SEC7/YDR170C Summary Help

Standard Name SEC7 1
Systematic Name YDR170C
Feature Type ORF, Verified
Description Guanine nucleotide exchange factor (GEF) for ADP ribosylation factors involved in proliferation of the Golgi, intra-Golgi transport and ER-to-Golgi transport; found in the cytoplasm and on Golgi-associated coated vesicles (2, 3, 4 and see Summary Paragraph)
Name Description SECretory 5
Chromosomal Location
ChrIV:802222 to 796193 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Genetic position: 96 cM
Gene Ontology Annotations All SEC7 GO evidence and references
  View Computational GO annotations for SEC7
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Mutant phenotypes All SEC7 Phenotype evidence and references
Classical genetics
conditional
overexpression
Large-scale survey
conditional
null
reduction of function
Resources
interactions All SEC7 Interaction evidence and references
131 total interaction(s) for 98 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 53
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 5
  • Co-localization: 2
  • Co-purification: 2
  • PCA: 6
  • Protein-peptide: 1
  • Reconstituted Complex: 2
  • Two-hybrid: 3
Genetic Interactions
  • Dosage Lethality: 1
  • Dosage Rescue: 7
  • Phenotypic Enhancement: 2
  • Synthetic Growth Defect: 19
  • Synthetic Lethality: 26
  • Synthetic Rescue: 1
Resources
Expression Summary
histogram
Resources
Protein Information All SEC7 Protein evidence and references
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrIV:802222 to 796193 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Genetic position: 96 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..6030 802222..796193 2011-02-03 1996-07-31
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 SGDIDS000002577
SUMMARY PARAGRAPH for SEC7

SEC7 encodes a guanine nucleotide exchange factor (GEF) for ADP ribosylation factors (ARFs, encoded by ARF1, ARF2, and ARF3 in yeast) (6). ARFs are GTPases of the Ras superfamily that regulate the formation of coated vesicles in intracellular trafficking (7, 8). The process of vesicle formation in the exocytic and endocytic pathways has been recently reviewed (9), as has the role of ARF (10).

SEC7 was first identified through mutations that cause defects in protein transport and proliferation of the Golgi (2); it plays a role in intra-Golgi and ER-to-Golgi transport (3). Sec7p is found in the cytosol and as a component of Golgi-associated coated vesicles (4, 11). The catalytic activity of Sec7p resides in a 200 amino acid domain (6) called the Sec7 domain that is conserved in proteins from yeast (Gea1p and Gea2p; 12) and many other species, including human (13, 14, 15), rat (16), mouse (17), and Arabidopsis (18). A bovine protein, p200, with a Sec7 domain has been shown to act as a GEF for rat ARF (19). ARF GEFs are targets of the drug Brefeldin A, which inhibits secretion; different Sec7 domains show differing sensitivities to Brefeldin A (reviewed in 20).

Last updated: 1999-10-26

References cited on this page View Complete Literature Guide for SEC7
1) Novick P, et al.  (1980) Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell 21(1):205-15
2) Achstetter T, et al.  (1988) SEC7 encodes an unusual, high molecular weight protein required for membrane traffic from the yeast Golgi apparatus. J Biol Chem 263(24):11711-7
3) Wolf J, et al.  (1998) An N-end rule destabilization mutant reveals pre-Golgi requirements for Sec7p in yeast membrane traffic. Biochem Biophys Res Commun 243(1):191-8
4) Franzusoff A, et al.  (1991) Localization of components involved in protein transport and processing through the yeast Golgi apparatus. J Cell Biol 112(1):27-37
5) Novick P and Schekman R  (1979) Secretion and cell-surface growth are blocked in a temperature-sensitive mutant of Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 76(4):1858-62
6) 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
7) Moss J and Vaughan M  (1998) Molecules in the ARF orbit. J Biol Chem 273(34):21431-4
8) Moss J and Vaughan M  (1999) Activation of toxin ADP-ribosyltransferases by eukaryotic ADP-ribosylation factors. Mol Cell Biochem 193(1-2):153-7
9) Springer S, et al.  (1999) A primer on vesicle budding. Cell 97(2):145-8
10) Roth MG  (1999) Snapshots of ARF1: implications for mechanisms of activation and inactivation. Cell 97(2):149-52
11) Franzusoff A, et al.  (1992) Immuno-isolation of Sec7p-coated transport vesicles from the yeast secretory pathway. Nature 355(6356):173-5
12) Peyroche A, et al.  (1996) Nucleotide exchange on ARF mediated by yeast Gea1 protein. Nature 384(6608):479-81
13) Liu L and Pohajdak B  (1992) Cloning and sequencing of a human cDNA from cytolytic NK/T cells with homology to yeast SEC7. Biochim Biophys Acta 1132(1):75-8
14) Chardin P, et al.  (1996) A human exchange factor for ARF contains Sec7- and pleckstrin-homology domains. Nature 384(6608):481-4
15) Meacci E, et al.  (1997) Cytohesin-1, a cytosolic guanine nucleotide-exchange protein for ADP-ribosylation factor. Proc Natl Acad Sci U S A 94(5):1745-8
16) Telemenakis I, et al.  (1997) Rat homologues of yeast sec7p. Eur J Cell Biol 74(2):143-9
17) Klarlund JK, et al.  (1997) Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains. Science 275(5308):1927-30
18) Shevell DE, et al.  (1994) EMB30 is essential for normal cell division, cell expansion, and cell adhesion in Arabidopsis and encodes a protein that has similarity to Sec7. Cell 77(7):1051-62
19) Morinaga N, et al.  (1997) Cloning and expression of a cDNA encoding a bovine brain brefeldin A-sensitive guanine nucleotide-exchange protein for ADP-ribosylation factor. Proc Natl Acad Sci U S A 94(24):12926-31
20) Chardin P and McCormick F  (1999) Brefeldin A: the advantage of being uncompetitive. Cell 97(2):153-5