Q6LEM5 · BNP1_BOTJA

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).

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)

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

AspectTerm
Cellular Componentcytosol
Cellular Componentextracellular region
Molecular Functionhormone activity
Molecular Functionpeptidyl-dipeptidase inhibitor activity
Molecular Functiontoxin activity
Biological Processblood vessel diameter maintenance
Biological Processnegative regulation of protein kinase activity
Biological Processregulation of blood pressure
Biological Processvasodilation

Keywords

Names & Taxonomy

Protein names

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Viperidae > Crotalinae > Bothrops

Accessions

  • Primary accession
    Q6LEM5
  • Secondary accessions
    • P01020
    • P30421
    • P68516

Subcellular Location

Secreted
Note: BPP-10c is internalized in the cytosol of prey cells.

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis34Low decrease in ability to enhance AsS activity.
Mutagenesis36Low decrease in ability to enhance AsS activity.
Mutagenesis38Low decrease in ability to enhance AsS activity.
Mutagenesis39Important decrease in ability to enhance AsS activity.
Mutagenesis40Important decrease in ability to enhance AsS activity.

PTM/Processing

Features

Showing features for signal, propeptide, modified residue, peptide, disulfide bond.

TypeIDPosition(s)Description
Signal1-23
PropeptidePRO_000025205024-30
Modified residue31Pyrrolidone carboxylic acid
PeptidePRO_000029202931-36Bradykinin-potentiating peptide 6a
PeptidePRO_000025205131-40Bradykinin-potentiating peptide 10a
PropeptidePRO_000025205241-43
Modified residue44Pyrrolidone carboxylic acid
PeptidePRO_000042296144-60Bradykinin-potentiating peptide 13a+QQWA
Modified residue45Pyrrolidone carboxylic acid
PeptidePRO_000042296245-60Bradykinin-potentiating peptide 13a+QWA
Modified residue48Pyrrolidone carboxylic acid
PeptidePRO_000025205348-60Bradykinin-potentiating peptide 13a
PropeptidePRO_000025205461-63
Modified residue64Pyrrolidone carboxylic acid
PeptidePRO_000042296364-77Bradykinin-potentiating peptide 10c+QQWA
Modified residue68Pyrrolidone carboxylic acid
PeptidePRO_000029203068-73Bradykinin-potentiating peptide 10c-F
PeptidePRO_000025205568-77Bradykinin-potentiating peptide 10c
PropeptidePRO_000025205678-84
Modified residue85Pyrrolidone carboxylic acid
PeptidePRO_000025205785-95Bradykinin-potentiating peptide 11b
PropeptidePRO_000025205896-102
Modified residue103Pyrrolidone carboxylic acid
PeptidePRO_0000252059103-113Bradykinin-potentiating peptide IIb
PropeptidePRO_0000252060114-116
Modified residue117Pyrrolidone carboxylic acid
PeptidePRO_0000252061117-121Bradykinin-potentiating peptide 5a
PropeptidePRO_0000252062122
Modified residue123Pyrrolidone carboxylic acid
PeptidePRO_0000252063123-127Bradykinin-potentiating peptide 5a
PropeptidePRO_0000252064128-207
PeptidePRO_0000421887208-225Poly-His-poly-Gly peptide 1
PropeptidePRO_0000421888226-234
PeptidePRO_0000252065235-256C-type natriuretic peptide
Disulfide bond240↔256

Keywords

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.

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region149-199Disordered

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    256
  • Mass (Da)
    26,814
  • Last updated
    2004-07-05 v1
  • Checksum
    85DBDBA0A9520A45
MVLSRLAASGLLLLALLALSVDGKPVQQWAQSWPGPNIPPLKVQQWAQGGWPRPGPEIPPLTVQQWAQNWPHPQIPPLTVQQWAQGRAPGPPIPPLTVQQWAQGRAPHPPIPPAPLQKWAPLQKWAPLLQPHESPASGTTALREELSLGPEAASGVPSAGAEVGRSGSKAPAAPHRLSKSKGAAATRPMRDLRPDGKQARQNWGRMAHHDHHAAAGGGGGGGGGARRLKGLAKKGAAKGCFGLKLDRIGTMSGLGC

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

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D85843
EMBL· GenBank· DDBJ
BAA12879.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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