| IED ID | IndEnz0002009561 |
| Enzyme Type ID | protease009561 |
| Protein Name |
CAAX prenyl protease 1 EC 3.4.24.84 A-factor-converting enzyme Prenyl protein-specific endoprotease 1 PPSEP 1 |
| Gene Name | STE24 AFC1 YJR117W J2032 |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MFDLKTILDHPNIPWKLIISGFSIAQFSFESYLTYRQYQKLSETKLPPVLEDEIDDETFHKSRNYSRAKAKFSIFGDVYNLAQKLVFIKYDLFPKIWHMAVSLLNAVLPVRFHMVSTVAQSLCFLGLLSSLSTLVDLPLSYYSHFVLEEKFGFNKLTVQLWITDMIKSLTLAYAIGGPILYLFLKIFDKFPTDFLWYIMVFLFVVQILAMTIIPVFIMPMFNKFTPLEDGELKKSIESLADRVGFPLDKIFVIDGSKRSSHSNAYFTGLPFTSKRIVLFDTLVNSNSTDEITAVLAHEIGHWQKNHIVNMVIFSQLHTFLIFSLFTSIYRNTSFYNTFGFFLEKSTGSFVDPVITKEFPIIIGFMLFNDLLTPLECAMQFVMSLISRTHEYQADAYAKKLGYKQNLCRALIDLQIKNLSTMNVDPLYSSYHYSHPTLAERLTALDYVSEKKKN |
| Enzyme Length | 453 |
| Uniprot Accession Number | P47154 |
| Absorption | |
| Active Site | ACT_SITE 298; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 394; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=The peptide bond hydrolyzed can be designated -C-|-A-A-X in which C is an S-isoprenylated cysteine residue, A is usually aliphatic and X is the C-terminal residue of the substrate protein, and may be any of several amino acids.; EC=3.4.24.84; |
| DNA Binding | |
| EC Number | 3.4.24.84 |
| Enzyme Function | FUNCTION: Proteolytically removes the C-terminal three residues of farnesylated A-factor mating pheromone. Also acts to cleave the N-terminal extension of the pheromone. Does not act on Ras. {ECO:0000269|PubMed:10692417, ECO:0000269|PubMed:9015299, ECO:0000269|PubMed:9065405, ECO:0000269|PubMed:9700155, ECO:0000269|PubMed:9725832}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (3); Topological domain (8); Transmembrane (7) |
| Keywords | Endoplasmic reticulum;Hydrolase;Membrane;Metal-binding;Metalloprotease;Pheromone response;Protease;Reference proteome;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9736709}; Multi-pass membrane protein {ECO:0000269|PubMed:9736709}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10688190; 10747800; 10760460; 11581258; 11950929; 12913070; 16093310; 16361710; 16429126; 16963638; 17467817; 18394190; 18467557; 18639527; 18923140; 19504624; 19536198; 19820121; 20505074; 21496492; 22933563; 23539602; 24040173; 26771486; 27129777; 27525482; 31644822; 32513868; 33033070; 9015298; 9122679; 9243507; 9559265; |
| Motif | |
| Gene Encoded By | |
| Mass | 52,324 |
| Kinetics | |
| Metal Binding | METAL 297; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 301; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 390; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.84; |