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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: -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

Miscellaneous

Present with 55714 molecules/cell in log phase SD medium.1 Publication

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processHydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-33760-MONOMER
ReactomeiR-SCE-1222556 ROS, RNS production in phagocytes
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

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

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

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
PaxDbiP32563
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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi34659, 355 interactors
ComplexPortaliCPX-1193 Vacuolar proton translocating ATPase complex, vacuole variant
DIPiDIP-2960N
IntActiP32563, 35 interactors
MINTiP32563
STRINGi4932.YOR270C

Structurei

Secondary structure

1840
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
OMAiWTAYDAH
OrthoDBiEOG092C0YCY

Family and domain databases

InterProiView protein in InterPro
IPR002490 V-ATPase_116kDa_su
IPR026028 V-type_ATPase_116kDa_su_euka
PANTHERiPTHR11629 PTHR11629, 1 hit
PfamiView protein in Pfam
PF01496 V_ATPase_I, 1 hit
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

Similar proteinsi

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[»]
5TJ5electron microscopy3.90A400-829[»]
5VOXelectron microscopy6.80b1-840[»]
5VOYelectron microscopy7.90b1-840[»]
5VOZelectron microscopy7.60b1-840[»]
6C6Lelectron microscopy3.50A1-840[»]
ProteinModelPortaliP32563
SMRiP32563
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34659, 355 interactors
ComplexPortaliCPX-1193 Vacuolar proton translocating ATPase complex, vacuole variant
DIPiDIP-2960N
IntActiP32563, 35 interactors
MINTiP32563
STRINGi4932.YOR270C

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
PaxDbiP32563
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
OMAiWTAYDAH
OrthoDBiEOG092C0YCY

Enzyme and pathway databases

BioCyciYEAST:G3O-33760-MONOMER
ReactomeiR-SCE-1222556 ROS, RNS production in phagocytes
R-SCE-6798695 Neutrophil degranulation
R-SCE-77387 Insulin receptor recycling
R-SCE-917977 Transferrin endocytosis and recycling

Miscellaneous databases

EvolutionaryTraceiP32563
PROiPR:P32563

Family and domain databases

InterProiView protein in InterPro
IPR002490 V-ATPase_116kDa_su
IPR026028 V-type_ATPase_116kDa_su_euka
PANTHERiPTHR11629 PTHR11629, 1 hit
PfamiView protein in Pfam
PF01496 V_ATPase_I, 1 hit
PIRSFiPIRSF001293 ATP6V0A1, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiVPH1_YEAST
AccessioniPrimary (citable) accession number: P32563
Secondary accession number(s): D6W2X0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: October 10, 2018
This is version 187 of the entry and version 3 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

Documents

  1. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
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Main funding by: National Institutes of Health

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