IED ID | IndEnz0002016252 |
Enzyme Type ID | protease016252 |
Protein Name |
Cystatin cpi-2 Ce-cpi-2a Cysele2 |
Gene Name | cpi-2 R01B10.1 |
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 | MKAILVFALIAISIISVNAGMMTGGSVEQDASQKEYSDKAWKAVKGINDQASNNGPYYYAPIKVTKASTQVVAGISTKLEVLVGESNCKKGELQAHEITSSNCQIKDGGSRALYQVTIWEKPWENFEQFTVEKIRDVTADEQF |
Enzyme Length | 143 |
Uniprot Accession Number | G5ECM9 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Cysteine protease inhibitor which inhibits members of the peptidase C1 family (PubMed:12704112, PubMed:15664654). Does not inhibit asparaginyl endopeptidase (PubMed:15664654). Required for the uptake and/or processing of yolk proteins during the development of oocytes, probably by regulating the catalytic activity of cysteine proteases cpl-1 and cpz-1 (PubMed:16857685). May play a protective role against exogenous cysteine proteases derived from soil bacteria or fungi, or rotting fruits and vegetation (PubMed:24001183). {ECO:0000269|PubMed:12704112, ECO:0000269|PubMed:15664654, ECO:0000269|PubMed:16857685, ECO:0000269|PubMed:24001183}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Disulfide bond (1); Motif (1); Signal peptide (1); Site (1) |
Keywords | Cytoplasm;Disulfide bond;Protease inhibitor;Reference proteome;Secreted;Signal;Thiol protease inhibitor |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16857685}. Secreted {ECO:0000269|PubMed:16857685}. Cytoplasmic granule {ECO:0000269|PubMed:16857685}. Note=Localizes to the sheath cell cytoplasm surrounding germ cells and oocytes. Localizes to yolk granules in the developing oocyte. {ECO:0000269|PubMed:16857685}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 11231151; 20439776; 21177967; 22560298; 23800452; 25487147; 29348603; |
Motif | MOTIF 70..74; /note=Secondary area of contact; /evidence=ECO:0000305 |
Gene Encoded By | |
Mass | 15,697 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |