ARF2 BASIC INFORMATION
| Standard Name | ARF2 1 |
|---|---|
| Systematic Name | YDL137W |
| Feature Type | ORF, Verified |
| Description | ADP-ribosylation factor, GTPase of the Ras superfamily involved in regulation of coated formation vesicles in intracellular trafficking within the Golgi; functionally interchangeable with Arf1p (1, 2 and see Summary Paragraph)
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| Name Description | ADP-Ribosylation Factor 1 |
| GO Annotations | All ARF2 GO evidence and references |
|---|---|
| View Computational GO annotations for ARF2 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated |
| Mutant Phenotype | All ARF2 Phenotype details and references |
|---|---|
| Classical genetics | |
| conditional | |
| overexpression | |
| Large-scale survey | |
| null | |
| overexpression |
| Interactions | ARF2 All interactions details and references |
|---|---|
| 51 total interaction(s) for 27 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| External Links | All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB |
|---|
| Primary SGDID | S000002296 |
|---|
ADDITIONAL INFORMATION for ARF2
SUMMARY PARAGRAPH for ARF2
ARF2 encodes one of three ADP ribosylation factors (ARFs) identified in S. cerevisiae (1). ARFs are GTPases of the Ras superfamily that regulate the formation of coated vesicles in intracellular trafficking (3, 4). The process of vesicle formation in the exocytic and endocytic pathways has been recently reviewed (5), as has the role of ARF (6). Yeast Arf1p and Arf2p are 96% identical in amino acid sequence; although deletion of ARF2 causes no detectable phenotype, Arf1p and Arf2p are functionally interchangeable (1). An arf1 arf2 double deletion is inviable (1), despite the presence of the third yeast ARF, Arf3p (7). Yeast ARF activity is regulated by the guanine nucleotide exchange factors Sec7p, Gea1p, and Gea2p (8, 9) and by the GTPase activating proteins Gcs1p (10) and Glo3p (2).
REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for ARF2]
| 1) | Stearns T, et al. (1990) ADP ribosylation factor is an essential protein in Saccharomyces cerevisiae and is encoded by two genes. Mol Cell Biol 10(12):6690-9 |
| 2) | Poon PP, et al. (1999) Retrograde transport from the yeast Golgi is mediated by two ARF GAP proteins with overlapping function. EMBO J 18(3):555-64 |
| 3) | Moss J and Vaughan M (1998) Molecules in the ARF orbit. J Biol Chem 273(34):21431-4 |
| 4) | Moss J and Vaughan M (1999) Activation of toxin ADP-ribosyltransferases by eukaryotic ADP-ribosylation factors. Mol Cell Biochem 193(1-2):153-7 |
| 5) | Springer S, et al. (1999) A primer on vesicle budding. Cell 97(2):145-8 |
| 6) | Roth MG (1999) Snapshots of ARF1: implications for mechanisms of activation and inactivation. Cell 97(2):149-52 |
| 7) | Lee FJ, et al. (1994) Characterization of a glucose-repressible ADP-ribosylation factor 3 (ARF3) from Saccharomyces cerevisiae. J Biol Chem 269(33):20931-7 |
| 8) | Peyroche A, et al. (1996) Nucleotide exchange on ARF mediated by yeast Gea1 protein. Nature 384(6608):479-81 |
| 9) | Sata M, et al. (1998) Brefeldin A-inhibited guanine nucleotide-exchange activity of Sec7 domain from yeast Sec7 with yeast and mammalian ADP ribosylation factors. Proc Natl Acad Sci U S A 95(8):4204-8 |
| 10) | Poon PP, et al. (1996) Saccharomyces cerevisiae Gcs1 is an ADP-ribosylation factor GTPase-activating protein. Proc Natl Acad Sci U S A 93(19):10074-7 |




