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Synonyms
zmpste24, ste24p, face-1, atste24, afc1p, hs ste24p, a-factor converting enzyme,
more
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a-factor-CaaX + H2O
a-factor-C + aaX
-
endoproteolytic cleavage of a C-terminal tripeptide of prenylated proteins with a CaaX motif
?
a-factor + H2O
fragments of a-factor
a-factor-CaaX + H2O
a-factor + aaX
a-factor-CaaX + H2O
a-factor-C + aaX
YIIKGVFWDPA(farnesyl)CVIA + H2O
YIIKGVFWDPA(farnesyl)C + Val-Ile-Ala
-
farnesylated 15-mer peptide containing the mature a-factor sequence and the native a-factor CAAX motif
-
?
a-factor + H2O
fragments of a-factor
-
mating pheromone a-factor
-
?
a-factor + H2O
fragments of a-factor
-
Ste24 participates in both N- and C-terminal processing steps of a-factor
-
?
a-factor + H2O
fragments of a-factor
-
Ste24 participates in both N- and C-terminal processing steps of a-factor
-
?
a-factor + H2O
fragments of a-factor
-
mutant a-factor, containing a A8G point mutation is not cleaved suggesting that Ste24 N-terminal protease activity is highly discriminating
-
?
a-factor + H2O
fragments of a-factor
-
Ste24 is required for the first of the two N-terminal processing steps of mating pheromone a-factor
-
-
?
a-factor-CaaX + H2O
a-factor + aaX
-
removal of the last three amino acids of carboxyl-terminal sequence motif CaaX, enzyme proteolyzes a-factor with A, V, L, I, C or M at the a1 position, V, L, I, C or M at the a2 position or any amino acid at the X position
-
?
a-factor-CaaX + H2O
a-factor + aaX
-
removal of the last three amino acids of carboxyl-terminal sequence motif CaaX, enzyme proteolyzes a-factor with A,V, L, I, C or M at the a1 position, V, L, I, C or M at the a2 position or any amino acid at the X position
-
?
a-factor-CaaX + H2O
a-factor-C + aaX
-
endoproteolytic cleavage of a C-terminal tripeptide of prenylated proteins with a CAAX motif, enzyme may also play a role in amino-terminal proteolytic processing of a-factor
-
?
a-factor-CaaX + H2O
a-factor-C + aaX
-
endoproteolytic cleavage of a C-terminal tripeptide of prenylated proteins with a CaaX motif
-
?
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a-factor-CaaX + H2O
a-factor-C + aaX
-
endoproteolytic cleavage of a C-terminal tripeptide of prenylated proteins with a CaaX motif
?
a-factor + H2O
fragments of a-factor
a-factor-CaaX + H2O
a-factor + aaX
-
removal of the last three amino acids of carboxyl-terminal sequence motif CaaX, enzyme proteolyzes a-factor with A,V, L, I, C or M at the a1 position, V, L, I, C or M at the a2 position or any amino acid at the X position
-
?
a-factor-CaaX + H2O
a-factor-C + aaX
-
endoproteolytic cleavage of a C-terminal tripeptide of prenylated proteins with a CaaX motif
-
?
a-factor + H2O
fragments of a-factor
-
Ste24 participates in both N- and C-terminal processing steps of a-factor
-
-
?
a-factor + H2O
fragments of a-factor
-
Ste24 is required for the first of the two N-terminal processing steps of mating pheromone a-factor
-
-
?
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Fujimura-Kamada, K.; Nouvet, F.J.; Michaelis, S.
A novel membrane-associated metalloprotease, Ste24p, is required for the first step of NH2-terminal processing of the yeast a-factor precursor
J. Cell Biol.
136
271-285
1997
Saccharomyces cerevisiae
brenda
Tam, A.; Nouvet, F.J.; Fujimura-Kamada, K.; Slunt, H.; Sisodia, S.S.; Michaelis, S.
Dual roles for Ste24p in yeast a-factor maturation: NH2-terminal proteolysis and COOH-terminal CAAX processing
J. Cell Biol.
142
635-649
1998
Saccharomyces cerevisiae, Homo sapiens
brenda
Schmidt, W.K.; Tam, A.; Fujimura-Kamada, K.; Michaelis, S.
Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage
Proc. Natl. Acad. Sci. USA
95
11175-11180
1998
Saccharomyces cerevisiae
brenda
Schmidt, W.K.; Tam, A.; Michaelis, S.
Reconstitution of the Ste24p-dependent N-terminal proteolytic step in yeast a-factor biogenesis
J. Biol. Chem.
275
6227-6233
2000
Saccharomyces cerevisiae, Homo sapiens
brenda
Tam, A.; Schmidt, W.K.; Michaelis, S.
The multispanning membrane protein Ste24p catalyzes CAAX proteolysis and NH2-terminal processing of the yeast a-factor precursor
J. Biol. Chem.
276
46798-46806
2001
Saccharomyces cerevisiae
brenda
Bracha, K.; Lavy, M.; Yalovsky, S.
The Arabidopsis AtSTE24 is a CAAX protease with broad substrate specificity
J. Biol. Chem.
277
29856-29864
2002
Homo sapiens (O75844), Saccharomyces cerevisiae (P47154), Saccharomyces cerevisiae, Arabidopsis thaliana (Q8RX88)
brenda
Boyartchuk, V.L.; Rine, J.
Roles pf prenyl protein proteases in maturation of Saccharomyces cerevisiae
Genetics
150
95-1001
1998
Saccharomyces cerevisiae
brenda
Trueblood, C.E.; Boyartchuk, V.L.; Picologlou, E.A.; Rozema, D.; Poulter, C.D.; Rine, J.
The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct substrate specificities
Mol. Cell. Biol.
20
4381-4392
2000
Saccharomyces cerevisiae
brenda
Boyartchuk.V.L.; Ashby, M.N.; Rine, J.
Modulation of Ras and a-factor function by carboxyl-terminal proteolysis
Science
275
1796-1800
1997
Saccharomyces cerevisiae (P47154)
brenda
Pei, J.; Grishin, N.V.
Type II CAAX prenyl endopeptidases belong to a novel superfamily of putative membrane-bound metalloproteases
Trends Biochem. Sci.
26
275-277
2001
Saccharomyces cerevisiae
brenda
Porter, S.B.; Hildebrandt, E.R.; Breevoort, S.R.; Mokry, D.Z.; Dore, T.M.; Schmidt, W.K.
Inhibition of the CaaX proteases Rce1p and Ste24p by peptidyl (acyloxy)methyl ketones
Biochim. Biophys. Acta
1773
853-862
2007
Arabidopsis thaliana, Saccharomyces cerevisiae, Homo sapiens
brenda