P22203 (VATE_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	VMA4
Synonyms:	VAT5
Ordered Locus Names:	YOR332W
ORF Names:	O6241

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	233 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Subunit structure	V-ATPase is an 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. Ref.11
Sequence similarities	Belongs to the V-ATPase E subunit family.

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
Cellular component	Membrane Vacuole
Domain	Coiled coil
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro vacuolar acidification Traceable author statement. Source: SGD
Cellular component	fungal-type vacuole membrane Traceable author statement. Source: SGD vacuolar proton-transporting V-type ATPase, V1 domain Inferred from direct assay. Source: SGD
Molecular function	protein binding Inferred from physical interaction Ref.9. Source: IntAct proton-transporting ATPase activity, rotational mechanism Traceable author statement. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RAV1	P47104	4	EBI-20268,EBI-25471

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 233

232

V-type proton ATPase subunit E

PRO_0000117310

Regions

Region

8 – 20

13

Interaction with VMA5

Region

19 – 38

20

Interaction with VMA10

Coiled coil

15 – 45

31

Potential

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.5

Modified residue

9

1

Phosphothreonine Ref.15

Modified residue

95

1

Phosphoserine Ref.15

Experimental info

Mutagenesis

2

1

S → A: Reduces ATPase activity by 11%. Ref.14

Mutagenesis

6

1

T → A: Reduces ATPase activity by 73%. Ref.14

Mutagenesis

9

1

T → A: Increases ATPase activity 1.4-fold. Ref.14

Mutagenesis

78

1

S → A: Reduces ATPase activity by 88%. Prevents assembly of V1 subunits at the membrane. Ref.14

Mutagenesis

145

1

D → G in VMA4-1; is rapidly degraded at 37 degrees Celsius. Ref.8

Mutagenesis

160

1

Y → A: Reduces ATPase activity by 22%. Ref.14

Mutagenesis

202

1

T → 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

Mutagenesis

230

1

K → A: Increases ATPase activity 1.3-fold. Ref.14

Mutagenesis

233

1

D → 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 conflict

97 – 98

2

DG → ER in AAA35209. Ref.1

Secondary structure

1

.

.

.

.

.

233

Helix Strand Turn

Details...

Helix

11 – 58

48

Helix

62 – 68

7

Sequences

	Sequence		Length	Mass (Da)
	P22203 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 7AC5169FF7E5A39C	FASTA	233	26,471
	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

References

	« Hide 'large scale' referencesShow '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: 2145285] [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: 8896263] [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: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[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, 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: 8416931] [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: 8626613] [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: 9660816] [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: 11283612] [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: 14562095] [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: 14562106] [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: 15751969] [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: 15718227] [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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9 AND SER-95, MASS SPECTROMETRY.
+	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.

PIR

S62063.

RefSeq

NP_014977.1. NM_001183752.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KZ9	NMR	-	A	3-69	[»]

ProteinModelPortal

P22203.

SMR

P22203. Positions 1-69, 94-224.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4595N.

IntAct

P22203. 64 interactions.

MINT

MINT-564623.

STRING

P22203.

Protein family/group databases

TCDB

3.A.2.2.3. H+- or Na+-translocating F-type, V-type and A-type ATPase (F-ATPase) superfamily.

2D gel databases

SWISS-2DPAGE

P22203.

Proteomic databases

PeptideAtlas

P22203.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YOR332W; YOR332W; YOR332W.

GeneID

854509.

KEGG

sce:YOR332W.

NMPDR

fig|4932.3.peg.6093.

Organism-specific databases

SGD

S000005859. VMA4.

Phylogenomic databases

eggNOG

fuNOG09779.

GeneTree

EFGT00050000005082.

HOGENOM

HBG525538.

OMA

QQRQKIM.

OrthoDB

EOG4RBTV4.

Gene expression databases

ArrayExpress

P22203.

Genevestigator

P22203.

GermOnline

YOR332W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR002842. ATPase_V1/A1-cplx_esu.
[Graphical view]

KO

K02150.

Pfam

PF01991. vATP-synt_E. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

976864.

Entry information

Entry name

VATE_YEAST

Accession

Primary (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:	December 14, 2011
This is version 117 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program