UniProtKB - P32842 (VATL2_YEAST)
Protein
V-type proton ATPase subunit c'
Gene
VMA11
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
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.2 Publications
Miscellaneous
Present with 538 molecules/cell in log phase SD medium.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 145 | Essential for proton translocation | 1 |
GO - Molecular functioni
- proton-transporting ATPase activity, rotational mechanism Source: GO_Central
GO - Biological processi
- vacuolar acidification Source: SGD
Keywordsi
Biological process | Hydrogen ion transport, Ion transport, Transport |
Protein family/group databases
TCDBi | 3.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): Proteolipid protein VMA11 Trifluoperazine resistance protein 3 V-ATPase 16 kDa proteolipid subunit 2 Vacuolar proton pump c' subunit |
Gene namesi | Name:VMA11 Synonyms:CLS9, TFP3 Ordered Locus Names:YPL234C ORF Names:P1064 |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000006155, VMA11 |
VEuPathDBi | FungiDB:YPL234C |
Subcellular locationi
Vacuole
- fungal-type vacuole Source: SGD
- fungal-type vacuole membrane Source: SGD
- vacuolar proton-transporting V-type ATPase, V0 domain Source: SGD
Other locations
- cell periphery Source: SGD
- integral component of membrane Source: SGD
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 14 | VacuolarSequence analysisAdd BLAST | 14 | |
Transmembranei | 15 – 37 | HelicalSequence analysisAdd BLAST | 23 | |
Topological domaini | 38 – 59 | CytoplasmicSequence analysisAdd BLAST | 22 | |
Transmembranei | 60 – 80 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 81 – 98 | VacuolarSequence analysisAdd BLAST | 18 | |
Transmembranei | 99 – 120 | HelicalSequence analysisAdd BLAST | 22 | |
Topological domaini | 121 – 132 | CytoplasmicSequence analysisAdd BLAST | 12 | |
Transmembranei | 133 – 158 | HelicalSequence analysisAdd BLAST | 26 | |
Topological domaini | 159 – 164 | VacuolarSequence analysis | 6 |
Keywords - Cellular componenti
Membrane, VacuolePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 145 | E → D: Partial inactivation. 1 Publication | 1 | |
Mutagenesisi | 145 | E → L or Q: Inactivation. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL1795084 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000071788 | 1 – 164 | V-type proton ATPase subunit c'Add BLAST | 164 |
Proteomic databases
MaxQBi | P32842 |
PaxDbi | P32842 |
PRIDEi | P32842 |
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
BioGRIDi | 35928, 236 interactors |
ComplexPortali | CPX-1192, Vacuolar proton translocating ATPase complex, Golgi variant CPX-1193, Vacuolar proton translocating ATPase complex, vacuole variant |
DIPi | DIP-5394N |
IntActi | P32842, 7 interactors |
MINTi | P32842 |
STRINGi | 4932.YPL234C |
Chemistry databases
BindingDBi | P32842 |
Miscellaneous databases
RNActi | P32842, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P32842 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Belongs to the V-ATPase proteolipid subunit family.Curated
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG0232, Eukaryota |
GeneTreei | ENSGT00960000189220 |
HOGENOMi | CLU_085752_1_1_1 |
OMAi | AMIFGCM |
Family and domain databases
InterProi | View 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 |
Pfami | View protein in Pfam PF00137, ATP-synt_C, 2 hits |
PRINTSi | PR00122, VACATPASE |
SUPFAMi | SSF81333, SSF81333, 1 hit |
TIGRFAMsi | TIGR01100, V_ATP_synt_C, 1 hit |
i Sequence
Sequence statusi: Complete.
P32842-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSTQLASNIY APLYAPFFGF AGCAAAMVLS CLGAAIGTAK SGIGIAGIGT
60 70 80 90 100
FKPELIMKSL IPVVMSGILA IYGLVVAVLI AGNLSPTEDY TLFNGFMHLS
110 120 130 140 150
CGLCVGFACL SSGYAIGMVG DVGVRKYMHQ PRLFVGIVLI LIFSEVLGLY
160
GMIVALILNT RGSE
Sequence cautioni
The sequence AAA35149 differs from that shown. Reason: Frameshift.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 27 – 35 | Missing in AAA35149 (PubMed:2192255).Curated | 9 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D10486 Genomic DNA Translation: BAA01367.1 M32736 Genomic DNA Translation: AAA35149.1 Frameshift. Z67751 Genomic DNA Translation: CAA91610.1 X94561 Genomic DNA Translation: CAA64253.1 Z73590 Genomic DNA Translation: CAA97951.1 AY558058 Genomic DNA Translation: AAS56384.1 BK006949 Genomic DNA Translation: DAA11202.1 |
PIRi | A41712 |
RefSeqi | NP_015090.1, NM_001184048.1 |
Genome annotation databases
EnsemblFungii | YPL234C_mRNA; YPL234C; YPL234C |
GeneIDi | 855842 |
KEGGi | sce:YPL234C |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D10486 Genomic DNA Translation: BAA01367.1 M32736 Genomic DNA Translation: AAA35149.1 Frameshift. Z67751 Genomic DNA Translation: CAA91610.1 X94561 Genomic DNA Translation: CAA64253.1 Z73590 Genomic DNA Translation: CAA97951.1 AY558058 Genomic DNA Translation: AAS56384.1 BK006949 Genomic DNA Translation: DAA11202.1 |
PIRi | A41712 |
RefSeqi | NP_015090.1, NM_001184048.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
5TJ5 | electron microscopy | 3.90 | D | 17-163 | [»] | |
5VOX | electron microscopy | 6.80 | S | 1-164 | [»] | |
5VOY | electron microscopy | 7.90 | S | 1-164 | [»] | |
5VOZ | electron microscopy | 7.60 | S | 1-164 | [»] | |
6C6L | electron microscopy | 3.50 | D | 1-164 | [»] | |
6M0R | electron microscopy | 2.70 | D | 7-164 | [»] | |
6M0S | electron microscopy | 3.60 | D | 7-164 | [»] | |
6O7T | electron microscopy | 3.20 | o | 1-164 | [»] | |
6O7U | electron microscopy | 3.10 | o | 1-164 | [»] | |
6O7V | electron microscopy | 6.60 | o | 1-164 | [»] | |
6O7W | electron microscopy | 7.00 | o | 1-164 | [»] | |
6O7X | electron microscopy | 8.70 | o | 1-164 | [»] | |
6PE4 | electron microscopy | 3.10 | H | 1-164 | [»] | |
6PE5 | electron microscopy | 3.20 | H | 1-164 | [»] | |
SMRi | P32842 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 35928, 236 interactors |
ComplexPortali | CPX-1192, Vacuolar proton translocating ATPase complex, Golgi variant CPX-1193, Vacuolar proton translocating ATPase complex, vacuole variant |
DIPi | DIP-5394N |
IntActi | P32842, 7 interactors |
MINTi | P32842 |
STRINGi | 4932.YPL234C |
Chemistry databases
BindingDBi | P32842 |
ChEMBLi | CHEMBL1795084 |
Protein family/group databases
TCDBi | 3.A.2.2.3, the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily |
Proteomic databases
MaxQBi | P32842 |
PaxDbi | P32842 |
PRIDEi | P32842 |
Genome annotation databases
EnsemblFungii | YPL234C_mRNA; YPL234C; YPL234C |
GeneIDi | 855842 |
KEGGi | sce:YPL234C |
Organism-specific databases
SGDi | S000006155, VMA11 |
VEuPathDBi | FungiDB:YPL234C |
Phylogenomic databases
eggNOGi | KOG0232, Eukaryota |
GeneTreei | ENSGT00960000189220 |
HOGENOMi | CLU_085752_1_1_1 |
OMAi | AMIFGCM |
Miscellaneous databases
PROi | PR:P32842 |
RNActi | P32842, protein |
Family and domain databases
InterProi | View 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 |
Pfami | View protein in Pfam PF00137, ATP-synt_C, 2 hits |
PRINTSi | PR00122, VACATPASE |
SUPFAMi | SSF81333, SSF81333, 1 hit |
TIGRFAMsi | TIGR01100, V_ATP_synt_C, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | VATL2_YEAST | |
Accessioni | P32842Primary (citable) accession number: P32842 Secondary accession number(s): D6W3D6, P32365 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1993 |
Last sequence update: | October 1, 1993 | |
Last modified: | April 7, 2021 | |
This is version 194 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome XVI
Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families