • Subunit d of the V0 integral membrane domain of V-ATPase; part of the electrogenic proton pump found in the endomembrane system; required for V1 domain assembly on the vacuolar membrane; the V0 integral membrane domain of vacuolar H+-ATPase (V-ATPase) has five subunits

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_001144.5 Reference assembly

    Range
    1026856..1027893 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001182335.3 → NP_013552.3  TPA: H(+)-transporting V0 sector ATPase subunit d [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_013552.3

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VZ81, P32366
    UniProtKB/TrEMBL
    A0A6A5PX09, A7A1W6, B3RHV5, B5VNY4, C7GSK9, C8ZE54, G2WJQ8, N1NZY4
    Conserved Domains (1) summary
    COG1527
    Location:1 → 345
    NtpC; Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 [Energy production and conversion]
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
5VOX_Q.1
5VOY_Q.1
5VOZ_Q.1
6C6L_B.1
6M0R_B.1
6M0S_B.1
6O7V_d.1
6O7W_d.1
6O7X_d.1
6PE4_D.1
6PE5_D.1
P32366.2

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