| IED ID | IndEnz0002003467 |
| Enzyme Type ID | protease003467 |
| Protein Name |
CAAX prenyl protease 1 homolog EC 3.4.24.84 Farnesylated proteins-converting enzyme 1 FACE-1 Prenyl protein-specific endoprotease 1 Zinc metalloproteinase Ste24 homolog |
| Gene Name | ZMPSTE24 FACE1 STE24 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MGMWASLDALWEMPAEKRIFGAVLLFSWTVYLWETFLAQRQRRIYKTTTHVPPELGQIMDSETFEKSRLYQLDKSTFSFWSGLYSETEGTLILLFGGIPYLWRLSGRFCGYAGFGPEYEITQSLVFLLLATLFSALTGLPWSLYNTFVIEEKHGFNQQTLGFFMKDAIKKFVVTQCILLPVSSLLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYADYIAPLFDKFTPLPEGKLKEEIEVMAKSIDFPLTKVYVVEGSKRSSHSNAYFYGFFKNKRIVLFDTLLEEYSVLNKDIQEDSGMEPRNEEEGNSEEIKAKVKNKKQGCKNEEVLAVLGHELGHWKLGHTVKNIIISQMNSFLCFFLFAVLIGRKELFAAFGFYDSQPTLIGLLIIFQFIFSPYNEVLSFCLTVLSRRFEFQADAFAKKLGKAKDLYSALIKLNKDNLGFPVSDWLFSMWHYSHPPLLERLQALKTMKQH |
| Enzyme Length | 475 |
| Uniprot Accession Number | O75844 |
| Absorption | |
| Active Site | ACT_SITE 336; /evidence=ECO:0000269|PubMed:23539603; ACT_SITE 419; /note=Proton donor; /evidence=ECO:0000250 |
| 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 proteins. Acts on lamin A/C. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (6); Chain (1); Helix (21); Metal binding (3); Natural variant (4); Sequence conflict (1); Topological domain (8); Transmembrane (7); Turn (6) |
| Keywords | 3D-structure;Disease variant;Endoplasmic reticulum;Hydrolase;Membrane;Metal-binding;Metalloprotease;Nucleus;Protease;Reference proteome;Transmembrane;Transmembrane helix;Zinc |
| Interact With | P02545-1; P06821; C5E519; Q20MH8 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23539603}; Multi-pass membrane protein {ECO:0000269|PubMed:23539603}. Nucleus inner membrane {ECO:0000269|PubMed:23539603}; Multi-pass membrane protein {ECO:0000269|PubMed:23539603}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 2YPT; 4AW6; 5SYT; 6BH8; |
| Mapped Pubmed ID | 15671064; 15843403; 16297189; 17342744; 17352743; 17353931; 18230615; 19351612; 19383993; 19453269; 19645629; 19680556; 19841875; 19913121; 20101687; 20550970; 20628086; 20635340; 21108632; 21724554; 21911578; 22718200; 22936788; 23606334; 24101728; 25665578; 26379196; 26638075; 26724531; 27034136; 27129777; 27729169; 27774687; 28246125; 28594571; 29794150; 30082509; 30625386; 31644822; 32199981; 32799420; 32872320; 33130089; 33293369; 34003736; 34647350; |
| Motif | |
| Gene Encoded By | |
| Mass | 54,813 |
| Kinetics | |
| Metal Binding | METAL 335; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:23539603; METAL 339; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:23539603; METAL 415; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:23539603 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.84; |