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Protein

V-type proton ATPase subunit a, vacuolar isoform

Gene

VPH1

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 integral membrane V0 complex of vacuolar ATPase essential for assembly and catalytic activity. Is present only in vacuolar V-ATPase complexes. Enzymes containing this subunit have a 4-fold higher ratio of proton transport to ATP hydrolysis than complexes containing the Golgi/endosomal isoform and undergo reversible dissociation of V1 and V0 in response to glucose depletion. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.3 Publications

GO - Molecular functioni

  • ATPase binding Source: GO_Central
  • proton-transporting ATPase activity, rotational mechanism Source: UniProtKB

GO - Biological processi

  • ATP hydrolysis coupled proton transport Source: FlyBase
  • ATP synthesis coupled proton transport Source: GO_Central
  • cell growth Source: UniProtKB
  • polyphosphate metabolic process Source: SGD
  • protein complex assembly Source: SGD
  • proton transport Source: UniProtKB
  • vacuolar acidification Source: SGD
  • vacuolar proton-transporting V-type ATPase complex assembly Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-33760-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 a, vacuolar isoform
Short name:
V-ATPase a 1 subunit
Alternative name(s):
V-ATPase 95 kDa subunit
Vacuolar pH protein 1
Vacuolar proton pump a subunit
Vacuolar proton translocating ATPase subunit a 1
Gene namesi
Name:VPH1
Ordered Locus Names:YOR270C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR270C.
SGDiS000005796. VPH1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 404CytoplasmicSequence analysisAdd BLAST403
Transmembranei405 – 423HelicalSequence analysisAdd BLAST19
Topological domaini424 – 425VacuolarSequence analysis2
Transmembranei426 – 442HelicalSequence analysisAdd BLAST17
Topological domaini443 – 456CytoplasmicSequence analysisAdd BLAST14
Transmembranei457 – 486HelicalSequence analysisAdd BLAST30
Topological domaini487 – 534VacuolarSequence analysisAdd BLAST48
Transmembranei535 – 554HelicalSequence analysisAdd BLAST20
Topological domaini555 – 572CytoplasmicSequence analysisAdd BLAST18
Transmembranei573 – 593HelicalSequence analysisAdd BLAST21
Topological domaini594 – 636VacuolarSequence analysisAdd BLAST43
Transmembranei637 – 656HelicalSequence analysisAdd BLAST20
Topological domaini657 – 719CytoplasmicSequence analysisAdd BLAST63
Transmembranei720 – 744HelicalSequence analysisAdd BLAST25
Topological domaini745 – 765VacuolarSequence analysisAdd BLAST21
Transmembranei766 – 804HelicalSequence analysisAdd BLAST39
Topological domaini805 – 840CytoplasmicSequence analysisAdd BLAST36

GO - Cellular componenti

  • fungal-type vacuole Source: SGD
  • fungal-type vacuole membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • vacuolar proton-transporting V-type ATPase, V0 domain Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi425D → N: Reduces assembly of V-ATPase complexes and reduces ATPase activity of the assembled complexes. 1 Publication1
Mutagenesisi538K → A: Reduces assembly of V-ATPase complexes. 1 Publication1
Mutagenesisi593K → A: Reduces ATPase activity. 1 Publication1
Mutagenesisi634Q → L: Reduces subunit stability. 1 Publication1
Mutagenesisi729H → R: Reduces ATPase activity. 1 Publication1
Mutagenesisi735R → L: Reduces subunit stability. 1 Publication1
Mutagenesisi739L → S: Reduces ATPase activity. 1 Publication1
Mutagenesisi743H → A, E or Y: Reduces ATPase activity. 2 Publications1
Mutagenesisi746L → S: Reduces ATPase activity. 1 Publication1
Mutagenesisi780L → S: Reduces assembly of V-ATPase complexes. 1 Publication1
Mutagenesisi789E → A, D, H or Q: Abolishes ATPase activity and proton transport, but does not affect complex assembly. 2 Publications1
Mutagenesisi800L → S: Reduces assembly of V-ATPase complexes. 1 Publication1
Mutagenesisi802W → R: Reduces assembly of V-ATPase complexes. 1 Publication1
Mutagenesisi803V → D: Reduces ATPase activity. 1 Publication1
Mutagenesisi803V → F: Reduces assembly of V-ATPase complexes. 1 Publication1
Mutagenesisi809F → L: Reduces assembly of V-ATPase complexes. 1 Publication1
Mutagenesisi814G → D: Reduces assembly of V-ATPase complexes. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001192242 – 840V-type proton ATPase subunit a, vacuolar isoformAdd BLAST839

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1

Post-translational modificationi

Glycosylated.

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

MaxQBiP32563.
PRIDEiP32563.

PTM databases

iPTMnetiP32563.

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

WithEntry#Exp.IntActNotes
VMA6P323665EBI-20455,EBI-20201
VMA7P391115EBI-20455,EBI-20272

GO - Molecular functioni

Protein-protein interaction databases

BioGridi34659. 164 interactors.
DIPiDIP-2960N.
IntActiP32563. 31 interactors.
MINTiMINT-630784.

Structurei

Secondary structure

1840
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi723 – 725Combined sources3
Helixi729 – 747Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JTWNMR-A728-748[»]
2NVJNMR-A721-745[»]
2RPWNMR-X728-748[»]
3J9Telectron microscopy6.90b1-840[»]
3J9Uelectron microscopy7.60b1-840[»]
3J9Velectron microscopy8.30b1-840[»]
5I1Melectron microscopy7.00V383-840[»]
ProteinModelPortaliP32563.
SMRiP32563.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32563.

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili117 – 145Sequence analysisAdd BLAST29

Sequence similaritiesi

Belongs to the V-ATPase 116 kDa subunit family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000004941.
HOGENOMiHOG000037059.
InParanoidiP32563.
KOiK02154.
OMAiIHESEIY.
OrthoDBiEOG092C0YCY.

Family and domain databases

InterProiIPR002490. V-ATPase_116kDa_su.
IPR026028. V-type_ATPase_116kDa_su_euka.
[Graphical view]
PANTHERiPTHR11629. PTHR11629. 1 hit.
PfamiPF01496. V_ATPase_I. 1 hit.
[Graphical view]
PIRSFiPIRSF001293. ATP6V0A1. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32563-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEKEEAIFR SAEMALVQFY IPQEISRDSA YTLGQLGLVQ FRDLNSKVRA
60 70 80 90 100
FQRTFVNEIR RLDNVERQYR YFYSLLKKHD IKLYEGDTDK YLDGSGELYV
110 120 130 140 150
PPSGSVIDDY VRNASYLEER LIQMEDATDQ IEVQKNDLEQ YRFILQSGDE
160 170 180 190 200
FFLKGDNTDS TSYMDEDMID ANGENIAAAI GASVNYVTGV IARDKVATLE
210 220 230 240 250
QILWRVLRGN LFFKTVEIEQ PVYDVKTREY KHKNAFIVFS HGDLIIKRIR
260 270 280 290 300
KIAESLDANL YDVDSSNEGR SQQLAKVNKN LSDLYTVLKT TSTTLESELY
310 320 330 340 350
AIAKELDSWF QDVTREKAIF EILNKSNYDT NRKILIAEGW IPRDELATLQ
360 370 380 390 400
ARLGEMIARL GIDVPSIIQV LDTNHTPPTF HRTNKFTAGF QSICDCYGIA
410 420 430 440 450
QYREINAGLP TIVTFPFMFA IMFGDMGHGF LMTLAALSLV LNEKKINKMK
460 470 480 490 500
RGEIFDMAFT GRYIILLMGV FSMYTGFLYN DIFSKTMTIF KSGWKWPDHW
510 520 530 540 550
KKGESITATS VGTYPIGLDW AWHGTENALL FSNSYKMKLS ILMGFIHMTY
560 570 580 590 600
SYFFSLANHL YFNSMIDIIG NFIPGLLFMQ GIFGYLSVCI VYKWAVDWVK
610 620 630 640 650
DGKPAPGLLN MLINMFLSPG TIDDELYPHQ AKVQVFLLLM ALVCIPWLLL
660 670 680 690 700
VKPLHFKFTH KKKSHEPLPS TEADASSEDL EAQQLISAMD ADDAEEEEVG
710 720 730 740 750
SGSHGEDFGD IMIHQVIHTI EFCLNCVSHT ASYLRLWALS LAHAQLSSVL
760 770 780 790 800
WTMTIQIAFG FRGFVGVFMT VALFAMWFAL TCAVLVLMEG TSAMLHSLRL
810 820 830 840
HWVESMSKFF VGEGLPYEPF AFEYKDMEVA VASASSSASS
Length:840
Mass (Da):95,529
Last modified:January 23, 2007 - v3
Checksum:i77709A914410CD4D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M89778 Genomic DNA. Translation: AAA35211.1.
X89633 Genomic DNA. Translation: CAA61776.1.
Z75178 Genomic DNA. Translation: CAA99494.1.
Z75179 Genomic DNA. Translation: CAA99496.1.
BK006948 Genomic DNA. Translation: DAA11036.1.
PIRiA42970.
RefSeqiNP_014913.3. NM_001183689.3.

Genome annotation databases

EnsemblFungiiYOR270C; YOR270C; YOR270C.
GeneIDi854444.
KEGGisce:YOR270C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M89778 Genomic DNA. Translation: AAA35211.1.
X89633 Genomic DNA. Translation: CAA61776.1.
Z75178 Genomic DNA. Translation: CAA99494.1.
Z75179 Genomic DNA. Translation: CAA99496.1.
BK006948 Genomic DNA. Translation: DAA11036.1.
PIRiA42970.
RefSeqiNP_014913.3. NM_001183689.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JTWNMR-A728-748[»]
2NVJNMR-A721-745[»]
2RPWNMR-X728-748[»]
3J9Telectron microscopy6.90b1-840[»]
3J9Uelectron microscopy7.60b1-840[»]
3J9Velectron microscopy8.30b1-840[»]
5I1Melectron microscopy7.00V383-840[»]
ProteinModelPortaliP32563.
SMRiP32563.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34659. 164 interactors.
DIPiDIP-2960N.
IntActiP32563. 31 interactors.
MINTiMINT-630784.

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.

PTM databases

iPTMnetiP32563.

Proteomic databases

MaxQBiP32563.
PRIDEiP32563.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR270C; YOR270C; YOR270C.
GeneIDi854444.
KEGGisce:YOR270C.

Organism-specific databases

EuPathDBiFungiDB:YOR270C.
SGDiS000005796. VPH1.

Phylogenomic databases

GeneTreeiENSGT00390000004941.
HOGENOMiHOG000037059.
InParanoidiP32563.
KOiK02154.
OMAiIHESEIY.
OrthoDBiEOG092C0YCY.

Enzyme and pathway databases

BioCyciYEAST:G3O-33760-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

EvolutionaryTraceiP32563.
PROiP32563.

Family and domain databases

InterProiIPR002490. V-ATPase_116kDa_su.
IPR026028. V-type_ATPase_116kDa_su_euka.
[Graphical view]
PANTHERiPTHR11629. PTHR11629. 1 hit.
PfamiPF01496. V_ATPase_I. 1 hit.
[Graphical view]
PIRSFiPIRSF001293. ATP6V0A1. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiVPH1_YEAST
AccessioniPrimary (citable) accession number: P32563
Secondary accession number(s): D6W2X0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 55714 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

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.