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Bradykinin potentiating and C-type natriuretic peptides (BPP-CNP) [Cleaved into: Bradykinin-potentiating peptide Cdt1a; Bradykinin-potentiating peptide Cdt1b; Bradykinin-potentiating peptide Cdt2; Bradykinin inhibitor peptide Cdt3; C-type natriuretic peptide (CNP)]

 BNP_CRODU               Reviewed;         181 AA.
Q90Y12; Q90Y11;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
22-NOV-2017, entry version 48.
RecName: Full=Bradykinin potentiating and C-type natriuretic peptides;
AltName: Full=BPP-CNP;
Contains:
RecName: Full=Bradykinin-potentiating peptide Cdt1a;
Contains:
RecName: Full=Bradykinin-potentiating peptide Cdt1b;
Contains:
RecName: Full=Bradykinin-potentiating peptide Cdt2;
Contains:
RecName: Full=Bradykinin inhibitor peptide Cdt3;
Contains:
RecName: Full=C-type natriuretic peptide;
Short=CNP;
Flags: Precursor;
Crotalus durissus terrificus (South American rattlesnake).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
NCBI_TaxID=8732;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SYNTHESIS OF 28-40; 31-40;
44-49 AND 53-58.
TISSUE=Venom gland;
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).
[2]
PROTEIN SEQUENCE OF 31-40, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
MASS SPECTROMETRY, AND PYROGLUTAMATE FORMATION AT GLN-31.
TISSUE=Venom;
PubMed=15912471; DOI=10.1002/rcm.1973;
Wermelinger L.S., Dutra D.L., Oliveira-Carvalho A.L., Soares M.R.,
Bloch C. Jr., Zingali R.B.;
"Fast analysis of low molecular mass compounds present in snake venom:
identification of ten new pyroglutamate-containing peptides.";
Rapid Commun. Mass Spectrom. 19:1703-1708(2005).
-!- FUNCTION: Bradykinin-potentiating peptide both inhibits the
activity of the angiotensin-converting enzyme (ACE) and enhances
the action of bradykinin by inhibiting the peptidases that
inactivate it. It acts as an indirect hypotensive agent. Synthetic
Cdt1a, Cdt1b and the short hexapeptide Cdt3 are able to potentiate
the hypotensive effect mediated by Bk on the blood pressure of
anesthetized rats. {ECO:0000269|PubMed:17714693}.
-!- FUNCTION: Snake venom natriuretic peptide that exhibits
hypotensive and vasodepressor activity. Acts by activating
natriuretic receptors (NPR1 and/or NPR2 and/or NPR3) (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15912471}.
-!- TISSUE SPECIFICITY: Venom gland. {ECO:0000269|PubMed:15912471}.
-!- MASS SPECTROMETRY: Mass=1255.36; Method=MALDI; Range=31-40;
Evidence={ECO:0000269|PubMed:15912471};
-!- 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; AF308593; AAL09426.1; -; mRNA.
EMBL; AF308594; AAL09427.1; -; mRNA.
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;
Cleavage on pair of basic residues; Direct protein sequencing;
Disulfide bond; Hypotensive agent; Metalloenzyme inhibitor;
Metalloprotease inhibitor; Protease inhibitor;
Pyrrolidone carboxylic acid; Secreted; Signal; Toxin; Vasoactive;
Vasodilator.
SIGNAL 1 23 {ECO:0000255}.
PROPEP 24 27 {ECO:0000255}.
/FTId=PRO_0000335906.
PEPTIDE 28 40 Bradykinin-potentiating peptide Cdt1a.
{ECO:0000250}.
/FTId=PRO_0000335907.
PEPTIDE 31 40 Bradykinin-potentiating peptide Cdt1b.
/FTId=PRO_0000335908.
PROPEP 41 43
/FTId=PRO_0000335909.
PEPTIDE 44 49 Bradykinin-potentiating peptide Cdt2.
{ECO:0000250}.
/FTId=PRO_0000335910.
PROPEP 50 52 {ECO:0000255}.
/FTId=PRO_0000335911.
PEPTIDE 53 58 Bradykinin inhibitor peptide Cdt3.
{ECO:0000250}.
/FTId=PRO_0000335912.
PROPEP 59 157 {ECO:0000255}.
/FTId=PRO_0000335913.
PEPTIDE 160 181 C-type natriuretic peptide.
{ECO:0000250}.
/FTId=PRO_0000335914.
COMPBIAS 93 97 Poly-Ala.
COMPBIAS 141 149 Poly-Gly.
MOD_RES 28 28 Pyrrolidone carboxylic acid.
{ECO:0000250}.
MOD_RES 31 31 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:15912471}.
MOD_RES 44 44 Pyrrolidone carboxylic acid.
{ECO:0000250}.
MOD_RES 53 53 Pyrrolidone carboxylic acid.
{ECO:0000250}.
DISULFID 165 181 {ECO:0000250}.
VARIANT 31 31 Q -> H (in isoform 1).
VARIANT 36 36 L -> P (in isoform 1).
VARIANT 144 144 C -> G (in isoform 1).
SEQUENCE 181 AA; 18560 MW; 7B5ADC5B9372D07F CRC64;
MFVSRLAASG LLLLALLAVS LDGKPLQQWS QRWPHLEIPP LVVQNWKSPT QLQARESPAG
GTTALREELS LGPEAALDTP PAGPDGGPRG SKAAAAAPQR LSKSKGASAT SAASRDLRTD
GKQARQNWGR LVSPDHHSAA GGGCGGGGGA RRLKGLAKKR AGNGCFGLKL DRIGSMSGLG
C


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