VMA5 H(+)-transporting V1 sector ATPase subunit C [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: VMA5
Official Full Name: H(+)-transporting V1 sector ATPase subunit C
Primary source: SGD:S000001563
Locus tag: YKL080W
See related: AllianceGenome:SGD:S000001563; FungiDB:YKL080W; VEuPathDB:YKL080W
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: CSL5; VAT3
Summary: Predicted to enable proton-transporting ATPase activity, rotational mechanism. Predicted to be involved in vacuolar acidification. Located in fungal-type vacuole membrane. Orthologous to human ATP6V1C1 (ATPase H+ transporting V1 subunit C1) and ATP6V1C2 (ATPase H+ transporting V1 subunit C2). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See VMA5 in Genome Data Viewer

Location:: chromosome: XI

Exon count:: 1

Sequence:: Chromosome: XI; NC_001143.9 (285030..286208)

Chromosome XI - NC_001143.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001143.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

We speculate that the spatial closeness of the a(NT), C(foot), and EG binding sites in the intact V-ATPase results in a high-avidity interaction that is able to resist the torque of rotational catalysis.
Title: Subunit interactions at the V1-Vo interface in yeast vacuolar ATPase.
Domain characterization and interaction of the yeast vacuolar ATPase subunit C with the peripheral stator stalk subunits E and G
Title: Domain characterization and interaction of the yeast vacuolar ATPase subunit C with the peripheral stator stalk subunits E and G.
Nucleotide occupancy by subunit C, followed by conformational changes of this subunit has shed light on the mechanism of V-ATPase regulation.
Title: Structural features and nucleotide-binding capability of the C subunit are integral to the regulation of the eukaryotic V1Vo ATPases.
Vma5 (subunit C) expressed as a glutathione-S-transferase fusion protein in Escherichia coli is able to interact strongly with Vma4 (subunit E) expressed in a cell-free system.
Title: Defined sites of interaction between subunits E (Vma4p), C (Vma5p), and G (Vma10p) within the stator structure of the vacuolar H+-ATPase.
The data show that subunit C is binding at the interface of the ATPase and proton channel, opposite from another stalk density previously identified as subunit H.
Title: Localization of subunit C (Vma5p) in the yeast vacuolar ATPase by immuno electron microscopy.
VMA5p subunit C localizes to the interface of the V1 and V0 domains, which is consistent with a role for this subunit in controlling assembly of the V-ATPase complex
Title: Cysteine-mediated cross-linking indicates that subunit C of the V-ATPase is in close proximity to subunits E and G of the V1 domain and subunit a of the V0 domain.
Expression, crystallization and phasing of vacuolar H(+)-ATPase subunit C (Vma5p) of Saccharomyces cerevisiae
Title: Expression, crystallization and phasing of vacuolar H(+)-ATPase subunit C (Vma5p) of Saccharomyces cerevisiae.

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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

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables proton-transporting ATPase activity, rotational mechanism	IBA Inferred from Biological aspect of Ancestor more info
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 fungal-type vacuole membrane	HDA more info	PubMed
located_in membrane	IEA Inferred from Electronic Annotation more info
part_of proton-transporting V-type ATPase, V1 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, V1 domain	IBA Inferred from Biological aspect of Ancestor more info
part_of vacuolar proton-transporting V-type ATPase, V1 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 V1 sector ATPase subunit C

NP_012843.1

Subunit C of the V1 peripheral membrane domain of V-ATPase; part of the electrogenic proton pump found throughout the endomembrane system; required for the V1 domain to assemble onto the vacuolar membrane; the V1 peripheral membrane domain of 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

NC_001143.9 Reference assembly

Range

285030..286208

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001179646.1 → NP_012843.1 TPA: H(+)-transporting V1 sector ATPase subunit C [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_012843.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VXK7, P31412

UniProtKB/TrEMBL

A6ZZN6, B3LR11, B5VM76, C7GVM8, C8ZC93, G2WHV2, N1P072

Conserved Domains (2) summary

COG5127
Location:6 → 392

COG5127; Vacuolar H+-ATPase V1 sector, subunit C [Energy production and conversion]

cd14785
Location:66 → 86

V-ATPase_C; 3-helical coiled coil [structural motif]