Detail Information for IndEnz0002003471
IED ID IndEnz0002003471
Enzyme Type ID protease003471
Protein Name CAAX prenyl protease 1 homolog
EC 3.4.24.84
Zinc metalloproteinase Ste24 homolog
Gene Name TsSte24p
Organism Taenia solium (Pork tapeworm)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Spiralia Lophotrochozoa Platyhelminthes Cestoda Eucestoda Cyclophyllidea Taeniidae Taenia Taenia solium (Pork tapeworm)
Enzyme Sequence MDVGGALDLYGCSVNVYNAILIFIWVLFLWETYINLRQLKVAKRVTESPEEIKCLMNDVDFDKSRRYAIDKMNFDIVSGFYNILSLSAVLYFQLIAWAWHKSQEHMLFVCSYAPRSFGTTEGSEILFSLLFTVYVALFQFFESLPWSYYRHFVIEERYGFNKQTIGFFIKDRLKSLAVGLVIGLPIISMLVWIIKAGGHYFYIYAYGFTFVVSFIIMFIYPEFIAPIFDRYEHFPDCELRKKIEELAASIEFPLKKLYVVEGSKRSSHSNAYFYGFGKNKRIVLFDTLIKGFKMPGVEADSSANADESSDETQNRGCGDDEEILATLAHELGHWKLKHMTFNLIIAQINIFFMFFAFGQLINVDQLFVDFGFPPSTAPILIRLIVVFQFIFMPYSSVLEFLMTMLSRKFEFQADAFAVSLKSGEKLKSALLVLTKDNLSFPVYDWLYSMCNHSHPPIIERLAAIDAKMGKEK
Enzyme Length 472
Uniprot Accession Number Q3Y6B8
Absorption
Active Site ACT_SITE 330; /evidence=ECO:0000250|UniProtKB:O75844; ACT_SITE 414; /note=Proton donor; /evidence=ECO:0000255
Activity Regulation ACTIVITY REGULATION: Inhibited by ethylenediaminetetraacetic acid (EDTA) but not by serine, aspartic or cysteine protease inhibitors. Inhibited by high concentration of Zn(2+) (> 0.1 mM). {ECO:0000269|PubMed:16750535}.
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:0000250|UniProtKB:Q9XVE5};
DNA Binding
EC Number 3.4.24.84
Enzyme Function FUNCTION: Zinc-dependent metalloproteinase (PubMed:16750535). Proteolytically removes the C-terminal three residues of farnesylated proteins (By similarity). {ECO:0000250|UniProtKB:Q9XVE5, ECO:0000269|PubMed:16750535}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. Loss of catalytic activity at temperatures above 50 degrees Celsius. {ECO:0000269|PubMed:16750535};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:16750535};
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Metal binding (3); Topological domain (8); Transmembrane (7)
Keywords Disulfide bond;Endoplasmic reticulum;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Transmembrane;Transmembrane helix;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P47154}; Multi-pass membrane protein {ECO:0000255}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 54,546
Kinetics
Metal Binding METAL 329; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:O75844; METAL 333; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:O75844; METAL 410; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:O75844
Rhea ID
Cross Reference Brenda