ARF1/YDL192W Summary Help

Standard Name ARF1 1
Systematic Name YDL192W
Feature Type ORF, Verified
Description ADP-ribosylation factor; GTPase of the Ras superfamily involved in regulation of coated vesicle formation in intracellular trafficking within the Golgi; ARF1 has a paralog, ARF2, that arose from the whole genome duplication (1, 2, 3, 4 and see Summary Paragraph)
Name Description ADP-Ribosylation Factor 1
Chromosomal Location
ChrIV:116321 to 116866 | ORF Map | GBrowse
Genetic position: -91 cM
Gene Ontology Annotations All ARF1 GO evidence and references
  View Computational GO annotations for ARF1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 6 genes
Classical genetics
Large-scale survey
616 total interaction(s) for 326 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 33
  • Affinity Capture-RNA: 6
  • Affinity Capture-Western: 28
  • Biochemical Activity: 3
  • Co-crystal Structure: 3
  • Co-purification: 5
  • PCA: 34
  • Reconstituted Complex: 11
  • Two-hybrid: 8

Genetic Interactions
  • Dosage Growth Defect: 2
  • Dosage Lethality: 1
  • Dosage Rescue: 18
  • Negative Genetic: 277
  • Phenotypic Enhancement: 3
  • Phenotypic Suppression: 76
  • Positive Genetic: 57
  • Synthetic Growth Defect: 18
  • Synthetic Lethality: 28
  • Synthetic Rescue: 5

Expression Summary
Length (a.a.) 181
Molecular Weight (Da) 20,529
Isoelectric Point (pI) 7.46
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrIV:116321 to 116866 | ORF Map | GBrowse
Genetic position: -91 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..546 116321..116866 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 SGDIDS000002351

ARF1 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). Deletion of ARF1 causes defects in secretion (2). Yeast Arf1p and Arf2p are 96% identical in amino acid sequence and are functionally interchangeable (3). An arf1 arf2 double deletion is inviable (3), despite the presence of the third yeast ARF, Arf3p (9). Yeast ARF activity is regulated by the guanine nucleotide exchange factors Sec7p, Gea1p, Gea2p (10, 11), and Syt1p (12) and by the GTPase activating proteins Gcs1p (13), Glo3p (14), Age1p, and Age2p (15).

Last updated: 1999-10-28 Contact SGD

References cited on this page View Complete Literature Guide for ARF1
1) Sewell JL and Kahn RA  (1988) Sequences of the bovine and yeast ADP-ribosylation factor and comparison to other GTP-binding proteins. Proc Natl Acad Sci U S A 85(13):4620-4
2) Stearns T, et al.  (1990) ADP-ribosylation factor is functionally and physically associated with the Golgi complex. Proc Natl Acad Sci U S A 87(3):1238-42
3) 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
4) Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
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) 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
10) Peyroche A, et al.  (1996) Nucleotide exchange on ARF mediated by yeast Gea1 protein. Nature 384(6608):479-81
11) 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
12) Jones S, et al.  (1999) Genetic interactions in yeast between Ypt GTPases and Arf guanine nucleotide exchangers. Genetics 152(4):1543-56
13) 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
14) 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
15) Zhang CJ, et al.  (1998) A family of Arf effectors defined as suppressors of the loss of Arf function in the yeast Saccharomyces cerevisiae. J Biol Chem 273(31):19792-6