| Standard Name | PCA1 1 (see Nomenclature conflict Note) |
|---|---|
| Systematic Name | YBR295W |
| Alias | CAD2 2 , PAY2 |
| Feature Type | ORF, Verified |
| Description | Cadmium transporting P-type ATPase; may also have a role in copper and iron homeostasis; stabilized by Cd binding, which prevents ubiquitination; S288C and other lab strains contain a G970R mutation which eliminates Cd transport function (1, 2, 3, 4, 5 and see Summary Paragraph) |
| Name Description | P-type Cation-transporting ATPase 1 |
| Chromosomal Location | |
|---|---|
| Genetic position: 161 cM |
| View Computational GO annotations for PCA1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated | |
| High-throughput |
| Classical genetics | |
|---|---|
| gain of function | |
| null | |
| overexpression | |
| Large-scale survey | |
| null |
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| Resources |
| 26 total interaction(s) for 23 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| Resources |
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| Resources |
| Localization | |
|---|---|
| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
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| Genetic position: 161 cM | |||||||||||||
| Last Update | Coordinates: 2011-02-03 | Sequence: 2011-02-03 | ||||||||||||
| Subfeature details |
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| Retrieve sequences | |||||||||||||
| S288C only | |
|---|---|
| S288C vs. other species | |
| S288C vs. other strains |
| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
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| Primary SGDID | S000000499 |
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NOMENCLATURE CONFLICT NOTE
| Name | Relevance | Description |
|---|---|---|
| ACF2 | Nomenclature conflict | Both PCA1/YBR295W, which encodes a cation-transporting ATPase, and ACF2/YLR144C, which encodes a glucan 1,3-beta-glucosidase, have been referred to as PCA1. |
PCA1 encodes a plasma membrane P-type ATPase ion pump responsible for the export of toxic cadmium ions. Early studies of Pca1p were complicated by the fact that most laboratory strains, including S288C, contain a G970R nonsense mutation which eliminates normal cadmium transport function (2, 4). Although initial characterizations described Pca1p as a copper-transporting ATPase (1), subsequent experiments have demonstrated that Pca1p is capable of high affinity copper ion binding, but not active copper ion transport. It is possible that Pca1p plays a role in yeast copper resistance by chelating and sequestering copper ions (4). Pca1p is very closely related to the human gene ATP7A, mutations in which cause Menkes disease ('kinky hair' disease) and occipital horn syndrome. Menkes disease is associated with defective copper metabolism (6).
| 1) | Rad MR, et al. (1994) A putative P-type Cu(2+)-transporting ATPase gene on chromosome II of Saccharomyces cerevisiae. Yeast 10(9):1217-25 |
| 2) | Shiraishi E, et al. (2000) The cadmium-resistant gene, CAD2, which is a mutated putative copper-transporter gene (PCA1), controls the intracellular cadmium-level in the yeast S. cerevisiae. Curr Genet 37(2):79-86 |
| 3) | De Freitas JM, et al. (2004) Exploratory and confirmatory gene expression profiling of mac1Delta. J Biol Chem 279(6):4450-8 |
| 4) | Adle DJ, et al. (2007) A cadmium-transporting P1B-type ATPase in yeast Saccharomyces cerevisiae. J Biol Chem 282(2):947-55 |
| 5) | Adle DJ and Lee J (2008) Expressional Control of a Cadmium-transporting P1B-type ATPase by a Metal Sensing Degradation Signal. J Biol Chem 283(46):31460-8 |
| 6) | Pena MM, et al. (1999) A delicate balance: homeostatic control of copper uptake and distribution. J Nutr 129(7):1251-60 |






