NEO1 BASIC INFORMATION
| Standard Name | NEO1 1 |
|---|---|
| Systematic Name | YIL048W |
| Feature Type | ORF, Verified |
| Description | Putative aminophospholipid translocase (flippase) involved in endocytosis and vacuolar biogenesis; localizes to endosomes and the Golgi aparatus (2, 3, 4 and see Summary Paragraph)
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| Name Description | NEOmycin-resistance 1 |
| GO Annotations | All NEO1 GO evidence and references |
|---|---|
| View Computational GO annotations for NEO1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated | |
| High-throughput |
| Mutant Phenotype | All NEO1 Phenotype details and references |
|---|---|
| Large-scale survey | |
| null |
| Interactions | NEO1 All interactions details and references |
|---|---|
| 19 total interaction(s) for 18 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 | TCDB | UniProtKB |
|---|
| Primary SGDID | S000001310 |
|---|
ADDITIONAL INFORMATION for NEO1
SUMMARY PARAGRAPH for NEO1
S. cerevisiae has five genes encoding type 4 P-type ATPases: NEO1, DRS2, DNF1, DNF2, and DNF3. The "P-type" designation indicates that these integral membrane proteins form a covalent aspartyl-phosphate catalytic intermediate during ATP hydrolysis (2 and references therein). Most P-type ATPases mediate the transport of small cations across biological membranes. However, members of the "type 4" subfamily are aminophospholipid translocases (flippases), rather than cation transporters, and move phospholipids from one side of a membrane bilayer to the other (reviewed in 5). Of the five S. cerevisiae type 4 P-type ATPases, only NEO1 is essential. Although the four other genes appear to have substantial functional overlap (any single DRS2/DNF gene confers cell viability) (2), they are distinct in their localization, specificity, and cofactor association.
Neo1p localizes primarily to endosomes and the Golgi apparatus, where it contributes to endocytosis and vacuolar biogenesis (3, 4). Because of the essential nature of this gene, Neo1p aminophospholipid translocase activity has not yet been experimentally demonstrated and substrate specificity is not currently known. Neo1p is associated with Mon2p (4), a Sec7p-family protein that shares very little sequence similarity with the non-catalytic subunits of other S. cerevisiae type 4 P-type ATPases.
The P-type ATPase superfamily is evolutionarily conserved, but the type 4 subfamily is found only in eukaryotes. Fourteen type 4 P-type ATPases have been characterized in humans (5 and references therein), including the DRS2 homolog, ATP8A1 (aka ATPase II) (6) and the DNF1/DNF2 homolog ATP8B1 (aka FIC1) (2). Mutations in ATP8B1 result in progressive familial intrahepatic cholestasis (Byler disease), benign recurrent intrahepatic cholestasis (BRIC), and intrahepatic cholestasis of pregnancy (ICP).
REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for NEO1]
| 1) | Prezant TR, et al. (1996) Identification of an overexpressed yeast gene which prevents aminoglycoside toxicity. Microbiology 142 ( Pt 12):3407-14 |
| 2) | Hua Z, et al. (2002) An essential subfamily of Drs2p-related P-type ATPases is required for protein trafficking between Golgi complex and endosomal/vacuolar system. Mol Biol Cell 13(9):3162-77 |
| 3) | Hua Z and Graham TR (2003) Requirement for neo1p in retrograde transport from the Golgi complex to the endoplasmic reticulum. Mol Biol Cell 14(12):4971-83 |
| 4) | Wicky S, et al. (2004) Molecular interactions of yeast Neo1p, an essential member of the Drs2 family of aminophospholipid translocases, and its role in membrane trafficking within the endomembrane system. Mol Cell Biol 24(17):7402-18 |
| 5) | Paulusma CC and Oude Elferink RP (2005) The type 4 subfamily of P-type ATPases, putative aminophospholipid translocases with a role in human disease. Biochim Biophys Acta 1741(1-2):11-24 |
| 6) | Natarajan P, et al. (2004) Drs2p-coupled aminophospholipid translocase activity in yeast Golgi membranes and relationship to in vivo function. Proc Natl Acad Sci U S A 101(29):10614-9 |




