IED ID | IndEnz0002005701 |
Enzyme Type ID | protease005701 |
Protein Name |
Aspartic protease 17 EC 3.4.23.- |
Gene Name | asp-17 Y39B6A.24 |
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 | MHLIFLLFLAPFCSAAVFQLPTKSTGSLRAKLIRAGKYQEFLITQHAARLNTISQPISDYSDEVYLGNFTVGTPPQPVSLVLDTGSANMWVIDASCDNMFCNGWIGSNYTRQKFDTSKSSSFSRENRKFSIQYGKGLCSGYLGTDTVGLGGGLTIRKQELGIANKLDVDFAVQPMDGIFGLAWPALAVDQITPPMQNLISQLDVPVFSVWLDRKIQASHGGSAGMITYGGIDTKNCDAGVTYVPLTAKTYWQFKMDGFAVGTYSQYGYNQVISDTGSSWISAPYAMINDIATQTHATWDEMNEIYTVKCSTMKTQPDLVFTIGGALFPVKSVEYILDIGLDEGKCALAISPLMASGFGPSWILGDVFIRQYCNIYDIGNARIGFANAHHSF |
Enzyme Length | 391 |
Uniprot Accession Number | Q8MYN5 |
Absorption | |
Active Site | ACT_SITE 83; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103; ACT_SITE 274; /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 proteinase. {ECO:0000250|UniProtKB:Q9LTW4}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (2); Signal peptide (1) |
Keywords | Aspartyl protease;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Signal |
Interact With | |
Induction | INDUCTION: Induced in response to thermal stress in conditions where severe cold temperatures are followed by warmer temperatures (PubMed:29664006). In particular, induced in the warming phase (10 to 22 degrees Celsius) during the cold (4 degrees Celsius) to warm (22 degrees Celsius) temperature transition (PubMed:29664006). {ECO:0000269|PubMed:29664006}. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..15; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10778742; 22267497; 22286215; 22560298; 23800452; 24884423; 25487147; 6593563; |
Motif | |
Gene Encoded By | |
Mass | 42,754 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |