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Protein

V-type proton ATPase subunit F

Gene

VMA7

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 essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

GO - Molecular functioni

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

GO - Biological processi

  • ATP hydrolysis coupled proton transport Source: InterPro
  • vacuolar acidification Source: SGD
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-30746-MONOMER.
ReactomeiR-SCE-1222556. ROS, RNS production in response to bacteria.
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 F
Short name:
V-ATPase subunit F
Alternative name(s):
V-ATPase 14 kDa subunit
Vacuolar proton pump subunit F
Gene namesi
Name:VMA7
Ordered Locus Names:YGR020C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR020C.
SGDiS000003252. VMA7.

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 118118V-type proton ATPase subunit FPRO_0000144812Add
BLAST

Proteomic databases

MaxQBiP39111.
TopDownProteomicsiP39111.

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).

Binary interactionsi

WithEntry#Exp.IntActNotes
VMA13P418074EBI-20272,EBI-20281
VMA6P323665EBI-20272,EBI-20201
VMA8P326105EBI-20272,EBI-20264
VPH1P325635EBI-20272,EBI-20455

Protein-protein interaction databases

BioGridi33262. 45 interactions.
DIPiDIP-2077N.
IntActiP39111. 23 interactions.
MINTiMINT-507949.

Structurei

Secondary structure

1
118
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 43Combined sources
Beta strandi7 – 137Combined sources
Helixi14 – 229Combined sources
Turni23 – 264Combined sources
Turni30 – 323Combined sources
Beta strandi37 – 404Combined sources
Turni42 – 443Combined sources
Helixi47 – 5913Combined sources
Beta strandi62 – 698Combined sources
Helixi71 – 766Combined sources
Helixi78 – 825Combined sources
Beta strandi86 – 938Combined sources
Helixi108 – 1158Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J9Telectron microscopy6.90N1-118[»]
3J9Uelectron microscopy7.60N1-118[»]
3J9Velectron microscopy8.30N1-118[»]
4IX9X-ray2.33A/B/C/D1-94[»]
4RNDX-ray3.18B/D1-118[»]
5D80X-ray6.20O/o1-118[»]
ProteinModelPortaliP39111.
SMRiP39111. Positions 1-118.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase F subunit family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000013208.
HOGENOMiHOG000056545.
InParanoidiP39111.
KOiK02151.
OMAiHRIDTYT.
OrthoDBiEOG092C5L7Q.

Family and domain databases

Gene3Di3.40.50.10580. 1 hit.
InterProiIPR008218. ATPase_V1-cplx_f_g_su.
IPR005772. ATPase_V1-cplx_fsu_euk.
[Graphical view]
PANTHERiPTHR13861. PTHR13861. 1 hit.
PfamiPF01990. ATP-synt_F. 1 hit.
[Graphical view]
PIRSFiPIRSF015945. ATPase_V1_F_euk. 1 hit.
SUPFAMiSSF159468. SSF159468. 1 hit.
TIGRFAMsiTIGR01101. V_ATP_synt_F. 1 hit.

Sequencei

Sequence statusi: Complete.

P39111-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEKRTLIAV IADEDTTTGL LLAGIGQITP ETQEKNFFVY QEGKTTKEEI
60 70 80 90 100
TDKFNHFTEE RDDIAILLIN QHIAENIRAR VDSFTNAFPA ILEIPSKDHP
110
YDPEKDSVLK RVRKLFGE
Length:118
Mass (Da):13,461
Last modified:February 1, 1995 - v1
Checksum:iD21EC0980EB99DFF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10073 Genomic DNA. Translation: AAA50753.1.
U12786 Genomic DNA. Translation: AAA53208.1.
Z72805 Genomic DNA. Translation: CAA97003.1.
BK006941 Genomic DNA. Translation: DAA08116.1.
PIRiA55118.
RefSeqiNP_011534.1. NM_001181149.1.

Genome annotation databases

EnsemblFungiiYGR020C; YGR020C; YGR020C.
GeneIDi852903.
KEGGisce:YGR020C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10073 Genomic DNA. Translation: AAA50753.1.
U12786 Genomic DNA. Translation: AAA53208.1.
Z72805 Genomic DNA. Translation: CAA97003.1.
BK006941 Genomic DNA. Translation: DAA08116.1.
PIRiA55118.
RefSeqiNP_011534.1. NM_001181149.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J9Telectron microscopy6.90N1-118[»]
3J9Uelectron microscopy7.60N1-118[»]
3J9Velectron microscopy8.30N1-118[»]
4IX9X-ray2.33A/B/C/D1-94[»]
4RNDX-ray3.18B/D1-118[»]
5D80X-ray6.20O/o1-118[»]
ProteinModelPortaliP39111.
SMRiP39111. Positions 1-118.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33262. 45 interactions.
DIPiDIP-2077N.
IntActiP39111. 23 interactions.
MINTiMINT-507949.

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

MaxQBiP39111.
TopDownProteomicsiP39111.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR020C; YGR020C; YGR020C.
GeneIDi852903.
KEGGisce:YGR020C.

Organism-specific databases

EuPathDBiFungiDB:YGR020C.
SGDiS000003252. VMA7.

Phylogenomic databases

GeneTreeiENSGT00390000013208.
HOGENOMiHOG000056545.
InParanoidiP39111.
KOiK02151.
OMAiHRIDTYT.
OrthoDBiEOG092C5L7Q.

Enzyme and pathway databases

BioCyciYEAST:G3O-30746-MONOMER.
ReactomeiR-SCE-1222556. ROS, RNS production in response to bacteria.
R-SCE-77387. Insulin receptor recycling.
R-SCE-917977. Transferrin endocytosis and recycling.

Miscellaneous databases

PROiP39111.

Family and domain databases

Gene3Di3.40.50.10580. 1 hit.
InterProiIPR008218. ATPase_V1-cplx_f_g_su.
IPR005772. ATPase_V1-cplx_fsu_euk.
[Graphical view]
PANTHERiPTHR13861. PTHR13861. 1 hit.
PfamiPF01990. ATP-synt_F. 1 hit.
[Graphical view]
PIRSFiPIRSF015945. ATPase_V1_F_euk. 1 hit.
SUPFAMiSSF159468. SSF159468. 1 hit.
TIGRFAMsiTIGR01101. V_ATP_synt_F. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiVATF_YEAST
AccessioniPrimary (citable) accession number: P39111
Secondary accession number(s): D6VUF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 7, 2016
This is version 151 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 4050 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, 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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: 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.