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Protein

V-type proton ATPase subunit d

Gene

VMA6

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

Functioni

Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. The active enzyme consists of a catalytic V1 domain attached to an integral membrane V0 proton pore complex. This subunit is a non-integral membrane component of the membrane pore domain and is required for proper assembly of the V0 sector. Might be involved in the regulated assembly of V1 subunits onto the membrane sector or alternatively may prevent the passage of protons through V0 pores.

Miscellaneous

Present with 1630 molecules/cell in log phase SD medium.1 Publication

GO - Molecular functioni

GO - Biological processi

  • ATP hydrolysis coupled proton transport Source: InterPro
  • vacuolar acidification Source: SGD
  • vacuolar transport Source: SGD

Keywordsi

Biological processHydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-32502-MONOMER
ReactomeiR-SCE-1222556 ROS, RNS production in phagocytes
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):
V-ATPase 39 kDa subunit
V-ATPase subunit M39
Vacuolar proton pump subunit d
Gene namesi
Name:VMA6
Ordered Locus Names:YLR447C
ORF Names:L9324.8
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR447C
SGDiS000004439 VMA6

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001193601 – 345V-type proton ATPase subunit dAdd BLAST345

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP32366
PaxDbiP32366
PRIDEiP32366

PTM databases

iPTMnetiP32366

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).1 Publication

Binary interactionsi

Protein-protein interaction databases

BioGridi31705, 71 interactors
ComplexPortaliCPX-1192 Vacuolar proton translocating ATPase complex, Golgi variant
CPX-1193 Vacuolar proton translocating ATPase complex, vacuole variant
DIPiDIP-1737N
IntActiP32366, 36 interactors
MINTiP32366
STRINGi4932.YLR447C

Structurei

Secondary structure

1345
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP32366
SMRiP32366
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase V0D/AC39 subunit family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000002200
HOGENOMiHOG000199065
InParanoidiP32366
KOiK02146
OMAiFMDFITY
OrthoDBiEOG092C3P8T

Family and domain databases

Gene3Di1.20.1690.10, 2 hits
InterProiView protein in InterPro
IPR036079 ATPase_su_C-like
IPR002843 ATPase_V0-cplx_csu/dsu
IPR016727 ATPase_V0-cplx_dsu
IPR035067 V-type_ATPase_suC
PANTHERiPTHR11028 PTHR11028, 1 hit
PfamiView protein in Pfam
PF01992 vATP-synt_AC39, 1 hit
PIRSFiPIRSF018497 V-ATP_synth_D, 1 hit
SUPFAMiSSF103486 SSF103486, 1 hit

Sequencei

Sequence statusi: Complete.

P32366-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEGVYFNIDN GFIEGVVRGY RNGLLSNNQY INLTQCDTLE DLKLQLSSTD
60 70 80 90 100
YGNFLSSVSS ESLTTSLIQE YASSKLYHEF NYIRDQSSGS TRKFMDYITY
110 120 130 140 150
GYMIDNVALM ITGTIHDRDK GEILQRCHPL GWFDTLPTLS VATDLESLYE
160 170 180 190 200
TVLVDTPLAP YFKNCFDTAE ELDDMNIEII RNKLYKAYLE DFYNFVTEEI
210 220 230 240 250
PEPAKECMQT LLGFEADRRS INIALNSLQS SDIDPDLKSD LLPNIGKLYP
260 270 280 290 300
LATFHLAQAQ DFEGVRAALA NVYEYRGFLE TGNLEDHFYQ LEMELCRDAF
310 320 330 340
TQQFAISTVW AWMKSKEQEV RNITWIAECI AQNQRERINN YISVY
Length:345
Mass (Da):39,791
Last modified:October 1, 1996 - v2
Checksum:i53A19450CAF35632
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti32N → T in AAA35210 (PubMed:8509410).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11584 Genomic DNA Translation: AAA35210.1
U22382 Genomic DNA Translation: AAB67533.1
BK006945 Genomic DNA Translation: DAA09747.1
PIRiS55969
RefSeqiNP_013552.3, NM_001182335.3

Genome annotation databases

EnsemblFungiiYLR447C; YLR447C; YLR447C
GeneIDi851168
KEGGisce:YLR447C

Similar proteinsi

Entry informationi

Entry nameiVA0D_YEAST
AccessioniPrimary (citable) accession number: P32366
Secondary accession number(s): D6VZ81
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: September 12, 2018
This is version 179 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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