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VMA8 H(+)-transporting V1 sector ATPase subunit D [ Saccharomyces cerevisiae S288C ]

Gene ID: 856659, updated on 13-Apr-2024

Summary

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Gene symbol
VMA8
Gene description
H(+)-transporting V1 sector ATPase subunit D
Primary source
SGD:S000000777
Locus tag
YEL051W
See related
AllianceGenome:SGD:S000000777
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 acidification. Located in fungal-type vacuole membrane and membrane raft. Part of vacuolar proton-transporting V-type ATPase complex. Orthologous to human ATP6V1D (ATPase H+ transporting V1 subunit D). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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Location:
chromosome: V
Exon count:
1
Sequence:
Chromosome: V; NC_001137.3 (58378..59148)

Chromosome V - NC_001137.3Genomic Context describing neighboring genes Neighboring gene Mak10p Neighboring gene Afg1p Neighboring gene mitochondrial 54S ribosomal protein RML2 Neighboring gene ncRNA

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_001137.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Vma8p-GFP fusions can be functionally incorporated into V-ATPase, suggesting structural flexibility at the top of V1. Nowakowski S, et al. Int J Mol Sci, 2011. PMID 21845105, Free PMC Article
  2. Subunit D (Vma8p) of the yeast vacuolar H+-ATPase plays a role in coupling of proton transport and ATP hydrolysis. Xu T, et al. J Biol Chem, 2000 Jul 21. PMID 10801866
  3. VMA8 encodes a 32-kDa V1 subunit of the Saccharomyces cerevisiae vacuolar H(+)-ATPase required for function and assembly of the enzyme complex. Graham LA, et al. J Biol Chem, 1995 Jun 23. PMID 7797485
  4. Crystal structure of subunits D and F in complex gives insight into energy transmission of the eukaryotic V-ATPase from Saccharomyces cerevisiae. Balakrishna AM, et al. J Biol Chem, 2015 Feb 6. PMID 25505269, Free PMC Article
  5. 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

See all (106) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. The low resolution structure was determined from solution X-ray scattering data. The protein is a boxing glove-shaped molecule consisting of two distinct domains, with a width of about 6.5 nm and 3.5 nm, respectively.
    Title: 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.
  2. Subunit d of VMA8 couples adenosine triphosphate (ATP) hydrolysis and proton transport.
    Title: Identification of a domain in the V0 subunit d that is critical for coupling of the yeast vacuolar proton-translocating ATPase.
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 proton-transporting ATPase activity, rotational mechanism IEA
Inferred from Electronic Annotation
more info
  
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 acidification 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
  
located_in membrane raft IDA
Inferred from Direct Assay
more info
 PubMed 
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 complex IDA
Inferred from Direct Assay
more info
 PubMed 
located_in vacuole IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
H(+)-transporting V1 sector ATPase subunit D
NP_010863.1
  • Subunit D of the V1 peripheral membrane domain of V-ATPase; part of the electrogenic proton pump found throughout the endomembrane system; plays a role in the coupling of proton transport and ATP hydrolysis; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight 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_001137.3 Reference assembly

    Range
    58378..59148
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001178866.1 → NP_010863.1  TPA: H(+)-transporting V1 sector ATPase subunit D [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_010863.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D3DLJ9, P32610
    UniProtKB/TrEMBL
    A0A6A5Q1W2, A6ZQQ0, B3LRW6, B5VH86, C7GXD8, C8Z6U2, G2WCI3, N1PA65
    Conserved Domains (1) summary
    TIGR00309
    Location:5 → 213
    V_ATPase_subD; H(+)-transporting ATP synthase, vacuolar type, subunit D
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
4RND_A.1
4RND_C.1
5BW9_G.1
5BW9_g.1
5D80_G.1
5D80_g.1
5VOX_M.1
5VOY_M.1
5VOZ_M.1
6O7V_M.1
6O7W_M.1
6O7X_M.1
P32610.1

Gene LinkOut

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