Q6LEM5 · BNP1_BOTJA
- ProteinBradykinin-potentiating and C-type natriuretic peptides
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids256 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
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).
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).
Bradykinin-potentiating peptide 10c-F
Has much lower activity than the full-length bradykinin-potentiating peptides.
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.
C-type natriuretic peptide
has a vasorelaxant activity in rat aortic strips and a diuretic potency in anesthetized rats (By similarity).
May act by activating natriuretic receptors (NPR1 and/or NPR2)
May act by activating natriuretic receptors (NPR1 and/or NPR2)
Miscellaneous
Negative results: does not bind to type-1 angiotensin-2 receptor (AGTR1).
Bradykinin-potentiating peptide 10c-F is present only in female snakes.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | extracellular region | |
Molecular Function | hormone activity | |
Molecular Function | peptidyl-dipeptidase inhibitor activity | |
Molecular Function | toxin activity | |
Biological Process | blood vessel diameter maintenance | |
Biological Process | negative regulation of protein kinase activity | |
Biological Process | regulation of blood pressure | |
Biological Process | vasodilation |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameBradykinin-potentiating and C-type natriuretic peptides
- Alternative names
- Cleaved into 13 chains
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Viperidae > Crotalinae > Bothrops
Accessions
- Primary accessionQ6LEM5
- Secondary accessions
Subcellular Location
UniProt Annotation
GO Annotation
Note: BPP-10c is internalized in the cytosol of prey cells.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 34 | Low decrease in ability to enhance AsS activity. | ||||
Sequence: P → A | ||||||
Mutagenesis | 36 | Low decrease in ability to enhance AsS activity. | ||||
Sequence: P → A | ||||||
Mutagenesis | 38 | Low decrease in ability to enhance AsS activity. | ||||
Sequence: I → A | ||||||
Mutagenesis | 39 | Important decrease in ability to enhance AsS activity. | ||||
Sequence: P → A | ||||||
Mutagenesis | 40 | Important decrease in ability to enhance AsS activity. | ||||
Sequence: P → A |
PTM/Processing
Features
Showing features for signal, propeptide, modified residue, peptide, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MVLSRLAASGLLLLALLALSVDG | ||||||
Propeptide | PRO_0000252050 | 24-30 | ||||
Sequence: KPVQQWA | ||||||
Modified residue | 31 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Peptide | PRO_0000292029 | 31-36 | Bradykinin-potentiating peptide 6a | |||
Sequence: QSWPGP | ||||||
Peptide | PRO_0000252051 | 31-40 | Bradykinin-potentiating peptide 10a | |||
Sequence: QSWPGPNIPP | ||||||
Propeptide | PRO_0000252052 | 41-43 | ||||
Sequence: LKV | ||||||
Modified residue | 44 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Peptide | PRO_0000422961 | 44-60 | Bradykinin-potentiating peptide 13a+QQWA | |||
Sequence: QQWAQGGWPRPGPEIPP | ||||||
Modified residue | 45 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Peptide | PRO_0000422962 | 45-60 | Bradykinin-potentiating peptide 13a+QWA | |||
Sequence: QWAQGGWPRPGPEIPP | ||||||
Modified residue | 48 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Peptide | PRO_0000252053 | 48-60 | Bradykinin-potentiating peptide 13a | |||
Sequence: QGGWPRPGPEIPP | ||||||
Propeptide | PRO_0000252054 | 61-63 | ||||
Sequence: LTV | ||||||
Modified residue | 64 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Peptide | PRO_0000422963 | 64-77 | Bradykinin-potentiating peptide 10c+QQWA | |||
Sequence: QQWAQNWPHPQIPP | ||||||
Modified residue | 68 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Peptide | PRO_0000292030 | 68-73 | Bradykinin-potentiating peptide 10c-F | |||
Sequence: QNWPHP | ||||||
Peptide | PRO_0000252055 | 68-77 | Bradykinin-potentiating peptide 10c | |||
Sequence: QNWPHPQIPP | ||||||
Propeptide | PRO_0000252056 | 78-84 | ||||
Sequence: LTVQQWA | ||||||
Modified residue | 85 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Peptide | PRO_0000252057 | 85-95 | Bradykinin-potentiating peptide 11b | |||
Sequence: QGRAPGPPIPP | ||||||
Propeptide | PRO_0000252058 | 96-102 | ||||
Sequence: LTVQQWA | ||||||
Modified residue | 103 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Peptide | PRO_0000252059 | 103-113 | Bradykinin-potentiating peptide IIb | |||
Sequence: QGRAPHPPIPP | ||||||
Propeptide | PRO_0000252060 | 114-116 | ||||
Sequence: APL | ||||||
Modified residue | 117 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Peptide | PRO_0000252061 | 117-121 | Bradykinin-potentiating peptide 5a | |||
Sequence: QKWAP | ||||||
Propeptide | PRO_0000252062 | 122 | ||||
Sequence: L | ||||||
Modified residue | 123 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Peptide | PRO_0000252063 | 123-127 | Bradykinin-potentiating peptide 5a | |||
Sequence: QKWAP | ||||||
Propeptide | PRO_0000252064 | 128-207 | ||||
Sequence: LLQPHESPASGTTALREELSLGPEAASGVPSAGAEVGRSGSKAPAAPHRLSKSKGAAATRPMRDLRPDGKQARQNWGRMA | ||||||
Peptide | PRO_0000421887 | 208-225 | Poly-His-poly-Gly peptide 1 | |||
Sequence: HHDHHAAAGGGGGGGGGA | ||||||
Propeptide | PRO_0000421888 | 226-234 | ||||
Sequence: RRLKGLAKK | ||||||
Peptide | PRO_0000252065 | 235-256 | C-type natriuretic peptide | |||
Sequence: GAAKGCFGLKLDRIGTMSGLGC | ||||||
Disulfide bond | 240↔256 | |||||
Sequence: CFGLKLDRIGTMSGLGC |
Keywords
- PTM
Expression
Tissue specificity
Expressed in venom gland.
Developmental stage
BPP-10a, BPP-10c+QQWA, BPP-13a, BPP-13+QWA and BPP-13A+QQWA seem to be found in both adult and newborn B.jararaca venoms.
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 149-199 | Disordered | ||||
Sequence: GPEAASGVPSAGAEVGRSGSKAPAAPHRLSKSKGAAATRPMRDLRPDGKQA |
Sequence similarities
In the N-terminal section; belongs to the bradykinin-potentiating peptide family.
In the central section; belongs to the pHpG family.
In the C-terminal section; belongs to the natriuretic peptide family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length256
- Mass (Da)26,814
- Last updated2004-07-05 v1
- Checksum85DBDBA0A9520A45
Mass Spectrometry
Bradykinin-potentiating peptide 5a
Molecular mass is 611.7 Da. Determined by Electrospray. BPP-5a.Bradykinin-potentiating peptide 6a
Molecular mass is 653.7 Da. Determined by Electrospray. BPP-6a.Bradykinin-potentiating peptide 10a
Molecular mass is 1,075.2 Da. Determined by Electrospray. BPP-10a.Bradykinin-potentiating peptide 10c
Molecular mass is 1,196.3 Da. Determined by Electrospray. BPP-10c.Bradykinin-potentiating peptide 10c
Molecular mass is 1,196.65 Da. Determined by MALDI. BPP-10c.Bradykinin-potentiating peptide 10c
Molecular mass is 1,195.6 Da. Determined by Electrospray.Bradykinin-potentiating peptide 10c-F
Molecular mass is 760.33 Da. Determined by MALDI. BPP-10c-F.Bradykinin-potentiating peptide 11b
Molecular mass is 1,069.2 Da. Determined by Electrospray. BPP-11b.Bradykinin-potentiating peptide 13a
Molecular mass is 1,370.76 Da. Determined by MALDI. BPP-13a.Bradykinin-potentiating peptide 13a
Molecular mass is 1,370.5 Da. Determined by Electrospray. BPP-13a.Keywords
- Technical term