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Protein

V-type proton ATPase subunit c

Gene

VMA3

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

Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. It is an electrogenic proton pump that generates a proton motive force of 180 mv, inside positive and acidic, in the vacuolar membrane vesicles.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei137 – 1371Essential for proton translocation

GO - Molecular functioni

GO - Biological processi

  • ATP hydrolysis coupled proton transport Source: InterPro
  • cellular copper ion homeostasis Source: SGD
  • cellular iron ion homeostasis Source: SGD
  • endocytosis Source: SGD
  • protein targeting to vacuole Source: SGD
  • proton transport Source: SGD
  • vacuolar acidification Source: SGD
  • vacuole organization Source: SGD
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-30150-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 c
Short name:
V-ATPase subunit c
Alternative name(s):
Guanine nucleotide exchange factor 2
V-ATPase 16 kDa proteolipid subunit 1
Vacuolar proton pump c subunit
Gene namesi
Name:VMA3
Synonyms:CLS7, CUP5, GEF2
Ordered Locus Names:YEL027W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YEL027W.
SGDiS000000753. VMA3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88VacuolarSequence analysis
Transmembranei9 – 3123HelicalSequence analysisAdd
BLAST
Topological domaini32 – 5322CytoplasmicSequence analysisAdd
BLAST
Transmembranei54 – 7421HelicalSequence analysisAdd
BLAST
Topological domaini75 – 9016VacuolarSequence analysisAdd
BLAST
Transmembranei91 – 11222HelicalSequence analysisAdd
BLAST
Topological domaini113 – 12412CytoplasmicSequence analysisAdd
BLAST
Transmembranei125 – 15026HelicalSequence analysisAdd
BLAST
Topological domaini151 – 16010VacuolarSequence analysis

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi137 – 1371E → D: Partial inactivation. 1 Publication
Mutagenesisi137 – 1371E → Q, V or K: Inactivation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 160160V-type proton ATPase subunit cPRO_0000071762Add
BLAST

Proteomic databases

MaxQBiP25515.
TopDownProteomicsiP25515.

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). The proteolipid components c, c' and c'' are present as a hexameric ring that forms the proton-conducting pore.

Protein-protein interaction databases

BioGridi36702. 180 interactions.
DIPiDIP-8123N.
IntActiP25515. 7 interactions.
MINTiMINT-1353979.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J9Telectron microscopy6.90R/S/T/U/V/W/X/Y/Z/a1-160[»]
3J9Uelectron microscopy7.60R/S/T/U/V/W/X/Y/Z/a1-160[»]
3J9Velectron microscopy8.30R/S/T/U/V/W/X/Y/Z/a1-160[»]
ProteinModelPortaliP25515.
SMRiP25515. Positions 11-160.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00550000074873.
HOGENOMiHOG000056520.
InParanoidiP25515.
KOiK02155.
OMAiQKLPLYT.
OrthoDBiEOG092C5DS5.

Family and domain databases

InterProiIPR002379. ATPase_proteolipid_c-like_dom.
IPR000245. ATPase_proteolipid_csu.
IPR011555. ATPase_proteolipid_su_C_euk.
[Graphical view]
PfamiPF00137. ATP-synt_C. 2 hits.
[Graphical view]
PRINTSiPR00122. VACATPASE.
SUPFAMiSSF81333. SSF81333. 2 hits.
TIGRFAMsiTIGR01100. V_ATP_synt_C. 1 hit.

Sequencei

Sequence statusi: Complete.

P25515-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTELCPVYAP FFGAIGCASA IIFTSLGAAY GTAKSGVGIC ATCVLRPDLL
60 70 80 90 100
FKNIVPVIMA GIIAIYGLVV SVLVCYSLGQ KQALYTGFIQ LGAGLSVGLS
110 120 130 140 150
GLAAGFAIGI VGDAGVRGSS QQPRLFVGMI LILIFAEVLG LYGLIVALLL
160
NSRATQDVVC
Length:160
Mass (Da):16,351
Last modified:May 1, 1992 - v1
Checksum:iFB8A142FFA1FA964
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15155 mRNA. Translation: CAA33249.1.
U18530 Genomic DNA. Translation: AAB64504.1.
AY558342 Genomic DNA. Translation: AAS56668.1.
BK006939 Genomic DNA. Translation: DAA07625.1.
PIRiS22257. PXBYL6.
RefSeqiNP_010887.3. NM_001178842.3.

Genome annotation databases

EnsemblFungiiYEL027W; YEL027W; YEL027W.
GeneIDi856686.
KEGGisce:YEL027W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15155 mRNA. Translation: CAA33249.1.
U18530 Genomic DNA. Translation: AAB64504.1.
AY558342 Genomic DNA. Translation: AAS56668.1.
BK006939 Genomic DNA. Translation: DAA07625.1.
PIRiS22257. PXBYL6.
RefSeqiNP_010887.3. NM_001178842.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J9Telectron microscopy6.90R/S/T/U/V/W/X/Y/Z/a1-160[»]
3J9Uelectron microscopy7.60R/S/T/U/V/W/X/Y/Z/a1-160[»]
3J9Velectron microscopy8.30R/S/T/U/V/W/X/Y/Z/a1-160[»]
ProteinModelPortaliP25515.
SMRiP25515. Positions 11-160.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36702. 180 interactions.
DIPiDIP-8123N.
IntActiP25515. 7 interactions.
MINTiMINT-1353979.

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

MaxQBiP25515.
TopDownProteomicsiP25515.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYEL027W; YEL027W; YEL027W.
GeneIDi856686.
KEGGisce:YEL027W.

Organism-specific databases

EuPathDBiFungiDB:YEL027W.
SGDiS000000753. VMA3.

Phylogenomic databases

GeneTreeiENSGT00550000074873.
HOGENOMiHOG000056520.
InParanoidiP25515.
KOiK02155.
OMAiQKLPLYT.
OrthoDBiEOG092C5DS5.

Enzyme and pathway databases

BioCyciYEAST:G3O-30150-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

PROiP25515.

Family and domain databases

InterProiIPR002379. ATPase_proteolipid_c-like_dom.
IPR000245. ATPase_proteolipid_csu.
IPR011555. ATPase_proteolipid_su_C_euk.
[Graphical view]
PfamiPF00137. ATP-synt_C. 2 hits.
[Graphical view]
PRINTSiPR00122. VACATPASE.
SUPFAMiSSF81333. SSF81333. 2 hits.
TIGRFAMsiTIGR01100. V_ATP_synt_C. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiVATL1_YEAST
AccessioniPrimary (citable) accession number: P25515
Secondary accession number(s): D3DLM1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: September 7, 2016
This is version 158 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 8450 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 V
    Yeast (Saccharomyces cerevisiae) chromosome V: 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.