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Protein

V-type proton ATPase subunit D

Gene

VMA8

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system.

GO - Molecular functioni

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

GO - Biological processi

  • vacuolar acidification Source: SGD
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-30169-MONOMER.
ReactomeiR-SCE-1222556. ROS, RNS production in response to bacteria.
R-SCE-6798695. Neutrophil degranulation.
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 D
Short name:
V-ATPase subunit D
Alternative name(s):
Vacuolar proton pump subunit D
Gene namesi
Name:VMA8
Ordered Locus Names:YEL051W
ORF Names:SYGP-ORF11
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YEL051W.
SGDiS000000777. VMA8.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001442441 – 256V-type proton ATPase subunit DAdd BLAST256

Proteomic databases

MaxQBiP32610.
PRIDEiP32610.

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). Interacts with RAV1 and RAV2 components of the RAVE complex, which are essential for the stability and assembly of V-ATPase.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RAV1P471042EBI-20264,EBI-25471
VMA7P391115EBI-20264,EBI-20272

Protein-protein interaction databases

BioGridi36678. 205 interactors.
DIPiDIP-2959N.
IntActiP32610. 37 interactors.
MINTiMINT-640736.

Structurei

Secondary structure

1256
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi29 – 75Combined sources47
Helixi79 – 85Combined sources7
Beta strandi91 – 101Combined sources11
Beta strandi104 – 113Combined sources10
Beta strandi115 – 117Combined sources3
Helixi128 – 175Combined sources48
Helixi177 – 202Combined sources26

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J9Telectron microscopy6.90M1-256[»]
3J9Uelectron microscopy7.60M1-256[»]
3J9Velectron microscopy8.30M1-256[»]
4RNDX-ray3.18A/C1-256[»]
5BW9X-ray7.00G/g1-256[»]
5D80X-ray6.20G/g1-256[»]
ProteinModelPortaliP32610.
SMRiP32610.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase D subunit family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000010770.
HOGENOMiHOG000230791.
InParanoidiP32610.
KOiK02149.
OMAiNIMGVTV.
OrthoDBiEOG092C4UH1.

Family and domain databases

InterProiIPR002699. V_ATPase_D.
[Graphical view]
PANTHERiPTHR11671. PTHR11671. 1 hit.
PfamiPF01813. ATP-synt_D. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00309. V_ATPase_subD. 1 hit.

Sequencei

Sequence statusi: Complete.

P32610-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGNREQVFP TRMTLGLMKT KLKGANQGYS LLKRKSEALT KRFRDITKRI
60 70 80 90 100
DDAKQKMGRV MQTAAFSLAE VSYATGENIG YQVQESVSTA RFKVRARQEN
110 120 130 140 150
VSGVYLSQFE SYIDPEINDF RLTGLGRGGQ QVQRAKEIYS RAVETLVELA
160 170 180 190 200
SLQTAFIILD EVIKVTNRRV NAIEHVIIPR TENTIAYINS ELDELDREEF
210 220 230 240 250
YRLKKVQEKK QNETAKLDAE MKLKRDRAEQ DASEVAADEE PQGETLVADQ

EDDVIF
Length:256
Mass (Da):29,194
Last modified:October 1, 1993 - v1
Checksum:iFDE93E1FAF0AEC5B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18779 Genomic DNA. Translation: AAB64991.1.
BK006939 Genomic DNA. Translation: DAA07603.1.
PIRiS30826.
RefSeqiNP_010863.1. NM_001178866.1.

Genome annotation databases

EnsemblFungiiYEL051W; YEL051W; YEL051W.
GeneIDi856659.
KEGGisce:YEL051W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18779 Genomic DNA. Translation: AAB64991.1.
BK006939 Genomic DNA. Translation: DAA07603.1.
PIRiS30826.
RefSeqiNP_010863.1. NM_001178866.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J9Telectron microscopy6.90M1-256[»]
3J9Uelectron microscopy7.60M1-256[»]
3J9Velectron microscopy8.30M1-256[»]
4RNDX-ray3.18A/C1-256[»]
5BW9X-ray7.00G/g1-256[»]
5D80X-ray6.20G/g1-256[»]
ProteinModelPortaliP32610.
SMRiP32610.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36678. 205 interactors.
DIPiDIP-2959N.
IntActiP32610. 37 interactors.
MINTiMINT-640736.

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.

Proteomic databases

MaxQBiP32610.
PRIDEiP32610.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYEL051W; YEL051W; YEL051W.
GeneIDi856659.
KEGGisce:YEL051W.

Organism-specific databases

EuPathDBiFungiDB:YEL051W.
SGDiS000000777. VMA8.

Phylogenomic databases

GeneTreeiENSGT00390000010770.
HOGENOMiHOG000230791.
InParanoidiP32610.
KOiK02149.
OMAiNIMGVTV.
OrthoDBiEOG092C4UH1.

Enzyme and pathway databases

BioCyciYEAST:G3O-30169-MONOMER.
ReactomeiR-SCE-1222556. ROS, RNS production in response to bacteria.
R-SCE-6798695. Neutrophil degranulation.
R-SCE-77387. Insulin receptor recycling.
R-SCE-917977. Transferrin endocytosis and recycling.

Miscellaneous databases

PROiP32610.

Family and domain databases

InterProiIPR002699. V_ATPase_D.
[Graphical view]
PANTHERiPTHR11671. PTHR11671. 1 hit.
PfamiPF01813. ATP-synt_D. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00309. V_ATPase_subD. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiVATD_YEAST
AccessioniPrimary (citable) accession number: P32610
Secondary accession number(s): D3DLJ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: November 30, 2016
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 8500 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 V
    Yeast (Saccharomyces cerevisiae) chromosome V: 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.