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)
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| 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 |
| Interactions | TFP3 All interactions details and references |
|---|---|
| 27 total interaction(s) for 24 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB |
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| Primary SGDID | S000006155 |
|---|
ADDITIONAL INFORMATION for TFP3
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).
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 |




