IED ID | IndEnz0002019038 |
Enzyme Type ID | protease019038 |
Protein Name |
Bradykinin potentiating and C-type natriuretic peptides BPP-CNP Cleaved into: Bradykinin-potentiating peptide 10c BPP-10c BPP-2 Bradykinin-potentiating peptide-1 BPP-1 ; Bradykinin-potentiating peptide-2 BPP-2 ; Bradykinin inhibitor peptide homolog; C-type natriuretic peptide CNP |
Gene Name | |
Organism | Sistrurus catenatus edwardsii (Desert massasauga) (Crotalophorus edwardsii) |
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) Sistrurus Sistrurus catenatus (massasauga) Sistrurus catenatus edwardsii (Desert massasauga) (Crotalophorus edwardsii) |
Enzyme Sequence | MFVSRLAASGLLLLALLAVSLDGKPVQQWSQNWPGPKVPPLVVQQWSQNWPHPQIPPLVVQNWKSPTQLQPRESPAGGTTALREELSLGPDAALDTPPAGPDVGPRGSKAAAAPQRLSKSKGASATSTASRPMRDLRTDGKQARQNWGRMLNPDHHSAPGGGGGGGGGGARRLKGLAKKRAGSGCFGLKLDRIGSMSGLGC |
Enzyme Length | 201 |
Uniprot Accession Number | B0VXV8 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: [Bradykinin-potentiating peptide 10c]: Inhibits the activity of the angiotensin-converting enzyme (ACE) by a preferential interaction with its C-domain. May also potentiate the hypotensive effects of bradykinin. {ECO:0000269|PubMed:11994001}.; FUNCTION: [Bradykinin inhibitor peptide homolog]: Antagonizes the vasodilatory actions of bradykinin at the B2 bradykinin receptor. {ECO:0000250}.; FUNCTION: [C-type natriuretic peptide]: 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 (1); Disulfide bond (1); Modified residue (2); Peptide (4); Propeptide (4); 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 48; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250; MOD_RES 61; /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 | 20,896 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |