| IED ID | IndEnz0002016356 |
| Enzyme Type ID | protease016356 |
| Protein Name |
Metacaspase-9 AtMC9 EC 3.4.22.- Cleaved into: Metacaspase-9 subunit p20; Metacaspase-9 subunit p10 Metacaspase 2f AtMCP2f |
| Gene Name | AMC9 MCP2F At5g04200 F21E1.120 |
| 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 | MDQQGMVKKRLAVLVGCNYPNTRNELHGCINDVLAMKETILSRFGFKQDDIEVLTDEPESKVKPTGANIKAALRRMVDKAQAGSGDILFFHYSGHGTRIPSVKSAHPFKQDEAIVPCDFNLITDVDFRELVNQLPKGTSFTMISDSCHSGGLIDKEKEQIGPSSVSSNISPAIETTNKTITSRALPFKAVLDHLSSLTGITTSDIGTHLLELFGRDAGLKFRLPAMDLMDLLETMTAREKHVDSGILMSGCQADETSADVGVGNGKAYGAFSNAIQRVLNENEGAMKNKQLVMMARDVLERLGFHQHPCLYCSDQNADATFLSQP |
| Enzyme Length | 325 |
| Uniprot Accession Number | Q9FYE1 |
| Absorption | |
| Active Site | ACT_SITE 95; /evidence=ECO:0000250; ACT_SITE 147 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by serpin ZX and nitric oxide through cysteine nitrosylation. {ECO:0000269|PubMed:17028019, ECO:0000269|PubMed:17110382}. |
| 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. Required for proteolytic processing of GRI (PubMed:25398910). {ECO:0000269|PubMed:25398910}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (3); Erroneous initiation (1); Glycosylation (1); Modified residue (1); Mutagenesis (2); Site (2) |
| Keywords | Apoplast;Autocatalytic cleavage;Direct protein sequencing;Glycoprotein;Hydrolase;Protease;Reference proteome;S-nitrosylation;Secreted;Thiol protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:17028019}. |
| Modified Residue | MOD_RES 147; /note=S-nitrosocysteine; /evidence=ECO:0000269|PubMed:17110382 |
| Post Translational Modification | PTM: The two subunits are derived from the precursor sequence by an autocatalytic mechanism.; PTM: S-nitrosylation at Cys-147 suppresses both autoprocessing and proteolytic activity of the full-length protein, but does not affect the activity of the mature processed form. {ECO:0000269|PubMed:17110382}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16055634; 22112449; 23522353; 23834670; 23964026; 26740571; 27725825; 28179567; 29243818; 30176090; 30753577; 31454707; |
| Motif | |
| Gene Encoded By | |
| Mass | 35,505 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |