| IED ID | IndEnz0002002729 |
| Enzyme Type ID | protease002729 |
| Protein Name |
Cysteine proteinase ACP1 EC 3.4.22.- |
| Gene Name | ACP1 CP3 |
| Organism | Entamoeba histolytica |
| Taxonomic Lineage | cellular organisms Eukaryota Amoebozoa Evosea Archamoebae Mastigamoebida Entamoebidae Entamoeba Entamoeba histolytica |
| Enzyme Sequence | MFALILFVSLACANEVAFKQWAATHNKVFANRAEYLYRFAVFLDNKKFVEANANTELNVFADMTHEEFIQTHLGMTYEVPETTSNVKAAVKAAPESVDWRSIMNPAKDQGQCGSCWTFCTTAVLEGRVNKDLGKLYSFSEQQLVDCDASDNGCEGGHPSNSLKFIQENNGLGLESDYPYKAVAGTCKKVKNVATVTGSRRVTDGSETGLQTIIAENGPVAVGMDASRPSFQLYKKGTIYSDTKCRSRMMNHCVTAVGYGSNSNGKYWIIRNSWGTSWGDAGYFLLARDSNNMCGIGRDSNYPTGVKLI |
| Enzyme Length | 308 |
| Uniprot Accession Number | P36184 |
| Absorption | |
| Active Site | ACT_SITE 115; /evidence=ECO:0000250; ACT_SITE 251; /evidence=ECO:0000250; ACT_SITE 271; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Involved in pathogenicity. Its presence correlates with increased proteinase expression and activity in pathogenic isolates. Probably involved in tissue invasion. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (2); Propeptide (1); Sequence conflict (3); 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..13; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 33,851 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |