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P01021 (BNP_GLOBL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Bradykinin-potentiating and C-type natriuretic peptides
Alternative name(s):
Angiotensin-converting enzyme inhibitor
BPP-CNP homolog

Cleaved into the following 9 chains:

  1. Blomhotin
  2. Bradykinin-potentiating peptide A
    Short name=BPP-a
    Alternative name(s):
    Potentiator A
  3. Leu3-blomhotin
    Alternative name(s):
    Potentiator D
  4. Bradykinin-potentiating peptide B
    Short name=BPP-b
    Alternative name(s):
    Potentiator B
  5. Bradykinin-potentiating peptide C
    Short name=BPP-c
    Alternative name(s):
    Potentiator C
  6. Bradykinin-potentiating peptide E
    Short name=BPP-e
    Alternative name(s):
    Potentiator E
  7. Bradykinin-potentiating peptide Ahb1
    Short name=BPP-Ahb1
  8. Bradykinin-potentiating peptide Ahb2
    Short name=BPP-Ahb2
  9. C-type natriuretic peptide
OrganismGloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi)
Taxonomic identifier242054 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Gloydius

Protein attributes

Sequence length263 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Blomhotin: inhibits the rabbit lung angiotensin-converting enzyme (ACE) with an IC50 of 15 µM. Ref.6 Ref.8

Bradykinin-potentiating peptide A: causes no contraction of the rat gastric fundus smooth muscle even at high concentrations. Ref.6 Ref.8

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. Ref.6 Ref.8

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 (Ref.7). Inhibits the rabbit lung angiotensin-converting enzyme (ACE) with an IC50 of 7.1 µM. Ref.6 Ref.8

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. Ref.6 Ref.8

Bradykinin-potentiating peptide Ahb1: potentiates the bradykinin in vivo. Ref.6 Ref.8

Bradykinin-potentiating peptide Ahb2: does not show any bradykinin-potentiating effects. Ref.6 Ref.8

C-type natriuretic peptide: exhibits hypotensive and vasodepressor activity. Acts by activating natriuretic receptors (NPR1 and/or NPR2 and/or NPR3) By similarity. Ref.6 Ref.8

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

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

In the C-terminal section; belongs to the natriuretic peptide family.

Mass spectrometry

Molecular mass is 1073.3 Da from positions 49 - 59. Determined by ESI. Ref.6

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Propeptide24 – 307 Potential
PRO_0000334172
Peptide31 – 4111Blomhotin Ref.2
PRO_5000049304
Peptide31 – 4010Bradykinin-potentiating peptide A Ref.3
PRO_5000049303
Propeptide42 – 487 Potential
PRO_0000334173
Peptide49 – 5911Leu3-blomhotin
PRO_5000049305
Propeptide60 – 667 Potential
PRO_0000334174
Peptide67 – 7711Bradykinin-potentiating peptide C Ref.4
PRO_5000049306
Propeptide78 – 847 Potential
PRO_0000334175
Peptide85 – 9511Bradykinin-potentiating peptide B Ref.5
PRO_5000049307
Propeptide96 – 1027 Potential
PRO_0000334176
Peptide103 – 11311Bradykinin-potentiating peptide B
PRO_5000049308
Propeptide114 – 1163 Potential
PRO_0000334177
Peptide117 – 12711Bradykinin-potentiating peptide E By similarity
PRO_5000049309
Peptide117 – 1215Bradykinin-potentiating peptide Ahb1 By similarity
PRO_0000342453
Propeptide128 – 239112 Potential
PRO_0000334178
Peptide131 – 1366Bradykinin-potentiating peptide Ahb2 By similarity
PRO_0000342454
Peptide242 – 26322C-type natriuretic peptide
PRO_5000049310

Regions

Compositional bias34 – 136103Pro-rich
Compositional bias226 – 2316Poly-Gly

Amino acid modifications

Modified residue311Pyrrolidone carboxylic acid
Modified residue491Pyrrolidone carboxylic acid
Modified residue671Pyrrolidone carboxylic acid
Modified residue851Pyrrolidone carboxylic acid
Modified residue1031Pyrrolidone carboxylic acid
Modified residue1171Pyrrolidone carboxylic acid By similarity
Disulfide bond247 ↔ 263 By similarity

Sequences

Sequence LengthMass (Da)Tools
P01021 [UniParc].

Last modified May 20, 2008. Version 4.
Checksum: 407BA9A572BF5FC8

FASTA26327,339
        10         20         30         40         50         60 
MFVSRLAASG LLLLALMALS LDGKPVQQWS QGRPPGPPIP RLVVQQWSQG LPPGPPIPRL 

        70         80         90        100        110        120 
VVQQWSQGLP PGPPIPPLVV QQWSQGLPPR PKIPPLVVQQ WSQGLPPRPK IPPLVVQKWD 

       130        140        150        160        170        180 
PPPVSPPLLL QPHESPAGGT TALREELSLG PEAASGPAAA GADGGRSGSK APAALHRLSK 

       190        200        210        220        230        240 
SKGASATSAS ASRPMRDLRT DGKQARQNWA RMVNPDHHAV GGCCCGGGGG GARRLKGLVK 

       250        260 
KGVAKGCFGL KLDRIGTMSG LGC

« Hide

References

[1]"Bradykinin-potentiating peptides and C-type natriuretic peptides from snake venom."
Higuchi S., Murayama N., Saguchi K., Ohi H., Fujita Y., de Camargo A.C.M., Ogawa T., Deshimaru M., Ohno M.
Immunopharmacology 44:129-135(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.
[2]"Blomhotin: a novel peptide with smooth muscle contractile activity identified in the venom of Agkistrodon halys blomhoffii."
Yanoshita R., Kasuga A., Inoue S., Ikeda K., Samejima Y.
Toxicon 37:1761-1770(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 31-41, PYROGLUTAMATE FORMATION AT GLN-31.
Tissue: Venom.
[3]"Structure of potentiator A, one of the five bradykinin potentiating peptides from the venom of Agkistrodon halys blomhoffii."
Kato H., Suzuki T., Okada K., Kimura T., Sakakibara S.
Experientia 29:574-575(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 31-40, PYROGLUTAMATE FORMATION AT GLN-31.
Tissue: Venom.
[4]"Bradykinin-potentiating peptides from the venom of Agkistrodon halys blomhoffi. Isolation of five bradykinin potentiators and the amino acid sequences of two of them, potentiators B and C."
Kato H., Suzuki T.
Biochemistry 10:972-980(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 67-77, PYROGLUTAMATE FORMATION AT GLN-67.
Tissue: Venom.
[5]"Amino acid sequence of bradykinin-potentiating peptide isolated from the venom of Agkistrodon halys blomhoffii."
Kato H., Suzuki T.
Proc. Jpn. Acad., B, Phys. Biol. Sci. 46:176-181(1970)
Cited for: PROTEIN SEQUENCE OF 85-95 AND 103-113, PYROGLUTAMATE FORMATION AT GLN-85 AND GLN-103.
Tissue: Venom.
[6]"cDNA cloning of bradykinin-potentiating peptides-C-type natriuretic peptide precursor, and characterization of the novel peptide Leu3-blomhotin from the venom of Agkistrodon blomhoffi."
Murayama N., Michel G.H., Yanoshita R., Samejima Y., Saguchi K., Ohi H., Fujita Y., Higuchi S.
Eur. J. Biochem. 267:4075-4080(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS OF 31-40 AND 49-59 (BPP-A AND LEU3-BLOMHOTIN), FUNCTION, PYROGLUTAMATE FORMATION AT GLN-49, MASS SPECTROMETRY.
Tissue: Venom.
[7]"Selective inhibition of the C-domain of angiotensin I converting enzyme by bradykinin potentiating peptides."
Cotton J., Hayashi M.A., Cuniasse P., Vazeux G., Ianzer D., De Camargo A.C., Dive V.
Biochemistry 41:6065-6071(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS OF 67-77; 85-95 AND 103-113 (BPP-B AND BPP-C).
[8]"Identification of novel bradykinin-potentiating peptides (BPPs) in the venom gland of a rattlesnake allowed the evaluation of the structure-function relationship of BPPs."
Gomes C.L., Konno K., Conceicao I.M., Ianzer D., Yamanouye N., Prezoto B.C., Assakura M.T., Radis-Baptista G., Yamane T., Santos R.A., de Camargo A.C.M., Hayashi M.A.F.
Biochem. Pharmacol. 74:1350-1360(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS OF 117-121 AND 131-136 (BPP-AHB1 AND BPP-AHB2), FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB020810 mRNA. Translation: BAA36953.1.
PIRXASNBA. A01254.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4AA2X-ray1.99P86-95[»]
4APJX-ray2.60P86-95[»]
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG073115.

Family and domain databases

InterProIPR000663. Natr_peptide.
[Graphical view]
PfamPF00212. ANP. 1 hit.
[Graphical view]
PRINTSPR00710. NATPEPTIDES.
SMARTSM00183. NAT_PEP. 1 hit.
[Graphical view]
PROSITEPS00263. NATRIURETIC_PEPTIDE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBNP_GLOBL
AccessionPrimary (citable) accession number: P01021
Secondary accession number(s): Q9PT52
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 20, 2008
Last modified: May 1, 2013
This is version 56 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents