| IED ID | IndEnz0002018626 |
| Enzyme Type ID | protease018626 |
| Protein Name |
Bradykinin-potentiating and C-type natriuretic peptides Brain BPP-CNP bBPP-CNP Evasin-CNP Cleaved into: Bradykinin-potentiating peptide 13a+QQWA BPP-13a+QQWA ; Bradykinin-potentiating peptide 13a+QWA BPP-13a+QWA ; Bradykinin-potentiating peptide 13a BPP-13a ; Bradykinin-potentiating peptide 10c+QQWA BPP-10c+QQWA ; Bradykinin-potentiating peptide 10c BPP-10c BPP-2 Evasin-10c ; Bradykinin-potentiating peptide 12b BPP-12b Evasin-12b ; Bradykinin-potentiating peptide AP; Bradykinin-potentiating peptide APL BPP-APL ; Bradykinin-potentiating peptide 11e BPP-11e Evasin-11e ; Bradykinin-potentiating peptide 5a BPP-5a Bradykinin-potentiating peptide Va BPPVa Evasin-5a Proline-rich peptide 5a Bj-PRO-5a PRO-5a ; Poly-His-poly-Gly peptide 1 pHpG-1 ; C-type natriuretic peptide Bj-CNP |
| Gene Name | |
| Organism | Bothrops jararaca (Jararaca) (Bothrops jajaraca) |
| 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) Bothrops Bothrops jararaca (Jararaca) (Bothrops jajaraca) |
| Enzyme Sequence | MVLSRLAASGLLLLALLALSVDGKPVQQWAQGGWPRPGPEIPPLKVQQWAQGGWPRPGPEIPPLTVQQWAQNWPHPQIPPLTVQQWAQWGRPPGPPIPPLTVQQWAQARPPHPPIPPAPLQKWAPVQKWAPLLQPHESPASGTTALREELSLGPEAASGVPSAGAEVGRSGSKAPAAPHRLSKSKGAAATSAASRPMRDLRPDGKQARQNWGRMVHHDHHAAVGGGGGGGGGGARRLKGLAKKGAAKGCFGLKVDRIGTMSGLGC |
| Enzyme Length | 265 |
| Uniprot Accession Number | Q9PW56 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: [Bradykinin-potentiating peptide 5a]: Modestly inhibits ACE (with highest affinity for the N-site) and reveals strong bradykinin-potentiating activity. Induces nitric oxide (NO) production depended on muscarinic acetylcholine receptor M1 subtype (CHRM1) and bradykinin B2 receptor (BDKRB2) activation. Both these receptors contribute to the vasodilation induced by this peptide that may have an indirect action on BDKRB2 and a direct agonistic action on CHRM1.; FUNCTION: [Bradykinin-potentiating peptide 10c]: Peptide with several activities. It inhibits the activity of the angiotensin-converting enzyme (ACE) by a preferential interaction with its C-domain (PubMed:11994001). It evokes transient hypotension (-14 mmHg) similar to that evoked by 0,5 ug of bradykinin, when injected alone into rats. It has a high bradykinin-potentiating effect (120%), when 60 nmol of BPP-10c are coinjected with 0.5 ug of bradykinin into rats (PubMed:22869554). Does not affect angiotensin-1 pressor effects. Shows potent and long-lasting antihypertensive activity as well as a reduction of the heart rate (PubMed:17475904). It also binds and dose-dependently promotes the activation of cytosolic argininosuccinate synthase (ASS1), an enzyme that catalyzes the conversion of citrulline, L-aspartate and ATP to argininosuccinate, AMP and pyrophosphate. It also enhances ASS1-dependent arginine production in HEK 293 cells, as well as in spontaneous hypertensive rat (SHR) and Wistar rat plasma. In addition, it induces the production of nitric-oxide (NO) by HUVEC cells via the endothelial nitric-oxide synthase (NOS3), which use arginine as a substrate and produce NO. It has been shown to be internalized by ASS1-expressing endothelial (HUVEC) and kidney (HEK 293) cells, and is detected homogenously distributed within the cell cytoplasm for up to 2 hours (PubMed:19491403). {ECO:0000269|PubMed:11994001, ECO:0000269|PubMed:17475904, ECO:0000269|PubMed:19491403, ECO:0000269|PubMed:22869554}.; FUNCTION: [Poly-His-poly-Gly peptide 1]: May serve as a metalloproteinase inhibitor during glandular storage. Their inhibition may be instantly disengaged, by dilution or physiochemical change, when venom is injected into tissue of the victim. {ECO:0000250|UniProtKB:A8YPR6}.; FUNCTION: Natriuretic peptide exhibits natriuretic and vasodepressor activity. Acts by stimulating cGMP. {ECO:0000305}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Disulfide bond (1); Modified residue (12); Mutagenesis (5); Peptide (16); Propeptide (9); Region (1); Signal peptide (1) |
| Keywords | Cleavage on pair of basic residues;Cytoplasm;Direct protein sequencing;Disulfide bond;G-protein coupled receptor impairing toxin;Hypotensive agent;Metalloenzyme inhibitor;Metalloprotease inhibitor;Protease inhibitor;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin;Vasoactive;Vasodilator |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. Cytoplasm, cytosol. Note=BPP-10c is internalized in the cytosol of prey cells. |
| Modified Residue | MOD_RES 27; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:20146532"; MOD_RES 28; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:20146532"; MOD_RES 31; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:15245866, ECO:0000269|PubMed:20146532, ECO:0000269|PubMed:22869554"; MOD_RES 47; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:20146532"; MOD_RES 48; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:20146532"; MOD_RES 51; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:15245866, ECO:0000269|PubMed:20146532, ECO:0000269|PubMed:22869554"; MOD_RES 67; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:20146532"; MOD_RES 71; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:15245866, ECO:0000269|PubMed:22869554"; MOD_RES 88; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:15245866, ECO:0000269|PubMed:22869554"; MOD_RES 107; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:15245866, ECO:0000269|PubMed:20146532, ECO:0000269|PubMed:22869554"; MOD_RES 121; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:15245866"; MOD_RES 127; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:15245866" |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 27,763 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |