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Protein

V-type proton ATPase subunit c'

Gene

VMA11

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.2 Publications

Miscellaneous

Present with 538 molecules/cell in log phase SD medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei145Essential for proton translocation1

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

Keywordsi

Biological processHydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-34121-MONOMER

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):
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
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL234C
SGDiS000006155 VMA11

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 – 14VacuolarSequence analysisAdd BLAST14
Transmembranei15 – 37HelicalSequence analysisAdd BLAST23
Topological domaini38 – 59CytoplasmicSequence analysisAdd BLAST22
Transmembranei60 – 80HelicalSequence analysisAdd BLAST21
Topological domaini81 – 98VacuolarSequence analysisAdd BLAST18
Transmembranei99 – 120HelicalSequence analysisAdd BLAST22
Topological domaini121 – 132CytoplasmicSequence analysisAdd BLAST12
Transmembranei133 – 158HelicalSequence analysisAdd BLAST26
Topological domaini159 – 164VacuolarSequence analysis6

Keywords - Cellular componenti

Membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi145E → D: Partial inactivation. 1 Publication1
Mutagenesisi145E → L or Q: Inactivation. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1795084

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000717881 – 164V-type proton ATPase subunit c'Add BLAST164

Proteomic databases

MaxQBiP32842
PaxDbiP32842
PRIDEiP32842

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

BioGridi35928, 235 interactors
ComplexPortaliCPX-1192 Vacuolar proton translocating ATPase complex, Golgi variant
CPX-1193 Vacuolar proton translocating ATPase complex, vacuole variant
DIPiDIP-5394N
IntActiP32842, 7 interactors
MINTiP32842
STRINGi4932.YPL234C

Chemistry databases

BindingDBiP32842

Structurei

Secondary structure

1164
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 11Combined sources3
Helixi15 – 48Combined sources34
Turni49 – 51Combined sources3
Helixi56 – 59Combined sources4
Helixi61 – 80Combined sources20
Beta strandi86 – 88Combined sources3
Helixi92 – 123Combined sources32
Helixi126 – 128Combined sources3
Helixi134 – 159Combined sources26

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5TJ5electron microscopy3.90D17-163[»]
5VOXelectron microscopy6.80S1-164[»]
5VOYelectron microscopy7.90S1-164[»]
5VOZelectron microscopy7.60S1-164[»]
6C6Lelectron microscopy3.50D1-164[»]
ProteinModelPortaliP32842
SMRiP32842
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000056520
KOiK02155
OMAiPDLIMKC
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, 1 hit
TIGRFAMsiTIGR01100 V_ATP_synt_C, 1 hit

Sequencei

Sequence statusi: Complete.

P32842-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:164
Mass (Da):17,037
Last modified:October 1, 1993 - v1
Checksum:iC82D165064EEBBF7
GO

Sequence cautioni

The sequence AAA35149 differs from that shown. Reason: Frameshift at position 102.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti27 – 35Missing in AAA35149 (PubMed:2192255).Curated9

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
PIRiA41712
RefSeqiNP_015090.1, NM_001184048.1

Genome annotation databases

EnsemblFungiiYPL234C; YPL234C; YPL234C
GeneIDi855842
KEGGisce:YPL234C

Similar proteinsi

Entry informationi

Entry nameiVATL2_YEAST
AccessioniPrimary (citable) accession number: P32842
Secondary accession number(s): D6W3D6, P32365
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 20, 2018
This is version 173 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

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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

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