| IED ID | IndEnz0002013734 |
| Enzyme Type ID | protease013734 |
| Protein Name |
Metacaspase-4 AtMC4 EC 3.4.22.- Metacaspase 2d AtMCP2d Metacaspase-7 Cleaved into: Metacaspase-4 subunit p20; Metacaspase-4 subunit p10 |
| Gene Name | AMC4 AMC7 MCP2D At1g79340 YUP8H12R.4 |
| Organism | Arabidopsis thaliana (Mouse-ear cress) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
| Enzyme Sequence | MTKKAVLIGINYPGTKAELRGCVNDVRRMYKCLVERYGFSEENITVLIDTDESSTQPTGKNIRRALADLVESADSGDVLVVHYSGHGTRLPAETGEDDDTGFDECIVPCDMNLITDDDFRDLVDKVPPGCRMTIISDSCHSGGLIDEAKEQIGESTKKEAEDEDESEESSSRFGFRKFLRSKVEGAIESRGFHIGGNKKDEDEAEEIETKEIELEDGETIHAKDKSLPLQTLIDILKQQTGNDNIEVGKIRPSLFDAFGDDSSPKVKKFMKVILGKLQAGNGEEGGLMGMLGKLASGFLEGKLNDEDYVKPAMQTHVGSKEEVYAGGSRGSVPLPDSGILISGCQTDQTSADATPAGKPTEAYGAMSNSIQTILEETDGEISNREMVTRARKALKKQGFTQQPGLYCHDGYANAPFIC |
| Enzyme Length | 418 |
| Uniprot Accession Number | O64517 |
| Absorption | |
| Active Site | ACT_SITE 86; /evidence=ECO:0000250; ACT_SITE 139 |
| Activity Regulation | ACTIVITY REGULATION: Activated by Ca(2+) which induces self-processing and accelerates the rate of the enzyme activity, but has no effect on Km. {ECO:0000269|PubMed:21209078}. |
| 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. Does not cleave caspase-specific substrates. Plays a positive regulatory role in biotic and abiotic stress-induced programmed cell death. {ECO:0000269|PubMed:15326173, ECO:0000269|PubMed:21209078, ECO:0000269|PubMed:21395887}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (12); Chain (3); Helix (14); Modified residue (1); Mutagenesis (4); Region (1); Sequence conflict (2); Site (1); Turn (2) |
| Keywords | 3D-structure;Autocatalytic cleavage;Cytoplasm;Hydrolase;Plant defense;Protease;Reference proteome;S-nitrosylation;Thiol protease |
| Interact With | Itself |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21395887}. |
| Modified Residue | MOD_RES 139; /note=S-nitrosocysteine; /evidence=ECO:0000250|UniProtKB:Q9FYE1 |
| Post Translational Modification | PTM: The two subunits are derived from the precursor sequence by an autocatalytic mechanism. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 6W8R; 6W8S; 6W8T; |
| Mapped Pubmed ID | 17644812; 18775970; 22112449; 27247031; 28627464; 29241568; 30176090; 30898901; 31454707; 32382010; |
| Motif | |
| Gene Encoded By | |
| Mass | 45,484 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=312 uM for t-butoxycarbonyl-GRR-aminomethylcoumarin (in the presence of 2 mM Ca(2+)) {ECO:0000269|PubMed:21209078}; KM=292 uM for t-butoxycarbonyl-GRR-aminomethylcoumarin (in the presence of 10 mM Ca(2+)) {ECO:0000269|PubMed:21209078}; KM=283 uM for t-butoxycarbonyl-GRR-aminomethylcoumarin (in the presence of 50 mM Ca(2+)) {ECO:0000269|PubMed:21209078}; Vmax=0.53 nmol/min/mg enzyme toward t-butoxycarbonyl-GRR-aminomethylcoumarin (in the presence of 2 mM Ca(2+)) {ECO:0000269|PubMed:21209078}; Vmax=2.28 nmol/min/mg enzyme toward t-butoxycarbonyl-GRR-aminomethylcoumarin (in the presence of 10 mM Ca(2+)) {ECO:0000269|PubMed:21209078}; Vmax=4.37 nmol/min/mg enzyme toward t-butoxycarbonyl-GRR-aminomethylcoumarin (in the presence of 50 mM Ca(2+)) {ECO:0000269|PubMed:21209078}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |