Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P01021

- BNP_GLOBL

UniProt

P01021 - BNP_GLOBL

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Bradykinin-potentiating and C-type natriuretic peptides

Gene
N/A
Organism
Gloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi)
Status
Reviewed - 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

  1. metalloendopeptidase inhibitor activity Source: UniProtKB-KW

GO - Biological processi

  1. regulation of blood pressure Source: UniProtKB-KW
  2. vasodilation Source: UniProtKB-KW
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

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Propeptidei24 – 307Sequence AnalysisPRO_0000334172
Peptidei31 – 4111BlomhotinPRO_5000049304Add
BLAST
Peptidei31 – 4010Bradykinin-potentiating peptide APRO_5000049303
Propeptidei42 – 487Sequence AnalysisPRO_0000334173
Peptidei49 – 5911Leu3-blomhotinPRO_5000049305Add
BLAST
Propeptidei60 – 667Sequence AnalysisPRO_0000334174
Peptidei67 – 7711Bradykinin-potentiating peptide CPRO_5000049306Add
BLAST
Propeptidei78 – 847Sequence AnalysisPRO_0000334175
Peptidei85 – 9511Bradykinin-potentiating peptide BPRO_5000049307Add
BLAST
Propeptidei96 – 1027Sequence AnalysisPRO_0000334176
Peptidei103 – 11311Bradykinin-potentiating peptide BPRO_5000049308Add
BLAST
Propeptidei114 – 1163Sequence AnalysisPRO_0000334177
Peptidei117 – 12711Bradykinin-potentiating peptide EBy similarityPRO_5000049309Add
BLAST
Peptidei117 – 1215Bradykinin-potentiating peptide Ahb1By similarityPRO_0000342453
Propeptidei128 – 239112Sequence AnalysisPRO_0000334178Add
BLAST
Peptidei131 – 1366Bradykinin-potentiating peptide Ahb2By similarityPRO_0000342454
Peptidei242 – 26322C-type natriuretic peptidePRO_5000049310Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311Pyrrolidone carboxylic acid2 Publications
Modified residuei49 – 491Pyrrolidone carboxylic acid1 Publication
Modified residuei67 – 671Pyrrolidone carboxylic acid1 Publication
Modified residuei85 – 851Pyrrolidone carboxylic acid1 Publication
Modified residuei103 – 1031Pyrrolidone carboxylic acid1 Publication
Modified residuei117 – 1171Pyrrolidone carboxylic acidBy similarity
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 interaction.
MINTiMINT-8400351.

Structurei

3D structure databases

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

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi34 – 136103Pro-richAdd
BLAST
Compositional biasi226 – 2316Poly-Gly

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.
[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 .
PIRi A01254. XASNBA.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4AA2 X-ray 1.99 P 104-113 [» ]
4APJ X-ray 2.60 P 104-113 [» ]
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P01021. 1 interaction.
MINTi MINT-8400351.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG073115.

Family and domain databases

InterProi IPR000663. Natr_peptide.
[Graphical view ]
Pfami PF00212. ANP. 1 hit.
[Graphical view ]
PRINTSi PR00710. NATPEPTIDES.
SMARTi SM00183. NAT_PEP. 1 hit.
[Graphical view ]
PROSITEi PS00263. NATRIURETIC_PEPTIDE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

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: October 29, 2014
This is version 64 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin 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

External Data

Dasty 3