| Primary information |
|---|
| ID | 13492 |
| Uniprot ID | Q27J49 |
| Description | Bradykinin-potentiating and C-type natriuretic peptides (BPP-CNP) [Cleaved into- Bradykinin-potentiating peptide 1 (BPP 1); Bradykinin-potentiating peptide 2 (BPP 2); Bradykinin-potentiating peptide 3 (BPP 3); Bradykinin-potentiating peptide 4 (BPP 4); Bradykinin-potentiating peptide 5 (BPP 5); Brad |
| Organism | Lachesis muta muta |
| Txonomy | 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); Lachesis; Lachesis muta (South American bushmaster); La |
| Subcellular Location | Secreted |
| Developmental Stage | NA |
| Similarity | In the N-terminal section; belongs to the bradykinin-potentiating peptide family. |
| Tissue Specificity | Expressed by the venom gland. |
| Post Translational Modification | NA |
| 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. |
| Length | 239 |
| Molecular Weight | 25 |
| Name | NA |
| Sequence | NA |
| Sequence map | NA |
| PDB ID | NA |
| Drugpedia | NA |
| Receptor | NA |
| Domain | NA |
| Pharmaceutical Use | NA
|