| Standard Name | ARF3 1 |
|---|---|
| Systematic Name | YOR094W |
| Alias | ARL2 |
| Feature Type | ORF, Verified |
| Description | Glucose-repressible ADP-ribosylation factor, GTPase of the Ras superfamily involved in development of polarity; also has mRNA binding activity (1, 2, 3 and see Summary Paragraph) |
| Name Description | ADP-Ribosylation Factor 1 |
| Chromosomal Location | |
|---|---|
Gene Ontology Annotations All ARF3 GO evidence and references
| View Computational GO annotations for ARF3 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated |
Mutant phenotypes All ARF3 Phenotype evidence and references
| Classical genetics | |
|---|---|
| null | |
| Large-scale survey | |
| null | |
| Resources |
interactions All ARF3 Interaction evidence and references
| 45 total interaction(s) for 37 unique genes/features. | |
| Physical Interactions |
|
| Genetic Interactions |
|
| Resources |
|
Expression Summary
|
| |
| Resources |
Protein Information All ARF3 Protein evidence and references
| Localization | |
|---|---|
| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
sequence information
|
| |||||||||||||
| Last Update | Coordinates: 2011-02-03 | Sequence: 1996-07-31 | ||||||||||||
| Subfeature details |
| ||||||||||||
| Retrieve sequences | |||||||||||||
Analyze Sequence
| S288C only | |
|---|---|
| S288C vs. other species | |
| S288C vs. other strains |
Resources
| External Links | All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
|---|
| Primary SGDID | S000005620 |
|---|
SUMMARY PARAGRAPH for ARF3
ARF3 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 (4, 5). The process of vesicle formation in the exocytic and endocytic pathways has been recently reviewed (6), as has the role of ARF (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 (11). Arf3p is not essential for viability or for ER to Golgi transport, and cannot substitute for Arf1p and Arf2p (1).
References cited on this page View Complete Literature Guide for ARF3
| 1) | 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 |
| 2) | Huang CF, et al. (2003) Role for Arf3p in development of polarity, but not endocytosis, in Saccharomyces cerevisiae. Mol Biol Cell 14(9):3834-47 |
| 3) | Tsvetanova NG, et al. (2010) Proteome-Wide Search Reveals Unexpected RNA-Binding Proteins in Saccharomyces cerevisiae.LID - e12671 [pii] PLoS One 5(9) |
| 4) | Moss J and Vaughan M (1998) Molecules in the ARF orbit. J Biol Chem 273(34):21431-4 |
| 5) | Moss J and Vaughan M (1999) Activation of toxin ADP-ribosyltransferases by eukaryotic ADP-ribosylation factors. Mol Cell Biochem 193(1-2):153-7 |
| 6) | Springer S, et al. (1999) A primer on vesicle budding. Cell 97(2):145-8 |
| 7) | Roth MG (1999) Snapshots of ARF1: implications for mechanisms of activation and inactivation. Cell 97(2):149-52 |
| 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 |
| 11) | 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 |





