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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: -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.

Miscellaneous

Present with 8450 molecules/cell in log phase SD medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei137Essential for proton translocation1

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 transmembrane transport Source: SGD
  • vacuolar acidification Source: SGD
  • vacuole organization Source: SGD

Keywordsi

Biological processHydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-30150-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 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

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 domaini1 – 8VacuolarSequence analysis8
Transmembranei9 – 31HelicalSequence analysisAdd BLAST23
Topological domaini32 – 53CytoplasmicSequence analysisAdd BLAST22
Transmembranei54 – 74HelicalSequence analysisAdd BLAST21
Topological domaini75 – 90VacuolarSequence analysisAdd BLAST16
Transmembranei91 – 112HelicalSequence analysisAdd BLAST22
Topological domaini113 – 124CytoplasmicSequence analysisAdd BLAST12
Transmembranei125 – 150HelicalSequence analysisAdd BLAST26
Topological domaini151 – 160VacuolarSequence analysis10

Keywords - Cellular componenti

Membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi137E → D: Partial inactivation. 1 Publication1
Mutagenesisi137E → Q, V or K: Inactivation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000717621 – 160V-type proton ATPase subunit cAdd BLAST160

Proteomic databases

MaxQBiP25515
PaxDbiP25515
PRIDEiP25515
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, 389 interactors
ComplexPortaliCPX-1192 Vacuolar proton translocating ATPase complex, Golgi variant
CPX-1193 Vacuolar proton translocating ATPase complex, vacuole variant
DIPiDIP-8123N
IntActiP25515, 10 interactors
MINTiP25515
STRINGi4932.YEL027W

Structurei

Secondary structure

1160
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Turni7 – 9Combined sources3
Helixi10 – 42Combined sources33
Beta strandi44 – 46Combined sources3
Helixi50 – 53Combined sources4
Helixi55 – 75Combined sources21
Helixi84 – 121Combined sources38
Helixi123 – 125Combined sources3
Helixi126 – 152Combined sources27

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5TJ5electron microscopy3.90E/F/G/H/I/J/M/N9-158[»]
5VOXelectron microscopy6.80T/U/V/W/X/Y/Z/a1-160[»]
5VOYelectron microscopy7.90T/U/V/W/X/Y/Z/a1-160[»]
5VOZelectron microscopy7.60T/U/V/W/X/Y/Z/a1-160[»]
6C6Lelectron microscopy3.50E/F/G/H/I/J/K/L1-160[»]
ProteinModelPortaliP25515
SMRiP25515
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00550000074873
HOGENOMiHOG000056520
InParanoidiP25515
KOiK02155
OMAiDMFARGI
OrthoDBiEOG092C5DS5

Family and domain databases

InterProiView protein in InterPro
IPR002379 ATPase_proteolipid_c-like_dom
IPR000245 ATPase_proteolipid_csu
IPR011555 ATPase_proteolipid_su_C_euk
IPR035921 F/V-ATP_Csub_sf
PfamiView protein in Pfam
PF00137 ATP-synt_C, 2 hits
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

Similar proteinsi

Entry informationi

Entry nameiVATL1_YEAST
AccessioniPrimary (citable) accession number: P25515
Secondary accession number(s): D3DLM1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 20, 2018
This is version 176 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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