TFP3/YPL234C Summary Help

TFP3 BASIC INFORMATION

Standard Name TFP3
Systematic Name YPL234C
Alias CLS9 , VMA11
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 (1, 2 and see Summary Paragraph)
Name Description TriFluoPerazine resistance 3
GO Annotations All TFP3 GO evidence and references
    View Computational GO annotations for TFP3
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Mutant Phenotype All TFP3 Phenotype details and references
Classical genetics
null
Large-scale survey
null
Interactions TFP3 All interactions details and references
27 total interaction(s) for 24 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 3
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 4
  • Co-fractionation: 1
  • Two-hybrid: 9

Genetic Interactions
  • Synthetic Growth Defect: 3
  • Synthetic Lethality: 6

Sequence Information
ChrXVI:105440 to 104946 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
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
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000006155

TFP3 RESOURCES

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SGD ORF mapGBrowse
SGD ORF map
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  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

SUMMARY PARAGRAPH for TFP3

TFP3 encodes the c' subunit of the yeast V-ATPase V0 domain (4, 1). 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 5, 6, 7 and 8.

The V0 c (Cup5p), c', and c'' (Ppa1p) subunits are highly hydrophobic integral membrane proteolipids, and have similar amino acid sequences; all three are required for V-ATPase activity (5, 8). The tfp3 null mutant is viable but lacks vacuolar (H )-ATPase activity, and is defective in vacuolar acidification (4). The a and b V0 subunits do not assemble in the absence of Tfp3p (4). Point mutations have identified amino acid residues in Tfp3p that are likely to be involved in proton transport(1).

Last updated: 2000-05-18

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for TFP3]

1) 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
2) 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
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) 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
5) Forgac M  (1999) Structure and properties of the vacuolar (H+)-ATPases. J Biol Chem 274(19):12951-4
6) Graham LA and Stevens TH  (1999) Assembly of the yeast vacuolar proton-translocating ATPase. J Bioenerg Biomembr 31(1):39-47
7) Kane PM  (1999) Biosynthesis and regulation of the yeast vacuolar H+-ATPase. J Bioenerg Biomembr 31(1):49-56
8) Stevens TH and Forgac M  (1997) Structure, function and regulation of the vacuolar (H+)-ATPase. Annu Rev Cell Dev Biol 13:779-808