Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P25515 (VATL1_YEAST)

Last modified November 24, 2009. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    V-type proton ATPase subunit c
      Short name=V-ATPase subunit c
Alternative name(s):
    Vacuolar proton pump c subunit
    V-ATPase 16 kDa proteolipid subunit 1
Gene names
Name: VMA3
Synonyms: CLS7, CUP5, GEF2
Ordered Locus Names: YEL027W
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length160 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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.

Subunit structure

V-ATPase is an 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.

Subcellular location

Vacuole membrane; Multi-pass membrane protein.

Miscellaneous

Present with 8450 molecules/cell in log phase SD medium. Ref.5

Sequence similarities

Belongs to the V-ATPase proteolipid subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 160160V-type proton ATPase subunit c
PRO_0000071762

Regions

Topological domain1 – 88Vacuolar Potential
Transmembrane9 – 3123 Potential
Topological domain32 – 5322Cytoplasmic Potential
Transmembrane54 – 7421 Potential
Topological domain75 – 9016Vacuolar Potential
Transmembrane91 – 11222 Potential
Topological domain113 – 12412Cytoplasmic Potential
Transmembrane125 – 15026 Potential
Topological domain151 – 16010Vacuolar Potential

Sites

Site1371Essential for proton translocation

Experimental info

Mutagenesis1371E → D: Partial inactivation. Ref.4
Mutagenesis1371E → Q, V or K: Inactivation. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P25515-1 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: FB8A142FFA1FA964

FASTA16016,351
        10         20         30         40         50         60 
MTELCPVYAP FFGAIGCASA IIFTSLGAAY GTAKSGVGIC ATCVLRPDLL FKNIVPVIMA 

        70         80         90        100        110        120 
GIIAIYGLVV SVLVCYSLGQ KQALYTGFIQ LGAGLSVGLS GLAAGFAIGI VGDAGVRGSS 

       130        140        150        160 
QQPRLFVGMI LILIFAEVLG LYGLIVALLL NSRATQDVVC 

« Hide

References

« Hide 'large scale' references
[1]"The progenitor of ATP synthases was closely related to the current vacuolar H+-ATPase."
Nelson H., Nelson N.
FEBS Lett. 247:147-153(1989) [PubMed: 2540044] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed: 9169868] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"Mutational analysis of yeast vacuolar H(+)-ATPase."
Moumi T., Beltran C., Nelson H., Nelson N.
Proc. Natl. Acad. Sci. U.S.A. 88:1938-1942(1991) [PubMed: 1825730] [Abstract]
Cited for: MUTAGENESIS OF GLU-137.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"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: 16847258] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

X15155 mRNA. Translation: CAA33249.1.
U18530 Genomic DNA. Translation: AAB64504.1.
AY558342 Genomic DNA. Translation: AAS56668.1.
PIRPXBYL6. S22257.
RefSeqNP_010887.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:8123N.
STRINGP25515.

Protein family/group databases

TCDB3.A.2.2.3. H+- or Na+-translocating F-type, V-type and A-type ATPase (F-ATPase) superfamily.

Proteomic databases

PeptideAtlasP25515.

Genome annotation databases

EnsemblYEL027W; YEL027W; YEL027W; Saccharomyces cerevisiae. [Genome view]
GeneID856686.
KEGGsce:YEL027W.
NMPDRfig|4932.3.peg.1941.

Organism-specific databases

CYGDYEL027w.
SGDS000000753. CUP5.

Phylogenomic databases

HOGENOMP25515.
OMAIANNIGD
OrthoDBEOG9KWM8V

Enzyme and pathway databases

BRENDA3.6.3.14. 250.

Gene expression databases

ArrayExpressP25515.
GenevestigatorP25515.
GermOnlineYEL027W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR002379. ATPase_F0/V0-cplx_csu.
IPR000245. ATPase_V0-cplx_csu.
IPR011555. ATPase_V0-cplx_csu_euk.
[Graphical view]
PfamPF00137. ATP-synt_C. 2 hits.
[Graphical view]
PRINTSPR00122. VACATPASE.
TIGRFAMsTIGR01100. V_ATP_synt_C. 1 hit.
ProtoNetSearch...

Other Resources

NextBio982721.

Entry information

Entry nameVATL1_YEAST
AccessionPrimary (citable) accession number: P25515
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 24, 2009
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome V

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents