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Bradykinin-potentiating and C-type natriuretic peptides (Angiotensin-converting enzyme inhibitor) (BPP-CNP homolog) [Cleaved into: Blomhotin; Bradykinin-potentiating peptide A (BPP-a) (Potentiator A); Leu3-blomhotin (Potentiator D); Bradykinin-potentiating peptide B (BPP-b) (Potentiator B); Bradykinin-potentiating peptide C (BPP-c) (Potentiator C); Bradykinin-potentiating peptide E (BPP-e) (Potentiator E); Bradykinin-potentiating peptide Ahb1 (BPP-Ahb1); Bradykinin-potentiating peptide Ahb2 (BPP-Ahb2); C-type natriuretic peptide]

 BNP_GLOBL               Reviewed;         263 AA.
P01021; Q9PT52;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
20-MAY-2008, sequence version 4.
28-FEB-2018, entry version 70.
RecName: Full=Bradykinin-potentiating and C-type natriuretic peptides;
AltName: Full=Angiotensin-converting enzyme inhibitor;
AltName: Full=BPP-CNP homolog;
Contains:
RecName: Full=Blomhotin;
Contains:
RecName: Full=Bradykinin-potentiating peptide A;
Short=BPP-a;
AltName: Full=Potentiator A;
Contains:
RecName: Full=Leu3-blomhotin;
AltName: Full=Potentiator D;
Contains:
RecName: Full=Bradykinin-potentiating peptide B;
Short=BPP-b;
AltName: Full=Potentiator B;
Contains:
RecName: Full=Bradykinin-potentiating peptide C;
Short=BPP-c;
AltName: Full=Potentiator C;
Contains:
RecName: Full=Bradykinin-potentiating peptide E;
Short=BPP-e;
AltName: Full=Potentiator E;
Contains:
RecName: Full=Bradykinin-potentiating peptide Ahb1;
Short=BPP-Ahb1;
Contains:
RecName: Full=Bradykinin-potentiating peptide Ahb2;
Short=BPP-Ahb2;
Contains:
RecName: Full=C-type natriuretic peptide;
Flags: Precursor;
Gloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
NCBI_TaxID=242054;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
PubMed=10604536; DOI=10.1016/S0162-3109(99)00119-8;
Higuchi S., Murayama N., Saguchi K., Ohi H., Fujita Y.,
de Camargo A.C.M., Ogawa T., Deshimaru M., Ohno M.;
"Bradykinin-potentiating peptides and C-type natriuretic peptides from
snake venom.";
Immunopharmacology 44:129-135(1999).
[2]
PROTEIN SEQUENCE OF 31-41, AND PYROGLUTAMATE FORMATION AT GLN-31.
TISSUE=Venom;
PubMed=10519653; DOI=10.1016/S0041-0101(99)00117-8;
Yanoshita R., Kasuga A., Inoue S., Ikeda K., Samejima Y.;
"Blomhotin: a novel peptide with smooth muscle contractile activity
identified in the venom of Agkistrodon halys blomhoffii.";
Toxicon 37:1761-1770(1999).
[3]
PROTEIN SEQUENCE OF 31-40, AND PYROGLUTAMATE FORMATION AT GLN-31.
TISSUE=Venom;
PubMed=4730295; DOI=10.1007/BF01926673;
Kato H., Suzuki T., Okada K., Kimura T., Sakakibara S.;
"Structure of potentiator A, one of the five bradykinin potentiating
peptides from the venom of Agkistrodon halys blomhoffii.";
Experientia 29:574-575(1973).
[4]
PROTEIN SEQUENCE OF 67-77, AND PYROGLUTAMATE FORMATION AT GLN-67.
TISSUE=Venom;
PubMed=4323853; DOI=10.1021/bi00782a007;
Kato H., Suzuki T.;
"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.";
Biochemistry 10:972-980(1971).
[5]
PROTEIN SEQUENCE OF 85-95 AND 103-113, AND PYROGLUTAMATE FORMATION AT
GLN-85 AND GLN-103.
TISSUE=Venom;
Kato H., Suzuki T.;
"Amino acid sequence of bradykinin-potentiating peptide isolated from
the venom of Agkistrodon halys blomhoffii.";
Proc. Jpn. Acad., B, Phys. Biol. Sci. 46:176-181(1970).
[6]
SYNTHESIS OF 31-40 AND 49-59 (BPP-A AND LEU3-BLOMHOTIN), FUNCTION,
PYROGLUTAMATE FORMATION AT GLN-49, AND MASS SPECTROMETRY.
TISSUE=Venom;
PubMed=10866809; DOI=10.1046/j.1432-1327.2000.01443.x;
Murayama N., Michel G.H., Yanoshita R., Samejima Y., Saguchi K.,
Ohi H., Fujita Y., Higuchi S.;
"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.";
Eur. J. Biochem. 267:4075-4080(2000).
[7]
SYNTHESIS OF 67-77; 85-95 AND 103-113 (BPP-B AND BPP-C).
PubMed=11994001; DOI=10.1021/bi012121x;
Cotton J., Hayashi M.A., Cuniasse P., Vazeux G., Ianzer D.,
De Camargo A.C., Dive V.;
"Selective inhibition of the C-domain of angiotensin I converting
enzyme by bradykinin potentiating peptides.";
Biochemistry 41:6065-6071(2002).
[8]
SYNTHESIS OF 117-121 AND 131-136 (BPP-AHB1 AND BPP-AHB2), AND
FUNCTION.
PubMed=17714693; DOI=10.1016/j.bcp.2007.07.014;
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.;
"Identification of novel bradykinin-potentiating peptides (BPPs) in
the venom gland of a rattlesnake allowed the evaluation of the
structure-function relationship of BPPs.";
Biochem. Pharmacol. 74:1350-1360(2007).
-!- FUNCTION: Blomhotin: inhibits the rabbit lung angiotensin-
converting enzyme (ACE) with an IC(50) of 15 uM.
-!- FUNCTION: Bradykinin-potentiating peptide A: causes no contraction
of the rat gastric fundus smooth muscle even at high
concentrations.
-!- FUNCTION: 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 IC(50)
of 1.1 uM.
-!- FUNCTION: 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 IC(50)
of 7.1 uM. {ECO:0000269|PubMed:11994001}.
-!- FUNCTION: Leu3-blomhotin: inhibits the rabbit lung angiotensin-
converting enzyme (ACE) with an IC(50) of 46 uM. Synthetic Leu3-
blomhotin contracts the rat gastric fundus smooth muscle in a
rapid and transient manner.
-!- FUNCTION: Bradykinin-potentiating peptide Ahb1: potentiates the
bradykinin in vivo.
-!- FUNCTION: Bradykinin-potentiating peptide Ahb2: does not show any
bradykinin-potentiating effects.
-!- FUNCTION: C-type natriuretic peptide: exhibits hypotensive and
vasodepressor activity. Acts by activating natriuretic receptors
(NPR1 and/or NPR2 and/or NPR3) (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- MASS SPECTROMETRY: Mass=1073.3; Method=Electrospray; Range=49-59;
Evidence={ECO:0000269|PubMed:10866809};
-!- SIMILARITY: In the N-terminal section; belongs to the bradykinin-
potentiating peptide family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the natriuretic
peptide family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AB020810; BAA36953.1; -; mRNA.
PIR; A01254; XASNBA.
PDB; 4AA2; X-ray; 1.99 A; P=104-113.
PDB; 4APJ; X-ray; 2.60 A; P=104-113.
PDBsum; 4AA2; -.
PDBsum; 4APJ; -.
SMR; P01021; -.
IntAct; P01021; 1.
MINT; P01021; -.
HOVERGEN; HBG073115; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005179; F:hormone activity; IEA:InterPro.
GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
InterPro; IPR000663; Natr_peptide.
InterPro; IPR030480; Natr_peptide_CS.
Pfam; PF00212; ANP; 1.
PRINTS; PR00710; NATPEPTIDES.
SMART; SM00183; NAT_PEP; 1.
PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
1: Evidence at protein level;
3D-structure; Cleavage on pair of basic residues;
Direct protein sequencing; Disulfide bond; Hypotensive agent;
Metalloenzyme inhibitor; Metalloprotease inhibitor;
Protease inhibitor; Pyrrolidone carboxylic acid; Repeat; Secreted;
Signal; Toxin; Vasoactive; Vasodilator.
SIGNAL 1 23 {ECO:0000255}.
PROPEP 24 30 {ECO:0000255}.
/FTId=PRO_0000334172.
PEPTIDE 31 41 Blomhotin.
/FTId=PRO_5000049304.
PEPTIDE 31 40 Bradykinin-potentiating peptide A.
/FTId=PRO_5000049303.
PROPEP 42 48 {ECO:0000255}.
/FTId=PRO_0000334173.
PEPTIDE 49 59 Leu3-blomhotin.
/FTId=PRO_5000049305.
PROPEP 60 66 {ECO:0000255}.
/FTId=PRO_0000334174.
PEPTIDE 67 77 Bradykinin-potentiating peptide C.
/FTId=PRO_5000049306.
PROPEP 78 84 {ECO:0000255}.
/FTId=PRO_0000334175.
PEPTIDE 85 95 Bradykinin-potentiating peptide B.
/FTId=PRO_5000049307.
PROPEP 96 102 {ECO:0000255}.
/FTId=PRO_0000334176.
PEPTIDE 103 113 Bradykinin-potentiating peptide B.
/FTId=PRO_5000049308.
PROPEP 114 116 {ECO:0000255}.
/FTId=PRO_0000334177.
PEPTIDE 117 127 Bradykinin-potentiating peptide E.
{ECO:0000250}.
/FTId=PRO_5000049309.
PEPTIDE 117 121 Bradykinin-potentiating peptide Ahb1.
{ECO:0000250}.
/FTId=PRO_0000342453.
PROPEP 128 239 {ECO:0000255}.
/FTId=PRO_0000334178.
PEPTIDE 131 136 Bradykinin-potentiating peptide Ahb2.
{ECO:0000250}.
/FTId=PRO_0000342454.
PEPTIDE 242 263 C-type natriuretic peptide.
/FTId=PRO_5000049310.
COMPBIAS 34 136 Pro-rich.
COMPBIAS 226 231 Poly-Gly.
MOD_RES 31 31 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:10519653,
ECO:0000269|PubMed:4730295}.
MOD_RES 49 49 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:10866809}.
MOD_RES 67 67 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:4323853}.
MOD_RES 85 85 Pyrrolidone carboxylic acid.
{ECO:0000269|Ref.5}.
MOD_RES 103 103 Pyrrolidone carboxylic acid.
{ECO:0000269|Ref.5}.
MOD_RES 117 117 Pyrrolidone carboxylic acid.
{ECO:0000250}.
DISULFID 247 263 {ECO:0000250}.
SEQUENCE 263 AA; 27339 MW; 407BA9A572BF5FC8 CRC64;
MFVSRLAASG LLLLALMALS LDGKPVQQWS QGRPPGPPIP RLVVQQWSQG LPPGPPIPRL
VVQQWSQGLP PGPPIPPLVV QQWSQGLPPR PKIPPLVVQQ WSQGLPPRPK IPPLVVQKWD
PPPVSPPLLL QPHESPAGGT TALREELSLG PEAASGPAAA GADGGRSGSK APAALHRLSK
SKGASATSAS ASRPMRDLRT DGKQARQNWA RMVNPDHHAV GGCCCGGGGG GARRLKGLVK
KGVAKGCFGL KLDRIGTMSG LGC


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