| IED ID | IndEnz0002019238 |
| Enzyme Type ID | protease019238 |
| Protein Name |
Cysteine proteinase 3 EC 3.4.22.- Cysteine proteinase ACP3 Fragment |
| Gene Name | CPNP |
| Organism | Entamoeba histolytica |
| Taxonomic Lineage | cellular organisms Eukaryota Amoebozoa Evosea Archamoebae Mastigamoebida Entamoebidae Entamoeba Entamoeba histolytica |
| Enzyme Sequence | LAIANAIDFNTWAANNNKHFTAVEALRRRAIFNMNARFVAEFNKKGSFKLSVDGPFAAMTNEEYRTLLKSKRTVEENGKVTYLNIQAPESVDWRAQGKVTPIRDQAQCGSCYTFGSLAALEGRLLIEKGGNANTLDLSEEHLVQCTRDNGNNGCNGGLGSNVYDYIIQNGVAKESDYPYTGTDSTCKTNVKAFAKITGYNKVPRNNEAELKAALSQGLVDVSIDASSAKFQLYKSGAYSDTKCKNNFFALNHEVCAVGYGVVDGKECWIVRNSWGTGWGDKGYINMVIEGNTCGVATDPLYPTGVQYL |
| Enzyme Length | 308 |
| Uniprot Accession Number | Q06964 |
| Absorption | |
| Active Site | ACT_SITE 111; /evidence=ECO:0000250; ACT_SITE 252; /evidence=ECO:0000250; ACT_SITE 272; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Can abolish adhesion and degrade matrix proteins such as collagen, laminin and fibronectin. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (2); Non-terminal residue (1); Propeptide (1); Signal peptide (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Hydrolase;Protease;Secreted;Signal;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL <1..?; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 33,680 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |