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Bradykinin-potentiating and C-type natriuretic peptides (BPP-CNP) [Cleaved into: Bradykinin-potentiating peptide 1 (BPP 1); Bradykinin-potentiating peptide 2 (BPP 2); Bradykinin-potentiating peptide 3 (BPP 3); Bradykinin-potentiating peptide 4 (BPP 4); Bradykinin-potentiating peptide 5 (BPP 5); Bradykinin inhibitor peptide (BIP); C-type natriuretic peptide (CNP)]

 BNP_LACMU               Reviewed;         239 AA.
Q27J49;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
04-APR-2006, sequence version 1.
22-NOV-2017, entry version 35.
RecName: Full=Bradykinin-potentiating and C-type natriuretic peptides;
AltName: Full=BPP-CNP;
Contains:
RecName: Full=Bradykinin-potentiating peptide 1;
Short=BPP 1;
Contains:
RecName: Full=Bradykinin-potentiating peptide 2;
Short=BPP 2;
Contains:
RecName: Full=Bradykinin-potentiating peptide 3;
Short=BPP 3;
Contains:
RecName: Full=Bradykinin-potentiating peptide 4;
Short=BPP 4;
Contains:
RecName: Full=Bradykinin-potentiating peptide 5;
Short=BPP 5;
Contains:
RecName: Full=Bradykinin inhibitor peptide;
Short=BIP;
Contains:
RecName: Full=C-type natriuretic peptide;
Short=CNP;
Flags: Precursor;
Lachesis muta muta (Bushmaster).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Lachesis.
NCBI_TaxID=8753;
[1] {ECO:0000305, ECO:0000312|EMBL:ABD52884.1}
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 34-42; 50-61; 65-75;
83-94; 98-108 AND 218-239, PYROGLUTAMATE FORMATION AT GLN-50; GLN-65;
GLN-83 AND GLN-98, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS
SPECTROMETRY.
TISSUE=Venom {ECO:0000269|PubMed:15876444}, and
Venom gland {ECO:0000269|PubMed:15876444};
PubMed=15876444; DOI=10.1016/j.toxicon.2005.03.006;
Soares M.R., Oliveira-Carvalho A.L., Wermelinger L.S., Zingali R.B.,
Ho P.L., Junqueira-de-Azevedo I.L.M., Diniz M.R.V.;
"Identification of novel bradykinin-potentiating peptides and C-type
natriuretic peptide from Lachesis muta venom.";
Toxicon 46:31-38(2005).
[2] {ECO:0000312|EMBL:ABD52884.1}
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland {ECO:0000269|PubMed:16582429};
PubMed=16582429; DOI=10.1534/genetics.106.056515;
Junqueira-de-Azevedo I.L.M., Ching A.T.C., Carvalho E., Faria F.,
Nishiyama M.Y. Jr., Ho P.L., Diniz M.R.V.;
"Lachesis muta (Viperidae) cDNAs reveal diverging pit viper molecules
and scaffolds typical of cobra (Elapidae) venoms: implications for
snake toxin repertoire evolution.";
Genetics 173:877-889(2006).
[3] {ECO:0000305}
PROTEIN SEQUENCE OF 137-147, FUNCTION, SUBCELLULAR LOCATION, AND MASS
SPECTROMETRY.
TISSUE=Venom {ECO:0000269|PubMed:16277978};
PubMed=16277978; DOI=10.1016/j.bbrc.2005.10.130;
Graham R.L.J., Graham C., McClean S., Chen T., O'Rourke M., Hirst D.,
Theakston D., Shaw C.;
"Identification and functional analysis of a novel bradykinin
inhibitory peptide in the venoms of new world crotalinae pit vipers.";
Biochem. Biophys. Res. Commun. 338:1587-1592(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 (By
similarity). {ECO:0000250}.
-!- FUNCTION: Bradykinin inhibitor peptide antagonizes the
vasodilatory actions of bradykinin at the B2 bradykinin receptor.
{ECO:0000269|PubMed:16277978}.
-!- 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:15876444,
ECO:0000269|PubMed:16277978}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
{ECO:0000269|PubMed:15876444}.
-!- MASS SPECTROMETRY: Mass=1088.11; Mass_error=0.02; Method=MALDI;
Range=34-42; Note=Bradykinin-potentiating peptide 1.;
Evidence={ECO:0000269|PubMed:15876444};
-!- MASS SPECTROMETRY: Mass=1244.63; Mass_error=0.02; Method=MALDI;
Range=50-61; Note=Bradykinin-potentiating peptide 2.;
Evidence={ECO:0000269|PubMed:15876444};
-!- MASS SPECTROMETRY: Mass=1404.60; Mass_error=0.02; Method=MALDI;
Range=65-75; Note=Bradykinin-potentiating peptide 3.;
Evidence={ECO:0000269|PubMed:15876444};
-!- MASS SPECTROMETRY: Mass=1277.74; Mass_error=0.02; Method=MALDI;
Range=83-94; Note=Bradykinin-potentiating peptide 4.;
Evidence={ECO:0000269|PubMed:15876444};
-!- MASS SPECTROMETRY: Mass=1374.16; Mass_error=0.02; Method=MALDI;
Range=98-108; Note=Bradykinin-potentiating peptide 5.;
Evidence={ECO:0000269|PubMed:15876444};
-!- MASS SPECTROMETRY: Mass=1063.18; Method=MALDI; Range=137-147;
Note=Bradykinin inhibitor peptide.;
Evidence={ECO:0000269|PubMed:16277978};
-!- SIMILARITY: In the N-terminal section; belongs to the bradykinin-
potentiating peptide family. {ECO:0000305}.
-!- SIMILARITY: In the central section; belongs to the bradykinin
inhibitor peptide family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the natriuretic
peptide family. {ECO:0000255}.
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EMBL; DQ396475; ABD52884.1; -; mRNA.
SMR; Q27J49; -.
PRIDE; Q27J49; -.
HOVERGEN; HBG073115; -.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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:0009405; P:pathogenesis; IDA:UniProtKB.
GO; GO:0045777; P:positive regulation of blood pressure; IDA:UniProtKB.
GO; GO:0050880; P:regulation of blood vessel size; IDA:UniProtKB.
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 33 {ECO:0000255,
ECO:0000269|PubMed:15876444}.
/FTId=PRO_0000258024.
PEPTIDE 34 42 Bradykinin-potentiating peptide 1.
{ECO:0000269|PubMed:15876444}.
/FTId=PRO_0000258025.
PROPEP 43 49 {ECO:0000269|PubMed:15876444}.
/FTId=PRO_0000258026.
PEPTIDE 50 61 Bradykinin-potentiating peptide 2.
{ECO:0000269|PubMed:15876444}.
/FTId=PRO_0000258027.
PROPEP 62 64 {ECO:0000269|PubMed:15876444}.
/FTId=PRO_0000258028.
PEPTIDE 65 75 Bradykinin-potentiating peptide 3.
{ECO:0000269|PubMed:15876444}.
/FTId=PRO_0000258029.
PROPEP 76 82 {ECO:0000269|PubMed:15876444}.
/FTId=PRO_0000258030.
PEPTIDE 83 94 Bradykinin-potentiating peptide 4.
{ECO:0000269|PubMed:15876444}.
/FTId=PRO_0000258031.
PROPEP 95 97 {ECO:0000269|PubMed:15876444}.
/FTId=PRO_0000258032.
PEPTIDE 98 108 Bradykinin-potentiating peptide 5.
{ECO:0000269|PubMed:15876444}.
/FTId=PRO_0000258033.
PROPEP 109 136 {ECO:0000269|PubMed:15876444,
ECO:0000269|PubMed:16277978}.
/FTId=PRO_0000258034.
PEPTIDE 137 147 Bradykinin inhibitor peptide.
{ECO:0000269|PubMed:16277978}.
/FTId=PRO_0000258035.
PROPEP 148 217 {ECO:0000269|PubMed:15876444,
ECO:0000269|PubMed:16277978}.
/FTId=PRO_0000258036.
PEPTIDE 218 239 C-type natriuretic peptide.
{ECO:0000269|PubMed:15876444}.
/FTId=PRO_0000258037.
COMPBIAS 35 159 Pro-rich. {ECO:0000255}.
COMPBIAS 200 207 Poly-Gly. {ECO:0000255}.
MOD_RES 50 50 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:15876444}.
MOD_RES 65 65 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:15876444}.
MOD_RES 83 83 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:15876444}.
MOD_RES 98 98 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:15876444}.
DISULFID 223 239 {ECO:0000250}.
SEQUENCE 239 AA; 25453 MW; 8E7FCFFC2B587497 CRC64;
MFVSRLAASG LLLLALLAVS LDGKPVQQWS HKGWPPRPQI PPLVVQQWSQ KPWPPGHHIP
PVVVQEWPPG HHIPPLVVQQ WSQKKWPPGH HIPPLVVQKW DPPPISPPLL KPHESPAGGT
TALREELSLG PEAALDTPPA GPDVGPRGSK APAAPHRLPK SKGASATSAA SRPMRDLRTD
GKQARQNWGR MMNPDHHAVG GGGGGGGARR LKGLAKKRVG DGCFGLKLDR IGSMSGLGC


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