IED ID | IndEnz0002015688 |
Enzyme Type ID | protease015688 |
Protein Name |
Cystatin-C PoCystatin-C |
Gene Name | |
Organism | Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Actinopterygii Actinopteri Neopterygii Teleostei Osteoglossocephalai Clupeocephala Euteleosteomorpha Neoteleostei Eurypterygia Ctenosquamata Acanthomorphata Euacanthomorphacea Percomorphaceae Carangaria Pleuronectiformes (flatfishes) Pleuronectoidei Paralichthyidae (large-tooth flounders) Paralichthys Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus) |
Enzyme Sequence | MKMLVFPVLAALFAVGLGNLVGAPRDINISEAQDALDFAVAKHNSGTNDMFLRQVAEVVRVQRQVVSGNKYIITVKMAKTPCRKDRVVNEVCEIHKDPALAQPYECTFSVWSRPWIPDLQLVGEKC |
Enzyme Length | 126 |
Uniprot Accession Number | B2Z450 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Thiol protease inhibitor. Has high papain inhibitory activity and inhibits to a lesser extent fish cathepsins L, S, K, F, X and bovine cathepsin B in vitro. {ECO:0000269|PubMed:23649306}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Stable between 20-40 degrees Celsius. {ECO:0000269|PubMed:23649306}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5-6 and pH 6-8 for papain and bovine cathepsin B, respectively. {ECO:0000269|PubMed:23649306}; |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Disulfide bond (2); Domain (1); Motif (1); Signal peptide (1); Site (1) |
Keywords | Disulfide bond;Protease inhibitor;Secreted;Signal;Thiol protease inhibitor |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q98967}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | MOTIF 64..68; /note=Secondary area of contact; /evidence=ECO:0000250|UniProtKB:P04080 |
Gene Encoded By | |
Mass | 14,027 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |