Detail Information for IndEnz0002005701
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