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Protein

V-type proton ATPase subunit E

Gene

VMA4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

GO - Molecular functioni

  • proton-transporting ATPase activity, rotational mechanism Source: SGD

GO - Biological processi

  • ATP hydrolysis coupled proton transport Source: InterPro
  • vacuolar acidification Source: SGD
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-33808-MONOMER.
ReactomeiR-SCE-1222556. ROS, RNS production in response to bacteria.
R-SCE-77387. Insulin receptor recycling.
R-SCE-917977. Transferrin endocytosis and recycling.

Protein family/group databases

TCDBi3.A.2.2.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase subunit E
Short name:
V-ATPase subunit E
Alternative name(s):
V-ATPase 27 kDa subunit
Vacuolar proton pump subunit E
Gene namesi
Name:VMA4
Synonyms:VAT5
Ordered Locus Names:YOR332W
ORF Names:O6241
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR332W.
SGDiS000005859. VMA4.

Subcellular locationi

GO - Cellular componenti

  • fungal-type vacuole membrane Source: SGD
  • vacuolar proton-transporting V-type ATPase, V1 domain Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2S → A: Reduces ATPase activity by 11%. 1 Publication1
Mutagenesisi6T → A: Reduces ATPase activity by 73%. 1 Publication1
Mutagenesisi9T → A: Increases ATPase activity 1.4-fold. 1 Publication1
Mutagenesisi78S → A: Reduces ATPase activity by 88%. Prevents assembly of V1 subunits at the membrane. 1 Publication1
Mutagenesisi145D → G in VMA4-1; is rapidly degraded at 37 degrees Celsius. 1 Publication1
Mutagenesisi160Y → A: Reduces ATPase activity by 22%. 1 Publication1
Mutagenesisi202T → A: Increases ATPase activity 2.1-fold by increasing Vmax for ATP hydrolysis 2-fold. Reduces ATPase activity by 90% and produces structurally aberrant V-ATPase complexes; when associated with A-233. 1 Publication1
Mutagenesisi230K → A: Increases ATPase activity 1.3-fold. 1 Publication1
Mutagenesisi233D → A: Reduces ATPase activity by 74%. Reduces ATPase activity by 90% and produces structurally aberrant V-ATPase complexes; when associated with A-202. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001173102 – 233V-type proton ATPase subunit EAdd BLAST232

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP22203.
PRIDEiP22203.
TopDownProteomicsiP22203.

2D gel databases

SWISS-2DPAGEP22203.

PTM databases

iPTMnetiP22203.

Interactioni

Subunit structurei

V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d and e). VMA4 forms a homodimer within this complex and interacts directly with VMA5 and VMA10. Interacts with RAV1 and RAV2 components of the RAVE complex, which are essential for the stability and assembly of V-ATPase.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RAV1P471043EBI-20268,EBI-25471

Protein-protein interaction databases

BioGridi34716. 63 interactors.
DIPiDIP-4595N.
IntActiP22203. 18 interactors.
MINTiMINT-564623.

Structurei

Secondary structure

1233
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 111Combined sources102
Helixi114 – 132Combined sources19
Beta strandi135 – 141Combined sources7
Turni143 – 145Combined sources3
Helixi146 – 149Combined sources4
Helixi153 – 163Combined sources11
Turni164 – 166Combined sources3
Beta strandi171 – 174Combined sources4
Turni181 – 183Combined sources3
Beta strandi185 – 191Combined sources7
Beta strandi198 – 202Combined sources5
Helixi203 – 222Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KZ9NMR-A1-69[»]
3J9Telectron microscopy6.90G/I/K1-233[»]
3J9Uelectron microscopy7.60G/I/K1-233[»]
3J9Velectron microscopy8.30G/I/K1-233[»]
4DL0X-ray2.90E/J1-233[»]
4EFAX-ray2.82E1-233[»]
5BW9X-ray7.00I/K/M/i/k/m1-233[»]
5D80X-ray6.20I/K/M/i/k/m1-233[»]
ProteinModelPortaliP22203.
SMRiP22203.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni8 – 20Interaction with VMA51 PublicationAdd BLAST13
Regioni19 – 38Interaction with VMA101 PublicationAdd BLAST20

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili15 – 45Sequence analysisAdd BLAST31

Sequence similaritiesi

Belongs to the V-ATPase E subunit family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00390000002730.
HOGENOMiHOG000202506.
InParanoidiP22203.
KOiK02150.
OMAiKKLYSQQ.
OrthoDBiEOG092C54E5.

Family and domain databases

HAMAPiMF_00311. ATP_synth_E_arch. 1 hit.
InterProiIPR002842. ATPase_V1/A1-cplx_esu.
[Graphical view]
PfamiPF01991. vATP-synt_E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22203-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSAITALTP NQVNDELNKM QAFIRKEAEE KAKEIQLKAD QEYEIEKTNI
60 70 80 90 100
VRNETNNIDG NFKSKLKKAM LSQQITKSTI ANKMRLKVLS AREQSLDGIF
110 120 130 140 150
EETKEKLSGI ANNRDEYKPI LQSLIVEALL KLLEPKAIVK ALERDVDLIE
160 170 180 190 200
SMKDDIMREY GEKAQRAPLE EIVISNDYLN KDLVSGGVVV SNASDKIEIN
210 220 230
NTLEERLKLL SEEALPAIRL ELYGPSKTRK FFD
Length:233
Mass (Da):26,471
Last modified:January 23, 2007 - v4
Checksum:i7AC5169FF7E5A39C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti97 – 98DG → ER in AAA35209 (PubMed:2145285).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60663 Genomic DNA. Translation: AAA35209.1.
Z49821 Genomic DNA. Translation: CAA89978.1.
Z75239 Genomic DNA. Translation: CAA99654.1.
BK006948 Genomic DNA. Translation: DAA11094.1.
PIRiS62063.
RefSeqiNP_014977.3. NM_001183752.3.

Genome annotation databases

EnsemblFungiiYOR332W; YOR332W; YOR332W.
GeneIDi854509.
KEGGisce:YOR332W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60663 Genomic DNA. Translation: AAA35209.1.
Z49821 Genomic DNA. Translation: CAA89978.1.
Z75239 Genomic DNA. Translation: CAA99654.1.
BK006948 Genomic DNA. Translation: DAA11094.1.
PIRiS62063.
RefSeqiNP_014977.3. NM_001183752.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KZ9NMR-A1-69[»]
3J9Telectron microscopy6.90G/I/K1-233[»]
3J9Uelectron microscopy7.60G/I/K1-233[»]
3J9Velectron microscopy8.30G/I/K1-233[»]
4DL0X-ray2.90E/J1-233[»]
4EFAX-ray2.82E1-233[»]
5BW9X-ray7.00I/K/M/i/k/m1-233[»]
5D80X-ray6.20I/K/M/i/k/m1-233[»]
ProteinModelPortaliP22203.
SMRiP22203.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34716. 63 interactors.
DIPiDIP-4595N.
IntActiP22203. 18 interactors.
MINTiMINT-564623.

Protein family/group databases

TCDBi3.A.2.2.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

iPTMnetiP22203.

2D gel databases

SWISS-2DPAGEP22203.

Proteomic databases

MaxQBiP22203.
PRIDEiP22203.
TopDownProteomicsiP22203.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR332W; YOR332W; YOR332W.
GeneIDi854509.
KEGGisce:YOR332W.

Organism-specific databases

EuPathDBiFungiDB:YOR332W.
SGDiS000005859. VMA4.

Phylogenomic databases

GeneTreeiENSGT00390000002730.
HOGENOMiHOG000202506.
InParanoidiP22203.
KOiK02150.
OMAiKKLYSQQ.
OrthoDBiEOG092C54E5.

Enzyme and pathway databases

BioCyciYEAST:G3O-33808-MONOMER.
ReactomeiR-SCE-1222556. ROS, RNS production in response to bacteria.
R-SCE-77387. Insulin receptor recycling.
R-SCE-917977. Transferrin endocytosis and recycling.

Miscellaneous databases

PROiP22203.

Family and domain databases

HAMAPiMF_00311. ATP_synth_E_arch. 1 hit.
InterProiIPR002842. ATPase_V1/A1-cplx_esu.
[Graphical view]
PfamiPF01991. vATP-synt_E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVATE_YEAST
AccessioniPrimary (citable) accession number: P22203
Secondary accession number(s): D6W328
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 164 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 16134 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.