VMA11/YPL234C Summary Help

Standard Name VMA11 1, 2
Systematic Name YPL234C
Alias CLS9 , TFP3 3
Feature Type ORF, Verified
Description Vacuolar ATPase V0 domain subunit c'; involved in proton transport activity; hydrophobic integral membrane protein (proteolipid) containing four transmembrane segments; N and C termini are in the vacuolar lumen (4, 5 and see Summary Paragraph)
Name Description Vacuolar Membrane Atpase 2
Chromosomal Location
ChrXVI:105440 to 104946 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All VMA11 GO evidence and references
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 2 genes
Resources
Classical genetics
null
Large-scale survey
null
Resources
233 total interaction(s) for 200 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 10
  • Affinity Capture-RNA: 5
  • Affinity Capture-Western: 5
  • Co-fractionation: 3
  • PCA: 9
  • Protein-peptide: 1
  • Reconstituted Complex: 2

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 156
  • Positive Genetic: 25
  • Synthetic Growth Defect: 5
  • Synthetic Lethality: 10
  • Synthetic Rescue: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 164
Molecular Weight (Da) 17,037
Isoelectric Point (pI) 7.69
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXVI:105440 to 104946 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Last Update Coordinates: 1996-07-31 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..495 105440..104946 1996-07-31 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000006155
SUMMARY PARAGRAPH for VMA11

VMA11 encodes the c' subunit of the yeast V-ATPase V0 domain (2, 4). Vacuolar (H )-ATPases (V-ATPases) are ATP-dependent proton pumps that have been identified in many eukaryotes, where they acidify intracellular vacuolar compartments. Vacuolar acidification is important for many cellular processes, including endocytosis, targeting of newly synthesized lysosomal enzymes, and other molecular targeting processes. The V-ATPase consists of two separable domains. The V1 domain has eight known subunits, is peripherally associated with the vacuolar membrane, and catalyzes ATP hydrolysis. The V0 domain is an integral membrane structure of five subunits, and transports protons across the membrane. The structure, function, and assembly of V-ATPases are reviewed in references 6, 7, 8 and 9.

The V0 c (Vma3p), c', and c'' (Vma16p) subunits are highly hydrophobic integral membrane proteolipids, and have similar amino acid sequences; all three are required for V-ATPase activity (6, 9). The vma11 null mutant is viable but lacks vacuolar (H )-ATPase activity, and is defective in vacuolar acidification (2). The a and b V0 subunits do not assemble in the absence of Vma11p (2). Point mutations have identified amino acid residues in Vma11p that are likely to be involved in proton transport(4).

Last updated: 2000-05-18 Contact SGD

References cited on this page View Complete Literature Guide for VMA11
1) Ohya Y, et al.  (1991) Calcium-sensitive cls mutants of Saccharomyces cerevisiae showing a Pet- phenotype are ascribable to defects of vacuolar membrane H(+)-ATPase activity. J Biol Chem 266(21):13971-7
2) Umemoto N, et al.  (1991) VMA11, a novel gene that encodes a putative proteolipid, is indispensable for expression of yeast vacuolar membrane H(+)-ATPase activity. J Biol Chem 266(36):24526-32
3) Shih CK, et al.  (1990) Expression of a proteolipid gene from a high-copy-number plasmid confers trifluoperazine resistance to Saccharomyces cerevisiae. Mol Cell Biol 10(7):3397-404
4) Hirata R, et al.  (1997) VMA11 and VMA16 encode second and third proteolipid subunits of the Saccharomyces cerevisiae vacuolar membrane H+-ATPase. J Biol Chem 272(8):4795-803
5) Flannery AR, et al.  (2004) Topological characterization of the c, c', and c" subunits of the vacuolar ATPase from the yeast Saccharomyces cerevisiae. J Biol Chem 279(38):39856-62
6) Forgac M  (1999) Structure and properties of the vacuolar (H+)-ATPases. J Biol Chem 274(19):12951-4
7) Graham LA and Stevens TH  (1999) Assembly of the yeast vacuolar proton-translocating ATPase. J Bioenerg Biomembr 31(1):39-47
8) Kane PM  (1999) Biosynthesis and regulation of the yeast vacuolar H+-ATPase. J Bioenerg Biomembr 31(1):49-56
9) Stevens TH and Forgac M  (1997) Structure, function and regulation of the vacuolar (H+)-ATPase. Annu Rev Cell Dev Biol 13:779-808