ID   3.4.26.1
DE   intramembrane prenyl-peptidase Rce1.
AN   CaaX prenyl protease 2.
AN   prenyl protein-specific endoprotease 2.
CA   Hydrolyzes the peptide bond -P2-(S-farnesyl or
CA   geranylgeranyl)C-P1'-P2'-P3'-COOH where P1' and P2' are amino acids with
CA   aliphatic sidechains and P3' is any C-terminal residue.
CC   -!- The cleavage site motif is typically referred to as CaaX, where the
CC       letter a represents any amino acid, rather than alanine, and X
CC       represents the C-terminal amino acid of the target protein.
CC   -!- The enzyme has been found in the yeast Saccharomyces cerevisiae and
CC       homologs exist in humans and several other species.
CC   -!- Although the cleavage site is similar to that of the metallo-
CC       peptidase EC 3.4.24.84, there appear to be specificity differences in
CC       the proteins hydrolyzed by these two enzymes, with amino-acid
CC       substitution studies indicating activity of the yeast enzyme toward
CC       substrates with a hydrophilic residue at (P1') that are not
CC       hydrolyzed by EC 3.4.24.84.
DR   Q8GW19, FACE2_ARATH;  A6H7A0, FACE2_BOVIN;  G5EEP3, FACE2_CAEEL;
DR   Q9U1H8, FACE2_DROME;  Q9Y256, FACE2_HUMAN;  P57791, FACE2_MOUSE;
DR   B0BMW8, FACE2_RAT  ;  Q6LZY8, RCE1_METMP ;  O94448, RCE1_SCHPO ;
DR   Q03530, RCE1_YEAST ;
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