ARF3/YOR094W Summary Help

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 regulating cell polarity and invasive growth; also has mRNA binding activity (1, 2, 3, 4 and see Summary Paragraph)
Name Description ADP-Ribosylation Factor 1
Chromosomal Location
ChrXV:502795 to 503346 | ORF Map | GBrowse
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
Regulators 6 genes
Classical genetics
Large-scale survey
51 total interaction(s) for 42 unique genes/features.
Physical Interactions
  • Affinity Capture-RNA: 3
  • Affinity Capture-Western: 4
  • Biochemical Activity: 1
  • Co-localization: 2
  • PCA: 6
  • Reconstituted Complex: 5
  • Two-hybrid: 6

Genetic Interactions
  • Dosage Rescue: 10
  • Negative Genetic: 8
  • Phenotypic Enhancement: 3
  • Phenotypic Suppression: 1
  • Positive Genetic: 1
  • Synthetic Growth Defect: 1

Expression Summary
Length (a.a.) 183
Molecular Weight (Da) 20,696
Isoelectric Point (pI) 10.21
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXV:502795 to 503346 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..552 502795..503346 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000005620

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 (5, 6). The process of vesicle formation in the exocytic and endocytic pathways has been recently reviewed (7), as has the role of ARF (8). Yeast ARF activity is regulated by the guanine nucleotide exchange factors Sec7p, Gea1p, and Gea2p (9, 10) and by the GTPase activating proteins Gcs1p (11) and Glo3p (12). Arf3p is not essential for viability or for ER to Golgi transport, and cannot substitute for Arf1p and Arf2p (1).

Last updated: 1999-10-28 Contact SGD

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) Hsu JW and Lee FJ  (2013) Arf3p GTPase is a key regulator of Bud2p activation for invasive growth in Saccharomyces cerevisiae. Mol Biol Cell 24(15):2328-39
5) Moss J and Vaughan M  (1998) Molecules in the ARF orbit. J Biol Chem 273(34):21431-4
6) Moss J and Vaughan M  (1999) Activation of toxin ADP-ribosyltransferases by eukaryotic ADP-ribosylation factors. Mol Cell Biochem 193(1-2):153-7
7) Springer S, et al.  (1999) A primer on vesicle budding. Cell 97(2):145-8
8) Roth MG  (1999) Snapshots of ARF1: implications for mechanisms of activation and inactivation. Cell 97(2):149-52
9) Peyroche A, et al.  (1996) Nucleotide exchange on ARF mediated by yeast Gea1 protein. Nature 384(6608):479-81
10) 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
11) 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
12) 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