| IED ID | IndEnz0002004169 |
| Enzyme Type ID | protease004169 |
| Protein Name |
Metacaspase-3 EC 3.4.22.- TcMCA3 |
| Gene Name | MCA3 |
| Organism | Trypanosoma cruzi (strain CL Brener) |
| Taxonomic Lineage | cellular organisms Eukaryota Discoba Euglenozoa Kinetoplastea (kinetoplasts) Metakinetoplastina Trypanosomatida Trypanosomatidae Trypanosoma Schizotrypanum Trypanosoma cruzi Trypanosoma cruzi (strain CL Brener) |
| Enzyme Sequence | MGFDFGCLLKLCSTVLKPGGAPGPINYMEIGLNLIKIAAPYIVQYLGIMERPPRVDVEEFFQQAEVTEGFKPWEAPTHVSGTFRALFIGINYYCTSAELSGCCNDVKQIIATLQRKRIPIDEMSILVDERGFPGANGLPTRDNIVRYMAWLFGGAKPGDVLFMHYSGHGTHTRATSDTEEKFDQCLAPVDFSTKGCILDNDIFRILLSGLLQGVRLTVVFDCCHSGSMLDLPYTFVGSRSLRRSVAGHMQRIRKGNDCAGDVLMISGCADEQTSADVSNAATFGTGASGAGGAATQCLAYTILKVSNLSYQDMLIATRDMLRRKGFTQVPQLSASKPINLQQKFSLMTTFEVDPAVAT |
| Enzyme Length | 358 |
| Uniprot Accession Number | Q2VLK6 |
| Absorption | |
| Active Site | ACT_SITE 168; /evidence=ECO:0000305|PubMed:22402587; ACT_SITE 223; /evidence=ECO:0000305|PubMed:22402587 |
| Activity Regulation | ACTIVITY REGULATION: Activated by Ca(2+). {ECO:0000269|PubMed:22402587}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Cysteine protease that cleaves specifically after arginine or lysine residues (PubMed:22402587). In epimastigotes, may play a role in cell cycle G1/S transition (PubMed:22402587). {ECO:0000269|PubMed:22402587}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Mutagenesis (2); Region (1) |
| Keywords | Calcium;Cytoplasm;Hydrolase;Metal-binding;Nucleus;Protease;Thiol protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16213036, ECO:0000269|PubMed:22402587}. Nucleus {ECO:0000269|PubMed:16213036}. Note=Localizes to cytoplasm in epimastigotes (PubMed:16213036). Translocates to the nucleus following apoptosis induced by human serum (PubMed:16213036). {ECO:0000269|PubMed:16213036}. |
| Modified Residue | |
| Post Translational Modification | PTM: In epimastigotes, the unprocessed enzyme appears to be the main form (PubMed:22402587). Auto-processing is dispensable for catalytic activity towards small oligopeptide substrates (PubMed:22402587). {ECO:0000269|PubMed:22402587}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 39,032 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |