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P01021

- BNP_GLOBL

UniProt

P01021 - BNP_GLOBL

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
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 4 (20 May 2008)
      Previous versions | rss
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    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

    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-SubCell

    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:
    PDBe
    RCSB PDB
    PDBj
    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

    MFVSRLAASG LLLLALMALS LDGKPVQQWS QGRPPGPPIP RLVVQQWSQG    50
    LPPGPPIPRL VVQQWSQGLP PGPPIPPLVV QQWSQGLPPR PKIPPLVVQQ 100
    WSQGLPPRPK IPPLVVQKWD PPPVSPPLLL QPHESPAGGT TALREELSLG 150
    PEAASGPAAA GADGGRSGSK APAALHRLSK SKGASATSAS ASRPMRDLRT 200
    DGKQARQNWA RMVNPDHHAV GGCCCGGGGG GARRLKGLVK KGVAKGCFGL 250
    KLDRIGTMSG LGC 263
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB020810 mRNA. Translation: BAA36953.1.
    PIRiA01254. XASNBA.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB020810 mRNA. Translation: BAA36953.1 .
    PIRi A01254. XASNBA.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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 1, 2014
    This is version 63 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

    External Data

    Dasty 3