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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.
ReactomeiREACT_322706. Transferrin endocytosis and recycling.
REACT_347079. Insulin receptor 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
ProteomesiUP000002311 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21S → A: Reduces ATPase activity by 11%. 1 Publication
Mutagenesisi6 – 61T → A: Reduces ATPase activity by 73%. 1 Publication
Mutagenesisi9 – 91T → A: Increases ATPase activity 1.4-fold. 1 Publication
Mutagenesisi78 – 781S → A: Reduces ATPase activity by 88%. Prevents assembly of V1 subunits at the membrane. 1 Publication
Mutagenesisi145 – 1451D → G in VMA4-1; is rapidly degraded at 37 degrees Celsius. 1 Publication
Mutagenesisi160 – 1601Y → A: Reduces ATPase activity by 22%. 1 Publication
Mutagenesisi202 – 2021T → 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 Publication
Mutagenesisi230 – 2301K → A: Increases ATPase activity 1.3-fold. 1 Publication
Mutagenesisi233 – 2331D → A: Reduces ATPase activity by 74%. Reduces ATPase activity by 90% and produces structurally aberrant V-ATPase complexes; when associated with A-202. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 233232V-type proton ATPase subunit EPRO_0000117310Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP22203.
PaxDbiP22203.
PeptideAtlasiP22203.

2D gel databases

SWISS-2DPAGEP22203.

Expressioni

Gene expression databases

GenevestigatoriP22203.

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. 62 interactions.
DIPiDIP-4595N.
IntActiP22203. 18 interactions.
MINTiMINT-564623.
STRINGi4932.YOR332W.

Structurei

Secondary structure

1
233
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 111102Combined sources
Helixi114 – 13219Combined sources
Beta strandi135 – 1417Combined sources
Turni143 – 1453Combined sources
Helixi146 – 1494Combined sources
Helixi153 – 16311Combined sources
Turni164 – 1663Combined sources
Beta strandi171 – 1744Combined sources
Turni181 – 1833Combined sources
Beta strandi185 – 1917Combined sources
Beta strandi198 – 2025Combined sources
Helixi203 – 22220Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KZ9NMR-A1-69[»]
4DL0X-ray2.90E/J1-233[»]
4EFAX-ray2.82E1-233[»]
ProteinModelPortaliP22203.
SMRiP22203. Positions 2-226.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni8 – 2013Interaction with VMA5Add
BLAST
Regioni19 – 3820Interaction with VMA10Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili15 – 4531Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the V-ATPase E subunit family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG1390.
GeneTreeiENSGT00390000002730.
HOGENOMiHOG000202506.
InParanoidiP22203.
KOiK02150.
OMAiFLSADTC.
OrthoDBiEOG7380GZ.

Family and domain databases

HAMAPiMF_00311. ATP_synth_E_arch.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 982DG → ER in AAA35209 (PubMed:2145285).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2KZ9NMR-A1-69[»]
4DL0X-ray2.90E/J1-233[»]
4EFAX-ray2.82E1-233[»]
ProteinModelPortaliP22203.
SMRiP22203. Positions 2-226.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34716. 62 interactions.
DIPiDIP-4595N.
IntActiP22203. 18 interactions.
MINTiMINT-564623.
STRINGi4932.YOR332W.

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.

2D gel databases

SWISS-2DPAGEP22203.

Proteomic databases

MaxQBiP22203.
PaxDbiP22203.
PeptideAtlasiP22203.

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

eggNOGiCOG1390.
GeneTreeiENSGT00390000002730.
HOGENOMiHOG000202506.
InParanoidiP22203.
KOiK02150.
OMAiFLSADTC.
OrthoDBiEOG7380GZ.

Enzyme and pathway databases

BioCyciYEAST:G3O-33808-MONOMER.
ReactomeiREACT_322706. Transferrin endocytosis and recycling.
REACT_347079. Insulin receptor recycling.

Miscellaneous databases

NextBioi976864.
PROiP22203.

Gene expression databases

GenevestigatoriP22203.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "The 31-kDa polypeptide is an essential subunit of the vacuolar ATPase in Saccharomyces cerevisiae."
    Foury F.
    J. Biol. Chem. 265:18554-18560(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT.
  2. "Sequence of 29 kb around the PDR10 locus on the right arm of Saccharomyces cerevisiae chromosome XV: similarity to part of chromosome I."
    Parle-McDermott A.G., Hand N.J., Goulding S.E., Wolfe K.H.
    Yeast 12:999-1004(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Bienvenut W.V., Peters C.
    Submitted (MAY-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-26; 39-63; 69-77; 86-131; 145-158; 167-181 AND 197-227, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "Isolation of vacuolar membrane H(+)-ATPase-deficient yeast mutants; the VMA5 and VMA4 genes are essential for assembly and activity of the vacuolar H(+)-ATPase."
    Ho M.N., Hill K.J., Lindorfer M.A., Stevens T.H.
    J. Biol. Chem. 268:221-227(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 209-219, SUBUNIT.
  7. "Resolution of subunit interactions and cytoplasmic subcomplexes of the yeast vacuolar proton-translocating ATPase."
    Tomashek J.J., Sonnenburg J.L., Artimovich J.M., Klionsky D.J.
    J. Biol. Chem. 271:10397-10404(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION.
  8. "Characterization of a temperature-sensitive yeast vacuolar ATPase mutant with defects in actin distribution and bud morphology."
    Zhang J.W., Parra K.J., Liu J., Kane P.M.
    J. Biol. Chem. 273:18470-18480(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-145.
  9. "Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly."
    Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J.
    Nat. Cell Biol. 3:384-391(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAV1 AND RAV2.
  10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. "Defined sites of interaction between subunits E (Vma4p), C (Vma5p), and G (Vma10p) within the stator structure of the vacuolar H(+)-ATPase."
    Jones R.P.O., Durose L.J., Findlay J.B.C., Harrison M.A.
    Biochemistry 44:3933-3941(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VMA5 AND VMA10.
  13. Cited for: MUTAGENESIS OF SER-2; THR-6; THR-9; SER-78; TYR-160; THR-202; LYS-230 AND ASP-233.
  14. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

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: May 27, 2015
This is version 150 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

External Data

Dasty 3

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 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.