| IED ID | IndEnz0002002421 |
| Enzyme Type ID | protease002421 |
| Protein Name |
Bradykinin-potentiating and C-type natriuretic peptides BPP-CNP Cleaved into: Bradykinin-potentiating peptide 6a BPP-6a ; Bradykinin-potentiating peptide 10a BPP-10a Bradykinin-potentiating peptide IV-1-A BPPIV-1-A Bradykinin-potentiating peptide V-8 ; 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 III-1-A III-1-A Bradykinin-potentiating peptide V-9 ; Bradykinin-potentiating peptide 10c+QQWA BPP-10c+QQWA ; Bradykinin-potentiating peptide 10c BPP-10c BPP-2 Bradykinin-potentiating peptide IV-1-Bbeta BPP IV-1-Bbeta Bradykinin-potentiating peptide V-7 ; Bradykinin-potentiating peptide 10c-F BPP-10c-F ; Bradykinin-potentiating peptide 11b BPP-11b Bradykinin-potentiating peptide IIa BPP-IIa ; Bradykinin-potentiating peptide IIb BPP-IIb ; Bradykinin-potentiating peptide 5a BPP-5a Bradykinin-potentiating peptide Va BPPVa 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 | MVLSRLAASGLLLLALLALSVDGKPVQQWAQSWPGPNIPPLKVQQWAQGGWPRPGPEIPPLTVQQWAQNWPHPQIPPLTVQQWAQGRAPGPPIPPLTVQQWAQGRAPHPPIPPAPLQKWAPLQKWAPLLQPHESPASGTTALREELSLGPEAASGVPSAGAEVGRSGSKAPAAPHRLSKSKGAAATRPMRDLRPDGKQARQNWGRMAHHDHHAAAGGGGGGGGGARRLKGLAKKGAAKGCFGLKLDRIGTMSGLGC |
| Enzyme Length | 256 |
| Uniprot Accession Number | Q6LEM5 |
| 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: [Bradykinin-potentiating peptide 10c-F]: Has much lower activity than the full-length bradykinin-potentiating peptides. {ECO:0000269|PubMed:17315274}.; 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: 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 | Disulfide bond (1); Modified residue (10); Mutagenesis (5); Peptide (14); 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 {ECO:0000269|PubMed:18200607}. Cytoplasm, cytosol. Note=BPP-10c is internalized in the cytosol of prey cells. |
| Modified Residue | MOD_RES 31; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:15245866, ECO:0000269|PubMed:20146532, ECO:0000269|PubMed:4334402"; MOD_RES 44; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:20146532"; MOD_RES 45; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:20146532"; MOD_RES 48; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:15245866, ECO:0000269|PubMed:15912471, ECO:0000269|PubMed:18200607, ECO:0000269|PubMed:20146532, ECO:0000269|PubMed:22869554, ECO:0000269|PubMed:4334402"; MOD_RES 64; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:20146532"; MOD_RES 68; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:15245866, ECO:0000269|PubMed:15912471, ECO:0000269|PubMed:17315274, ECO:0000269|PubMed:22869554, ECO:0000269|PubMed:4334402"; MOD_RES 85; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:15245866"; MOD_RES 103; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000305|PubMed:9037028"; MOD_RES 117; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:15245866"; MOD_RES 123; /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 | 26,814 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |