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

Summary

Go to the top of the page Help

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. Predicted to act upstream of or within proton transmembrane transport. 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, Apr 2025]
Orthologs: all
: Try the new Gene page
Try the new Transcripts and proteins table

Genomic context

Go to the top of the page Help

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

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:: NC_001143.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

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.

Submit: New GeneRIF Correction

Pathways from PubChem

Go to the top of the page

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Homology

NCBI Orthologs

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables proton transmembrane transporter activity	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	IC Inferred by Curator more info	PubMed
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 Golgi lumen acidification	NAS Non-traceable Author Statement more info	PubMed
involved_in endosomal lumen acidification	NAS Non-traceable Author Statement more info	PubMed
involved_in proton transmembrane transport	IC Inferred by Curator more info	PubMed
involved_in proton transmembrane transport	IDA Inferred from Direct Assay more info	PubMed
involved_in proton transmembrane transport	IEA Inferred from Electronic Annotation more info
involved_in vacuolar acidification	IC Inferred by Curator more info	PubMed
involved_in vacuolar acidification	NAS Non-traceable Author Statement more info	PubMed
involved_in vacuolar acidification	TAS Traceable Author Statement more info	PubMed

Component	Evidence Code	Pubs
located_in Golgi membrane	NAS Non-traceable Author Statement more info	PubMed
located_in fungal-type vacuole membrane	HDA more info	PubMed
located_in fungal-type vacuole membrane	NAS Non-traceable Author Statement more info	PubMed
part_of proton-transporting V-type ATPase complex	IPI Inferred from Physical Interaction more info	PubMed
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 complex	IPI Inferred from Physical Interaction more info	PubMed
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	IDA Inferred from Direct Assay more info	PubMed
part_of vacuolar proton-transporting V-type ATPase, V1 domain	TAS Traceable Author Statement more info	PubMed

General protein information

Go to the top of the page Help

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)

Go to the top of the page Help

NEW Try the new Transcript table

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

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001179646.1 → NP_012843.1 H(+)-transporting V1 sector ATPase subunit C

See identical proteins and their annotated locations for NP_012843.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VXK7, P31412

UniProtKB/TrEMBL

B3LR11

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]