| IED ID | IndEnz0002002615 |
| Enzyme Type ID | protease002615 |
| Protein Name |
Aspartic protease 1 EC 3.4.23.- |
| Gene Name | asp-1 Y39B6A.20 |
| Organism | Caenorhabditis elegans |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
| Enzyme Sequence | MQTFVLLALVAACSAAVIQVPTHKTESLRAKLIKEGKYTAFLASQHAARAQQLNTGFQPFVDYFDDFYLGNITLGTPPQPATVVLDTGSSNLWVIDAACKTQACNGYPDSGYTKQKFDTTKSTTFVKETRKFSIQYGSGSCNGYLGKDVLNFGGLTVQSQEFGVSTHLADVFGYQPVDGILGLGWPALAVDQVVPPMQNLIAQKQLDAPLFTVWLDRNLQIAQGTPGGLITYGAIDTVNCAKQVTYVPLSAKTYWQFPLDAFAVGTYSETKKDQVISDTGTSWLGAPNTIVSAIVKQTKAVFDWSTELYTVDCSTMKTQPDLIFTIGGAQFPVKSVEYVLDLQLGGGKCALAVFSMGSGGFGPSWILGDTFIRQYCNVYDIGNGQIGFATAVHKGL |
| Enzyme Length | 396 |
| Uniprot Accession Number | G5EEI4 |
| Absorption | |
| Active Site | ACT_SITE 86; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103; ACT_SITE 278; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.23.- |
| Enzyme Function | FUNCTION: Aspartic protease, which is part of the necrosis cell death pathway (PubMed:26795495, PubMed:12410314). Promotes B.thuringiensis Cry6Aa stability by preventing its proteolysis by host gut proteases. Required for Cry6Aa-induced necrotic death of intestinal cells (PubMed:26795495). Cry6Aa uptake into the host intestinal cells triggers an increase in intracellular Ca(2+) levels leading to lysosome rupture and to the subsequent release of asp-1 which leads to necrosis (PubMed:26795495). {ECO:0000269|PubMed:12410314, ECO:0000269|PubMed:26795495}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Sequence conflict (2); Signal peptide (1) |
| Keywords | Aspartyl protease;Cytoplasm;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Necrosis;Protease;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Up-regulated by B.thuringiensis endotoxin Cry6Aa (at protein level). {ECO:0000269|PubMed:26795495}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10854422}. Lysosome {ECO:0000305|PubMed:10854422}. Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..15; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11559592; 14704431; 15990870; 16854972; 17164286; 17486083; 17889653; 19123269; 19343510; 21110867; 21177967; 22347378; 22560298; 23800452; 25487147; 26351692; 27506200; 31216475; |
| Motif | |
| Gene Encoded By | |
| Mass | 42,693 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |