| IED ID | IndEnz0002018874 |
| Enzyme Type ID | protease018874 |
| Protein Name |
CAAX prenyl protease 1 homolog EC 3.4.24.84 Farnesylated proteins-converting enzyme 1 FACE-1 |
| Gene Name | fce-1 C04F12.10 |
| Organism | Caenorhabditis elegans |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
| Enzyme Sequence | MDASCLFKALLATNWALFLWDQYITFRQYKAHKNAVKRPNEVKELIGEEDYKKARDYKIDNHLFGFFHSWFNQLLLTAQLIGGYYPFLWYATASYPLHVAVFLSINSIIETIIDLPWDLYSTFIIEDAHGFNKQTIGFYFVDKIKKMLVGFALTMPIVYGIEWIIVNGGPYFFVYIWLFVSVVVLLLMTIYPTFIAPLFDKYFPLPDGDLKTKIEQLAASLSYPLTELYVVNGSKRSAHSNAYMYGFWKNKRIVLYDTLLSGAEKEKVHELYVAAGEKIEETENDKKRGMNNDEVVAVLGHELGHWALWHTLINLVITEVNLFFSFAVFGYFYKWEALYQGFGYHDTPPVIGMMLIFQFVLALYNQLASIGMVIHSRSAEFGADEFAANLGHGENLIGALTKLGVDNLSMPINDSLYSWCTHTHPPVVERVAAVRAFQAKNK |
| Enzyme Length | 442 |
| Uniprot Accession Number | Q9XVE5 |
| Absorption | |
| Active Site | ACT_SITE 302; /evidence=ECO:0000250|UniProtKB:O75844; ACT_SITE 384; /note=Proton donor; /evidence=ECO:0000255 |
| 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; Evidence={ECO:0000269|PubMed:12487630}; |
| DNA Binding | |
| EC Number | 3.4.24.84 |
| Enzyme Function | FUNCTION: Proteolytically removes the C-terminal three residues of farnesylated proteins. {ECO:0000269|PubMed:12487630}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (3); Topological domain (7); Transmembrane (6) |
| Keywords | Endoplasmic reticulum;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P47154}; Multi-pass membrane protein {ECO:0000255}. Membrane {ECO:0000269|PubMed:12487630}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15338614; 17164286; 17486083; 17850180; 19343510; 21085631; 21177967; 21367940; 22347378; 22560298; 23800452; 25487147; 27506200; |
| Motif | |
| Gene Encoded By | |
| Mass | 50,699 |
| Kinetics | |
| Metal Binding | METAL 301; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:O75844; METAL 305; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:O75844; METAL 380; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:O75844 |
| Rhea ID | |
| Cross Reference Brenda |