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Entry version 76 (02 Jun 2021)
Sequence version 4 (20 May 2008)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

inhibits the rabbit lung angiotensin-converting enzyme (ACE) (IC50=15 µM) (PubMed:10866809).

Contracts the rat gastric fundus smooth muscle in a rapid and transient manner (PubMed:10519653, PubMed:10866809).

2 Publications

causes no contraction of the rat gastric fundus smooth muscle even at high concentrations. Causes very weak contraction of the isolated guinea pig ileum (PubMed:4323853).

Causes weak contraction on rat uterus (PubMed:4323853).

1 Publication

inhibits the activity of the angiotensin-converting enzyme (ACE) by a preferential interaction with its C-domain (Ki=30 nM, IC50=1.1 µM) (PubMed:10866809, PubMed:11994001, PubMed:23082758).

It binds ACE in a zinc-independent manner (PubMed:23056909).

Also potentiates the hypotensive effects of bradykinin. Causes high contraction of the isolated guinea pig ileum and weak contraction on rat uterus (PubMed:4323853).

4 Publications

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) (IC50=7.1 µM) (PubMed:10866809).

Causes weak contraction of the isolated guinea pig ileum (PubMed:4323853).

Causes weak contraction on rat uterus (PubMed:4323853).

3 Publications

inhibits the rabbit lung angiotensin-converting enzyme (ACE) (IC50=46 µM) (PubMed:10866809).

Synthetic Leu3-blomhotin contracts the rat gastric fundus smooth muscle in a rapid and transient manner (PubMed:10866809).

Causes moderate contraction of the isolated guinea pig ileum (PubMed:4323853).

Causes weak contraction on rat uterus (PubMed:4323853).

2 Publications

causes weak contraction of the isolated guinea pig ileum (PubMed:4323853).

Causes about 50-fold more potentiating activity on rat uterus than on guinea pig ileum (PubMed:4323853).

1 Publication

synthetic peptide potentiates the bradykinin in vivo.

1 Publication

synthetic peptide does not show any bradykinin-potentiating effects.

1 Publication

exhibits hypotensive and vasodepressor activity. Acts by activating natriuretic receptors (NPR1 and/or NPR2 and/or NPR3) (By similarity).

By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei86Angiotensin-converting enzyme binding active site; via amide nitrogen1 Publication1
Binding sitei104Angiotensin-converting enzyme binding active site; via amide nitrogen1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHypotensive agent, Metalloenzyme inhibitor, Metalloprotease inhibitor, Protease inhibitor, Toxin, Vasoactive, Vasodilator

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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:
Blomhotin2 Publications
Alternative name(s):
Potentiator A2 Publications
Leu3-blomhotin1 Publication
Alternative name(s):
Potentiator D1 Publication
Bradykinin-potentiating peptide B1 Publication
Short name:
BPP-b
Alternative name(s):
Potentiator B1 Publication
Alternative name(s):
Potentiator C1 Publication
Alternative name(s):
Potentiator E1 Publication
Bradykinin-potentiating peptide Ahb11 Publication
Short name:
BPP-Ahb11 Publication
Bradykinin-potentiating peptide Ahb21 Publication
Short name:
BPP-Ahb21 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiGloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri242054 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeGloydius

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Secreted

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 23Sequence analysisAdd BLAST23
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000033417224 – 30Sequence analysis7
<p>This subsection of the 'PTM / Processing' section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_500004930431 – 41Blomhotin1 PublicationAdd BLAST11
PeptideiPRO_500004930331 – 40Bradykinin-potentiating peptide A1 Publication10
PropeptideiPRO_000033417342 – 48Sequence analysis7
PeptideiPRO_500004930549 – 59Leu3-blomhotin1 PublicationAdd BLAST11
PropeptideiPRO_000033417460 – 66Sequence analysis7
PeptideiPRO_500004930667 – 77Bradykinin-potentiating peptide C1 PublicationAdd BLAST11
PropeptideiPRO_000033417578 – 84Sequence analysis7
PeptideiPRO_500004930785 – 95Bradykinin-potentiating peptide B1 PublicationAdd BLAST11
PropeptideiPRO_000033417696 – 102Sequence analysis7
PeptideiPRO_5000049308103 – 113Bradykinin-potentiating peptide B1 PublicationAdd BLAST11
PropeptideiPRO_0000334177114 – 116Sequence analysis3
PeptideiPRO_5000049309117 – 127Bradykinin-potentiating peptide E1 PublicationAdd BLAST11
PeptideiPRO_0000342453117 – 121Bradykinin-potentiating peptide Ahb11 Publication5
PropeptideiPRO_0000334178128 – 239Sequence analysisAdd BLAST112
PeptideiPRO_0000342454131 – 136Bradykinin-potentiating peptide Ahb21 Publication6
PeptideiPRO_5000049310242 – 263C-type natriuretic peptideAdd BLAST22

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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 acid1 Publication1
Modified residuei131Pyrrolidone carboxylic acid1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi247 ↔ 263By similarity

Keywords - PTMi

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

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed by the venom gland.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P01021, 1 interactor

Molecular INTeraction database

More...
MINTi
P01021

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P01021

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni89 – 95Angiotensin-converting enzyme active site binding2 Publications7
Regioni107 – 113Angiotensin-converting enzyme active site binding2 Publications7
Regioni152 – 171DisorderedSequence analysisAdd BLAST20
Regioni177 – 205DisorderedSequence analysisAdd BLAST29

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>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

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000663, Natr_peptide
IPR030480, Natr_peptide_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00212, ANP, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00710, NATPEPTIDES

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00183, NAT_PEP, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00263, NATRIURETIC_PEPTIDE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i407BA9A572BF5FC8
GO

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 1073.3 Da. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AB020810 mRNA Translation: BAA36953.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A01254, XASNBA

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4AA2X-ray1.99P104-113[»]
4APJX-ray2.60P104-113[»]
SMRiP01021
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP01021, 1 interactor
MINTiP01021

Family and domain databases

InterProiView protein in InterPro
IPR000663, Natr_peptide
IPR030480, Natr_peptide_CS
PfamiView protein in Pfam
PF00212, ANP, 1 hit
PRINTSiPR00710, NATPEPTIDES
SMARTiView protein in SMART
SM00183, NAT_PEP, 1 hit
PROSITEiView protein in PROSITE
PS00263, NATRIURETIC_PEPTIDE, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiBNP_GLOBL
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P01021
Secondary accession number(s): Q9PT52
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 20, 2008
Last modified: June 2, 2021
This is version 76 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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
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