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P22203 (VATE_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:VMA4
Synonyms:VAT5
Ordered Locus Names:YOR332W
ORF Names:O6241
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length233 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00311

Subunit structure

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. Ref.1 Ref.6 Ref.7 Ref.9 Ref.12

Subcellular location

Vacuole membrane; Peripheral membrane protein Ref.10.

Miscellaneous

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

Sequence similarities

Belongs to the V-ATPase E subunit family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RAV1P471043EBI-20268,EBI-25471

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 233232V-type proton ATPase subunit E HAMAP-Rule MF_00311
PRO_0000117310

Regions

Region8 – 2013Interaction with VMA5 HAMAP-Rule MF_00311
Region19 – 3820Interaction with VMA10 HAMAP-Rule MF_00311
Coiled coil15 – 4531 Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.5 Ref.16

Experimental info

Mutagenesis21S → A: Reduces ATPase activity by 11%. Ref.14
Mutagenesis61T → A: Reduces ATPase activity by 73%. Ref.14
Mutagenesis91T → A: Increases ATPase activity 1.4-fold. Ref.14
Mutagenesis781S → A: Reduces ATPase activity by 88%. Prevents assembly of V1 subunits at the membrane. Ref.14
Mutagenesis1451D → G in VMA4-1; is rapidly degraded at 37 degrees Celsius. Ref.8
Mutagenesis1601Y → A: Reduces ATPase activity by 22%. Ref.14
Mutagenesis2021T → 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. Ref.14
Mutagenesis2301K → A: Increases ATPase activity 1.3-fold. Ref.14
Mutagenesis2331D → A: Reduces ATPase activity by 74%. Reduces ATPase activity by 90% and produces structurally aberrant V-ATPase complexes; when associated with A-202. Ref.14
Sequence conflict97 – 982DG → ER in AAA35209. Ref.1

Secondary structure

...................... 233
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22203 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 7AC5169FF7E5A39C

FASTA23326,471
        10         20         30         40         50         60 
MSSAITALTP NQVNDELNKM QAFIRKEAEE KAKEIQLKAD QEYEIEKTNI VRNETNNIDG 

        70         80         90        100        110        120 
NFKSKLKKAM LSQQITKSTI ANKMRLKVLS AREQSLDGIF EETKEKLSGI ANNRDEYKPI 

       130        140        150        160        170        180 
LQSLIVEALL KLLEPKAIVK ALERDVDLIE SMKDDIMREY GEKAQRAPLE EIVISNDYLN 

       190        200        210        220        230 
KDLVSGGVVV SNASDKIEIN NTLEERLKLL SEEALPAIRL ELYGPSKTRK FFD 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[11]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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]Erratum
Jones R.P.O., Durose L.J., Findlay J.B.C., Harrison M.A.
Biochemistry 44:11924-11924(2005)
[14]"Mutational analysis of the stator subunit E of the yeast V-ATPase."
Owegi M.A., Carenbauer A.L., Wick N.M., Brown J.F., Terhune K.L., Bilbo S.A., Weaver R.S., Shircliff R., Newcomb N., Parra-Belky K.J.
J. Biol. Chem. 280:18393-18402(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF SER-2; THR-6; THR-9; SER-78; TYR-160; THR-202; LYS-230 AND ASP-233.
[15]"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].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60663 Genomic DNA. Translation: AAA35209.1.
Z49821 Genomic DNA. Translation: CAA89978.1.
Z75239 Genomic DNA. Translation: CAA99654.1.
BK006948 Genomic DNA. Translation: DAA11094.1.
PIRS62063.
RefSeqNP_014977.3. NM_001183752.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KZ9NMR-A3-69[»]
4DL0X-ray2.90E/J1-233[»]
4EFAX-ray2.82E1-233[»]
ProteinModelPortalP22203.
SMRP22203. Positions 2-226.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34716. 59 interactions.
DIPDIP-4595N.
IntActP22203. 17 interactions.
MINTMINT-564623.
STRING4932.YOR332W.

Protein family/group databases

TCDB3.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

PaxDbP22203.
PeptideAtlasP22203.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR332W; YOR332W; YOR332W.
GeneID854509.
KEGGsce:YOR332W.

Organism-specific databases

SGDS000005859. VMA4.

Phylogenomic databases

eggNOGCOG1390.
GeneTreeENSGT00390000002730.
HOGENOMHOG000202506.
KOK02150.
OMATIRCRKQ.
OrthoDBEOG7380GZ.

Enzyme and pathway databases

BioCycYEAST:G3O-33808-MONOMER.

Gene expression databases

GenevestigatorP22203.

Family and domain databases

HAMAPMF_00311. ATP_synth_E_arch.
InterProIPR002842. ATPase_V1/A1-cplx_esu.
[Graphical view]
PfamPF01991. vATP-synt_E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio976864.

Entry information

Entry nameVATE_YEAST
AccessionPrimary (citable) accession number: P22203
Secondary accession number(s): D6W328
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 138 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references