| IED ID | IndEnz0002019039 | 
| Enzyme Type ID | protease019039 | 
| Protein Name | 
                        
                            
                                Bradykinin-potentiating and C-type natriuretic peptides  BPP-CNP Cleaved into: Bradykinin-potentiating peptide Tg1 BPP ; C-type natriuretic peptide CNP  | 
                    
| Gene Name | |
| Organism | Trimeresurus gramineus (Bamboo pit viper) (Indian green tree viper) | 
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Lepidosauria (lepidosaurs) Squamata (squamates) Bifurcata (split-tongued squamates) Unidentata Episquamata Toxicofera Serpentes (snakes) Colubroidea Viperidae Crotalinae (pit vipers) Trimeresurus Trimeresurus gramineus (Bamboo pit viper) (Indian green tree viper) | 
| Enzyme Sequence | MFVSRLAASGLLLLALLALSLDGKPVQEKPGRSPPISPLLVPPPPPPPHWPPPHHIPPLSVQKFPPGWKPTHPHHIPPLEVQQWSQGGPRSELVQPHESPAGGTTAFREELSLGPEAASGPAAPQRLPKRKGASATSAASRSMRDLRADGKQARQKWGRMVQPDHHAAPGGGGGGGGGARRLKGLAKKAVGKGCFGLPLDRIGSMSGMGC | 
| Enzyme Length | 210 | 
| Uniprot Accession Number | P0C7P6 | 
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Bradykinin-potentiating peptide both inhibits the activity of the angiotensin-converting enzyme (ACE) and enhances the action of bradykinin by inhibiting the peptidases that inactivate it. It acts as an indirect hypotensive agent (By similarity). Tg1 does not show bradykinin-potentiating effects. {ECO:0000250, ECO:0000269|PubMed:17714693}.; FUNCTION: Snake venom natriuretic peptide that exhibits hypotensive and vasodepressor activity. Acts by activating natriuretic receptors (NPR1 and/or NPR2 and/or NPR3) (By similarity). {ECO:0000250}. | 
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Compositional bias (2); Disulfide bond (1); Modified residue (1); Peptide (2); Propeptide (2); Region (1); Signal peptide (1) | 
| Keywords | Cleavage on pair of basic residues;Disulfide bond;Hypotensive agent;Metalloenzyme inhibitor;Metalloprotease inhibitor;Protease inhibitor;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin;Vasoactive;Vasodilator | 
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | 
| Modified Residue | MOD_RES 27; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250 | 
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 | 
| Structure 3D | |
| Cross Reference PDB | - | 
| Mapped Pubmed ID | - | 
| Motif | |
| Gene Encoded By | |
| Mass | 21,905 | 
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |