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Literature summary for 7.6.2.1 extracted from
- Cdc50p, a protein required for polarized growth, associates with the Drs2p P-type ATPase implicated in phospholipid translocation in Saccharomyces cerevisiae (2004), Mol. Biol. Cell, 15, 3418-3432.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Saccharomyces cerevisiae |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| trans-Golgi network transport vesicle | Cdc50p and Drs2p are localized to the trans-Golgi network and late endosome | Saccharomyces cerevisiae | 30140 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + H2O + phospholipid [side 1] = ADP + phosphate + phospholipid [side 2] | The Cdc50p/Lem3p family comprises a set of subunits specific to phospholipid-translocating P-type ATPases. Cdc50p physically associates with Drs2p. Cds50p forms a complex with Drs2p, whereas Lem3p forms a complex with Dnf1p in vivo. The Cdc50p-Drs2p complex possesses aminophospholipid translocase activity, which translocates aminophospholipids more efficiently than phosphatidylcholine. | Saccharomyces cerevisiae |
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