| IED ID | IndEnz0002006895 |
| Enzyme Type ID | protease006895 |
| Protein Name |
Vignain EC 3.4.22.- Cysteine endopeptidase |
| Gene Name | CYSEP |
| Organism | Ricinus communis (Castor bean) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Malpighiales Euphorbiaceae Acalyphoideae Acalypheae Ricinus Ricinus communis (Castor bean) |
| Enzyme Sequence | MQKFILLALSLALVLAITESFDFHEKELESEESLWGLYERWRSHHTVSRSLHEKQKRFNVFKHNAMHVHNANKMDKPYKLKLNKFADMTNHEFRNTYSGSKVKHHRMFRGGPRGNGTFMYEKVDTVPASVDWRKKGAVTSVKDQGQCGSCWAFSTIVAVEGINQIKTNKLVSLSEQELVDCDTDQNQGCNGGLMDYAFEFIKQRGGITTEANYPYEAYDGTCDVSKENAPAVSIDGHENVPENDENALLKAVANQPVSVAIDAGGSDFQFYSEGVFTGSCGTELDHGVAIVGYGTTIDGTKYWTVKNSWGPEWGEKGYIRMERGISDKEGLCGIAMEASYPIKKSSNNPSGIKSSPKDEL |
| Enzyme Length | 360 |
| Uniprot Accession Number | O65039 |
| Absorption | |
| Active Site | ACT_SITE 150; ACT_SITE 286; ACT_SITE 307 |
| Activity Regulation | ACTIVITY REGULATION: Low pH triggers activation of the protease and removal of the propeptide and the KDEL motif. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Involved in programmed cell death. Shows a pronounced preference for hydrophobic residues in the P2 position and no obvious preference in the P1 position of the cleavage site. Accepts proline at the P1 and P1' positions. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (8); Chain (1); Disulfide bond (3); Helix (7); Propeptide (2); Region (2); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Cytoplasmic vesicle;Direct protein sequencing;Disulfide bond;Hydrolase;Protease;Signal;Thiol protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000269|PubMed:11296243}. Note=The pro-endopeptidase accumulates in the ricinosomes. |
| Modified Residue | |
| Post Translational Modification | PTM: The potential N-glycosylation site at Asn-115 is not glycosylated. |
| Signal Peptide | SIGNAL 1..20 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1S4V; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 40,111 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.B1; |