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Protein

V-type proton ATPase subunit c''

Gene

VMA16

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei108 – 1081Essential for proton translocation

GO - Molecular functioni

  • hydrogen-exporting ATPase activity, phosphorylative mechanism Source: MGI
  • proton-transporting ATPase activity, rotational mechanism Source: SGD

GO - Biological processi

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

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-31086-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):
V-ATPase 22 kDa proteolipid subunit
Vacuolar proton pump c'' subunit
Gene namesi
Name:VMA16
Synonyms:PPA1
Ordered Locus Names:YHR026W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHR026W.
SGDiS000001068. VMA16.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1414CytoplasmicSequence analysisAdd
BLAST
Transmembranei15 – 3521HelicalSequence analysisAdd
BLAST
Topological domaini36 – 6126ExtracellularSequence analysisAdd
BLAST
Transmembranei62 – 8221HelicalSequence analysisAdd
BLAST
Topological domaini83 – 10018CytoplasmicSequence analysisAdd
BLAST
Transmembranei101 – 12121HelicalSequence analysisAdd
BLAST
Topological domaini122 – 14524ExtracellularSequence analysisAdd
BLAST
Transmembranei146 – 16722HelicalSequence analysisAdd
BLAST
Topological domaini168 – 17912CytoplasmicSequence analysisAdd
BLAST
Transmembranei180 – 20526HelicalSequence analysisAdd
BLAST
Topological domaini206 – 2138ExtracellularSequence analysis

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi108 – 1081E → D: Partial inactivation. 1 Publication
Mutagenesisi108 – 1081E → L, Q or V: Inactivation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 213213V-type proton ATPase subunit c''PRO_0000071780Add
BLAST

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

BioGridi36457. 54 interactions.
DIPiDIP-4054N.
IntActiP23968. 6 interactions.
MINTiMINT-539549.

Structurei

3D structure databases

ProteinModelPortaliP23968.
SMRiP23968. Positions 62-211.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00550000075120.
HOGENOMiHOG000056522.
KOiK03661.
OMAiGLYMLFT.
OrthoDBiEOG092C5DS5.

Family and domain databases

InterProiIPR002379. ATPase_proteolipid_c-like_dom.
IPR000245. ATPase_proteolipid_csu.
[Graphical view]
PfamiPF00137. ATP-synt_C. 2 hits.
[Graphical view]
PRINTSiPR00122. VACATPASE.
SUPFAMiSSF81333. SSF81333. 2 hits.

Sequencei

Sequence statusi: Complete.

P23968-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKESKDDDM SLGKFSFSHF LYYLVLIVVI VYGLYKLFTG HGSDINFGKF
60 70 80 90 100
LLRTSPYMWA NLGIALCVGL SVVGAAWGIF ITGSSMIGAG VRAPRITTKN
110 120 130 140 150
LISIIFCEVV AIYGLIIAIV FSSKLTVATA ENMYSKSNLY TGYSLFWAGI
160 170 180 190 200
TVGASNLICG IAVGITGATA AISDAADSAL FVKILVIEIF GSILGLLGLI
210
VGLLMAGKAS EFQ
Length:213
Mass (Da):22,596
Last modified:March 1, 1992 - v1
Checksum:i033FF5A516B97F8B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35294 Genomic DNA. Translation: AAA34892.1.
U10399 Genomic DNA. Translation: AAB68881.1.
AY692797 Genomic DNA. Translation: AAT92816.1.
BK006934 Genomic DNA. Translation: DAA06717.1.
PIRiA34633.
RefSeqiNP_011891.1. NM_001179156.1.

Genome annotation databases

EnsemblFungiiYHR026W; YHR026W; YHR026W.
GeneIDi856421.
KEGGisce:YHR026W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35294 Genomic DNA. Translation: AAA34892.1.
U10399 Genomic DNA. Translation: AAB68881.1.
AY692797 Genomic DNA. Translation: AAT92816.1.
BK006934 Genomic DNA. Translation: DAA06717.1.
PIRiA34633.
RefSeqiNP_011891.1. NM_001179156.1.

3D structure databases

ProteinModelPortaliP23968.
SMRiP23968. Positions 62-211.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36457. 54 interactions.
DIPiDIP-4054N.
IntActiP23968. 6 interactions.
MINTiMINT-539549.

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.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR026W; YHR026W; YHR026W.
GeneIDi856421.
KEGGisce:YHR026W.

Organism-specific databases

EuPathDBiFungiDB:YHR026W.
SGDiS000001068. VMA16.

Phylogenomic databases

GeneTreeiENSGT00550000075120.
HOGENOMiHOG000056522.
KOiK03661.
OMAiGLYMLFT.
OrthoDBiEOG092C5DS5.

Enzyme and pathway databases

BioCyciYEAST:G3O-31086-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

PROiP23968.

Family and domain databases

InterProiIPR002379. ATPase_proteolipid_c-like_dom.
IPR000245. ATPase_proteolipid_csu.
[Graphical view]
PfamiPF00137. ATP-synt_C. 2 hits.
[Graphical view]
PRINTSiPR00122. VACATPASE.
SUPFAMiSSF81333. SSF81333. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiVATO_YEAST
AccessioniPrimary (citable) accession number: P23968
Secondary accession number(s): D3DKX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: September 7, 2016
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: 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.