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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: 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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei145 – 1451Essential for proton translocation

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
Complete GO annotation...

Keywords - Biological processi

Hydrogen 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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1414VacuolarSequence analysisAdd
BLAST
Transmembranei15 – 3723HelicalSequence analysisAdd
BLAST
Topological domaini38 – 5922CytoplasmicSequence analysisAdd
BLAST
Transmembranei60 – 8021HelicalSequence analysisAdd
BLAST
Topological domaini81 – 9818VacuolarSequence analysisAdd
BLAST
Transmembranei99 – 12022HelicalSequence analysisAdd
BLAST
Topological domaini121 – 13212CytoplasmicSequence analysisAdd
BLAST
Transmembranei133 – 15826HelicalSequence analysisAdd
BLAST
Topological domaini159 – 1646VacuolarSequence analysis

GO - Cellular componenti

  • fungal-type vacuole Source: SGD
  • 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
Mutagenesisi145 – 1451E → D: Partial inactivation. 1 Publication
Mutagenesisi145 – 1451E → L or Q: Inactivation. 1 Publication

Chemistry

ChEMBLiCHEMBL1795084.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 164164V-type proton ATPase subunit c'PRO_0000071788Add
BLAST

Proteomic databases

MaxQBiP32842.
PeptideAtlasiP32842.

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. 200 interactions.
DIPiDIP-5394N.
IntActiP32842. 5 interactions.
MINTiMINT-498339.

Chemistry

BindingDBiP32842.

Structurei

3D structure databases

ProteinModelPortaliP32842.
SMRiP32842. Positions 17-164.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000056520.
KOiK02155.
OMAiIMKCLIP.
OrthoDBiEOG79W9J3.

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. 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 AAA35149.1 differs from that shown. Reason: Frameshift at position 102. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 359Missing in AAA35149 (PubMed:2192255).Curated

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.

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.
PIRiA41712.
RefSeqiNP_015090.1. NM_001184048.1.

3D structure databases

ProteinModelPortaliP32842.
SMRiP32842. Positions 17-164.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35928. 200 interactions.
DIPiDIP-5394N.
IntActiP32842. 5 interactions.
MINTiMINT-498339.

Chemistry

BindingDBiP32842.
ChEMBLiCHEMBL1795084.

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

MaxQBiP32842.
PeptideAtlasiP32842.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL234C; YPL234C; YPL234C.
GeneIDi855842.
KEGGisce:YPL234C.

Organism-specific databases

EuPathDBiFungiDB:YPL234C.
SGDiS000006155. VMA11.

Phylogenomic databases

HOGENOMiHOG000056520.
KOiK02155.
OMAiIMKCLIP.
OrthoDBiEOG79W9J3.

Enzyme and pathway databases

BioCyciYEAST:G3O-34121-MONOMER.

Miscellaneous databases

NextBioi980422.
PROiP32842.

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. 1 hit.
TIGRFAMsiTIGR01100. V_ATP_synt_C. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "VMA11, a novel gene that encodes a putative proteolipid, is indispensable for expression of yeast vacuolar membrane H(+)-ATPase activity."
    Umemoto N., Ohya Y., Anraku Y.
    J. Biol. Chem. 266:24526-24532(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: ATCC 26786 / X2180-1A.
  2. "Expression of a proteolipid gene from a high-copy-number plasmid confers trifluoperazine resistance to Saccharomyces cerevisiae."
    Shih C.-K., Kwong J., Montalvo E., Neff N.
    Mol. Cell. Biol. 10:3397-3404(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "VMA11 and VMA16 encode second and third proteolipid subunits of the Saccharomyces cerevisiae vacuolar membrane H+-ATPase."
    Hirata R., Graham L.A., Takatsuki A., Stevens T.H., Anraku Y.
    J. Biol. Chem. 272:4795-4803(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLU-145.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.

Entry informationi

Entry nameiVATL2_YEAST
AccessioniPrimary (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: May 11, 2016
This is version 153 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 538 molecules/cell in log phase SD medium.1 Publication

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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: 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.