FOG16494
EOG88932F

sce:SSY5

Genes: 26

SGD Description
Serine protease of SPS plasma membrane amino acid sensor system; contains an inhibitory domain that dissociates in response to extracellular amino acids, freeing a catalytic domain to activate transcription factor Stp1p; other members are Ssy1p and Ptr3p


References

Jørgensen MU, et al. (1998 Jan 30). Mutations in five loci affecting GAP1-independent uptake of neutral amino acids in yeast.

Forsberg H, et al. (2001 Feb). Genetic and biochemical analysis of the yeast plasma membrane Ssy1p-Ptr3p-Ssy5p sensor of extracellular amino acids.

Bernard F, et al. (2001 Jul). Genetic analysis of the signalling pathway activated by external amino acids in Saccharomyces cerevisiae.

Andréasson C, et al. (2002 Dec 15). Receptor-mediated endoproteolytic activation of two transcription factors in yeast.

Abdel-Sater F, et al. (2004 Nov). Amino acid signaling in yeast: casein kinase I and the Ssy5 endoprotease are key determinants of endoproteolytic activation of the membrane-bound Stp1 transcription factor.

Poulsen P, et al. (2005 Jun). Constitutive signal transduction by mutant Ssy5p and Ptr3p components of the SPS amino acid sensor system in Saccharomyces cerevisiae.

Andréasson C, et al. (2006 Jun 15). Regulation of transcription factor latency by receptor-activated proteolysis.

Poulsen P, et al. (2006 Mar). Mapping of an internal protease cleavage site in the Ssy5p component of the amino acid sensor of Saccharomyces cerevisiae and functional characterization of the resulting pro- and protease domains by gain-of-function genetics.

Wendland J, et al. (2011 Dec). Genome evolution in the eremothecium clade of the Saccharomyces complex revealed by comparative genomics.

Mitochondrial localization predictions
Predotar	TargetP	MitoProt
Raw data
Phobius transmembrane predictions 3 genes with posterior transmembrane prediction > 50%