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Protein

Bradykinin-potentiating and C-type natriuretic peptides

Gene
N/A
Organism
Gloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Blomhotin: inhibits the rabbit lung angiotensin-converting enzyme (ACE) with an IC50 of 15 µM.
Bradykinin-potentiating peptide A: causes no contraction of the rat gastric fundus smooth muscle even at high concentrations.
Bradykinin-potentiating peptide B: inhibits the activity of the angiotensin-converting enzyme (ACE) by a preferential interaction with its C-domain. Also potentiates the hypotensive effects of bradykinin. Inhibits the rabbit lung ACE with an IC50 of 1.1 µM.
Bradykinin-potentiating peptide C: inhibits the activity of the angiotensin-converting enzyme (ACE) by interacting with the same potency to its C- and N-domains (PubMed:11994001). Inhibits the rabbit lung angiotensin-converting enzyme (ACE) with an IC50 of 7.1 µM.1 Publication
Leu3-blomhotin: inhibits the rabbit lung angiotensin-converting enzyme (ACE) with an IC50 of 46 µM. Synthetic Leu3-blomhotin contracts the rat gastric fundus smooth muscle in a rapid and transient manner.
Bradykinin-potentiating peptide Ahb1: potentiates the bradykinin in vivo.
Bradykinin-potentiating peptide Ahb2: does not show any bradykinin-potentiating effects.
C-type natriuretic peptide: exhibits hypotensive and vasodepressor activity. Acts by activating natriuretic receptors (NPR1 and/or NPR2 and/or NPR3) (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hypotensive agent, Metalloenzyme inhibitor, Metalloprotease inhibitor, Protease inhibitor, Toxin, Vasoactive, Vasodilator

Names & Taxonomyi

Protein namesi
Recommended name:
Bradykinin-potentiating and C-type natriuretic peptides
Alternative name(s):
Angiotensin-converting enzyme inhibitor
BPP-CNP homolog
Cleaved into the following 9 chains:
Alternative name(s):
Potentiator A
Alternative name(s):
Potentiator D
Alternative name(s):
Potentiator B
Alternative name(s):
Potentiator C
Alternative name(s):
Potentiator E
OrganismiGloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi)
Taxonomic identifieri242054 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeGloydius

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
PropeptideiPRO_000033417224 – 30Sequence analysis7
PeptideiPRO_500004930431 – 41BlomhotinAdd BLAST11
PeptideiPRO_500004930331 – 40Bradykinin-potentiating peptide A10
PropeptideiPRO_000033417342 – 48Sequence analysis7
PeptideiPRO_500004930549 – 59Leu3-blomhotinAdd BLAST11
PropeptideiPRO_000033417460 – 66Sequence analysis7
PeptideiPRO_500004930667 – 77Bradykinin-potentiating peptide CAdd BLAST11
PropeptideiPRO_000033417578 – 84Sequence analysis7
PeptideiPRO_500004930785 – 95Bradykinin-potentiating peptide BAdd BLAST11
PropeptideiPRO_000033417696 – 102Sequence analysis7
PeptideiPRO_5000049308103 – 113Bradykinin-potentiating peptide BAdd BLAST11
PropeptideiPRO_0000334177114 – 116Sequence analysis3
PeptideiPRO_5000049309117 – 127Bradykinin-potentiating peptide EBy similarityAdd BLAST11
PeptideiPRO_0000342453117 – 121Bradykinin-potentiating peptide Ahb1By similarity5
PropeptideiPRO_0000334178128 – 239Sequence analysisAdd BLAST112
PeptideiPRO_0000342454131 – 136Bradykinin-potentiating peptide Ahb2By similarity6
PeptideiPRO_5000049310242 – 263C-type natriuretic peptideAdd BLAST22

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei31Pyrrolidone carboxylic acid2 Publications1
Modified residuei49Pyrrolidone carboxylic acid1 Publication1
Modified residuei67Pyrrolidone carboxylic acid1 Publication1
Modified residuei85Pyrrolidone carboxylic acid1 Publication1
Modified residuei103Pyrrolidone carboxylic acid1 Publication1
Modified residuei117Pyrrolidone carboxylic acidBy similarity1
Disulfide bondi247 ↔ 263By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Pyrrolidone carboxylic acid

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Protein-protein interaction databases

IntActiP01021. 1 interactor.
MINTiMINT-8400351.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4AA2X-ray1.99P104-113[»]
4APJX-ray2.60P104-113[»]
SMRiP01021.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi34 – 136Pro-richAdd BLAST103
Compositional biasi226 – 231Poly-Gly6

Sequence similaritiesi

In the N-terminal section; belongs to the bradykinin-potentiating peptide family.Curated
In the C-terminal section; belongs to the natriuretic peptide family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

HOVERGENiHBG073115.

Family and domain databases

InterProiIPR000663. Natr_peptide.
IPR030480. Natr_peptide_CS.
[Graphical view]
PfamiPF00212. ANP. 1 hit.
[Graphical view]
PRINTSiPR00710. NATPEPTIDES.
SMARTiSM00183. NAT_PEP. 1 hit.
[Graphical view]
PROSITEiPS00263. NATRIURETIC_PEPTIDE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01021-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFVSRLAASG LLLLALMALS LDGKPVQQWS QGRPPGPPIP RLVVQQWSQG
60 70 80 90 100
LPPGPPIPRL VVQQWSQGLP PGPPIPPLVV QQWSQGLPPR PKIPPLVVQQ
110 120 130 140 150
WSQGLPPRPK IPPLVVQKWD PPPVSPPLLL QPHESPAGGT TALREELSLG
160 170 180 190 200
PEAASGPAAA GADGGRSGSK APAALHRLSK SKGASATSAS ASRPMRDLRT
210 220 230 240 250
DGKQARQNWA RMVNPDHHAV GGCCCGGGGG GARRLKGLVK KGVAKGCFGL
260
KLDRIGTMSG LGC
Length:263
Mass (Da):27,339
Last modified:May 20, 2008 - v4
Checksum:i407BA9A572BF5FC8
GO

Mass spectrometryi

Molecular mass is 1073.3 Da from positions 49 - 59. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020810 mRNA. Translation: BAA36953.1.
PIRiA01254. XASNBA.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020810 mRNA. Translation: BAA36953.1.
PIRiA01254. XASNBA.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4AA2X-ray1.99P104-113[»]
4APJX-ray2.60P104-113[»]
SMRiP01021.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP01021. 1 interactor.
MINTiMINT-8400351.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG073115.

Family and domain databases

InterProiIPR000663. Natr_peptide.
IPR030480. Natr_peptide_CS.
[Graphical view]
PfamiPF00212. ANP. 1 hit.
[Graphical view]
PRINTSiPR00710. NATPEPTIDES.
SMARTiSM00183. NAT_PEP. 1 hit.
[Graphical view]
PROSITEiPS00263. NATRIURETIC_PEPTIDE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBNP_GLOBL
AccessioniPrimary (citable) accession number: P01021
Secondary accession number(s): Q9PT52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 20, 2008
Last modified: November 2, 2016
This is version 67 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.