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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-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.
PeptideAtlasiP39111.
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[»]
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.
OMAiQNVAEMI.
OrthoDBiEOG7SN8RW.

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[»]
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.
PeptideAtlasiP39111.
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.
OMAiQNVAEMI.
OrthoDBiEOG7SN8RW.

Enzyme and pathway databases

BioCyciYEAST:G3O-30746-MONOMER.
ReactomeiR-SCE-77387. Insulin receptor recycling.
R-SCE-917977. Transferrin endocytosis and recycling.

Miscellaneous databases

NextBioi972586.
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...

Publicationsi

« Hide 'large scale' publications
  1. "The Saccharomyces cerevisiae VMA7 gene encodes a 14-kDa subunit of the vacuolar H(+)-ATPase catalytic sector."
    Nelson H., Mandiyan S., Nelson N.
    J. Biol. Chem. 269:24150-24155(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 200060 / W303.
  2. "VMA7 encodes a novel 14-kDa subunit of the Saccharomyces cerevisiae vacuolar H(+)-ATPase complex."
    Graham L.A., Hill K.J., Stevens T.H.
    J. Biol. Chem. 269:25974-25977(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Sigma 1278B.
  3. "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII."
    Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.
    Yeast 13:1077-1090(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

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: May 11, 2016
This is version 148 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.