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PROSITE documentation PDOC50190 [for PROSITE entry PS50190]

SEC7 domain profile





Description

The SEC7 domain was named after the first protein found to contain such a region [1]. SEC7 family proteins are guanine nucleotide exchange factor (GEF) specific for the ADP-rybosylation factors (ARF), a Ras-like GTPases which is important for vesicular protein trafficking. Although SEC7 proteins are highly divergent in their overall sequence they share a common region of roughly 200 amino acids known as the SEC7 domain. Proteins containing a SEC7 domain are found in fungi, animals and plants.

SEC7 domains mediate interaction with ARF and catalyses GDP to GTP exchange [2,3,4]. Crystal structure of the human ARNO SEC7 domain has been solved [5,6] and consist of 10 α-helices. The helices are arranged in a right-handed superhelix reminiscent of that found in the armadillo-repeat (see <PDOC50176>). The C-terminal part of the domain mediates interaction with Arf-1 through hydrophobic and polar residues. The nucleotide exchange activity is dependent on a conserved glutamate residue located in the loop between helix f and g [5,6]. The corresponding residue in Arabidopsis Emb30 protein is mutated to a lysine in a deficient allele [7].

Some proteins known to contain a SEC7 domain are listed below.

  • Yeast SEC7 protein. Associated with ER, essential for fusion of vesicles to the Golgi.
  • Mammalian cytohesin 1.
  • Mammalian cytohesin 2 (ARF nucleotide-binding site opener; ARNO).
  • Mammalian cytohesin 3.
  • Mammalian cytohesin 4.
  • Mammalian brefeldin A-inhibited guanine nucleotide-exchange proteins 1 and 2 (ARFGEP1 and ARFGEP2).
  • Mammalian golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1 (GBF1).

We developed a profile that spans the whole domain.

Last update:

December 2001 / First entry.

Technical section

PROSITE method (with tools and information) covered by this documentation:

SEC7, PS50190; SEC7 domain profile  (MATRIX)


References

1AuthorsAchstetter T. Franzusoff A. Field C. Schekman R.
TitleSEC7 encodes an unusual, high molecular weight protein required for membrane traffic from the yeast Golgi apparatus.
SourceJ. Biol. Chem. 263:11711-11717(1988).
PubMed ID3042778

2AuthorsKlarlund J.K. Guilherme A. Holik J.J. Virbasius J.V. Chawla A. Czech M.P.
TitleSignaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains.
SourceScience 275:1927-1930(1997).
PubMed ID9072969

3AuthorsKlarlund J.K. Rameh L.E. Cantley L.C. Buxton J.M. Holik J.J. Sakelis C. Patki V. Corvera S. Czech M.P.
TitleRegulation of GRP1-catalyzed ADP ribosylation factor guanine nucleotide exchange by phosphatidylinositol 3,4,5-trisphosphate.
SourceJ. Biol. Chem. 273:1859-1862(1998).
PubMed ID9442017

4AuthorsAbergel C. Chavrier P. Claverie J.-M.
TitleTriple association of CDC25-, Dbl- and Sec7-related domains in mammalian guanine-nucleotide-exchange factors.
SourceTrends Biochem. Sci. 23:472-473(1998).
PubMed ID9868368

5AuthorsCherfils J. Menetrey J. Mathieu M. Le Bras G. Robineau S. Beraud-Dufour S. Antonny B. Chardin P.
TitleStructure of the Sec7 domain of the Arf exchange factor ARNO.
SourceNature 392:101-105(1998).
PubMed ID9510256
DOI10.1038/32210

6AuthorsMossessova E. Gulbis J.M. Goldberg J.
TitleStructure of the guanine nucleotide exchange factor Sec7 domain of human arno and analysis of the interaction with ARF GTPase.
SourceCell 92:415-423(1998).
PubMed ID9476900

7AuthorsShevell D.E. Leu W.M. Gillmor C.S. Xia G. Feldmann K.A. Chua N.H.
TitleEMB30 is essential for normal cell division, cell expansion, and cell adhesion in Arabidopsis and encodes a protein that has similarity to Sec7.
SourceCell 77:1051-1062(1994).
PubMed ID8020095



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