VMA4 H(+)-transporting V1 sector ATPase subunit E [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: VMA4
Official Full Name: H(+)-transporting V1 sector ATPase subunit E
Primary source: SGD:S000005859
Locus tag: YOR332W
See related: AllianceGenome:SGD:S000005859; FungiDB:YOR332W; VEuPathDB:YOR332W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Predicted to enable proton-transporting ATPase activity, rotational mechanism. Predicted to be involved in vacuolar acidification. Located in fungal-type vacuole membrane and membrane raft. Part of vacuolar proton-transporting V-type ATPase, V1 domain. Human ortholog(s) of this gene implicated in autosomal recessive cutis laxa type IIC. Orthologous to several human genes including ATP6V1E2 (ATPase H+ transporting V1 subunit E2). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See VMA4 in Genome Data Viewer

Location:: chromosome: XV

Exon count:: 1

Sequence:: Chromosome: XV; NC_001147.6 (943656..944357)

Chromosome XV - NC_001147.6 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001147.6

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Glu-44 is one of the key functional residues for subunit interaction in the V-ATPase complex.
Title: Glu-44 in the amino-terminal α-helix of yeast vacuolar ATPase E subunit (Vma4p) has a role for VoV1 assembly.
Data indicate the interactions in V-ATPase Vma4 (subunit E) and Vma10 (subunit G).
Title: Probing subunit-subunit interactions in the yeast vacuolar ATPase by peptide arrays.
new structural details of subunit E are discussed in the light of the structural arrangements of this subunit inside the V- and VV ATPase.
Title: Structural elements of the C-terminal domain of subunit E (E₁₃₃₋₂₂₂) from the Saccharomyces cerevisiae V₁V₀ ATPase determined by solution NMR spectroscopy.
NMR solution structure of subunit E (fragment E(1-69)) of the Saccharomyces cerevisiae V (1)V (O) ATPase.
Title: NMR solution structure of subunit E (fragment E(1-69)) of the Saccharomyces cerevisiae V (1)V (O) ATPase.
These results suggest that subunit E, especially its amino-terminal domain, plays a pertinent role in the assembly of V-ATPase subunits in vacuolar membranes from mice and yeast.
Title: Defective assembly of a hybrid vacuolar H(+)-ATPase containing the mouse testis-specific E1 isoform and yeast subunits.
an increase in the level of the TIM23 translocase associated with the cytochrome bc1-COX supercomplex is observed in the absence of Su e and Su g
Title: The F1F0-ATP synthase complex influences the assembly state of the cytochrome bc1-cytochrome oxidase supercomplex and its association with the TIM23 machinery.
Mutational analysis of V-ATPase indicates that subunit E could communicate cellular changes to the catalytic sites upon binding to regulatory proteins which interact with subunit E as a means of regulating V-ATPase function.
Title: Mutational analysis of the stator subunit E of the yeast V-ATPase.
Protein interaction studies show that the N-terminal region of Vma4 (subunit E) is a key factor not only in the stator structure of the vacuolar ATPase rotary molecular motor, but also in mediating interactions with putative regulatory subunits.
Title: Defined sites of interaction between subunits E (Vma4p), C (Vma5p), and G (Vma10p) within the stator structure of the vacuolar H+-ATPase.

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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 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 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
part_of proton-transporting two-sector ATPase complex, catalytic 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	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 E

NP_014977.3

Subunit E of the V1 domain of the vacuolar H+-ATPase (V-ATPase); V-ATPase is an electrogenic proton pump found throughout the endomembrane system; V1 domain has eight subunits; required for the V1 domain to assemble onto the vacuolar membrane; protein abundance increases in response to DNA replication stress

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_001147.6 Reference assembly

Range

943656..944357

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001183752.3 → NP_014977.3 TPA: H(+)-transporting V1 sector ATPase subunit E [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_014977.3

Status: REVIEWED

UniProtKB/Swiss-Prot

D6W328, P22203

UniProtKB/TrEMBL

A6ZPG3, B3LJZ2, C7GNT3, C8ZH84, G2WNJ5, N1NYZ0

Conserved Domains (1) summary

pfam01991
Location:23 → 223

vATP-synt_E; ATP synthase (E/31 kDa) subunit