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Bradykinin-potentiating and C-type natriuretic peptides (Angiotensin-converting enzyme inhibitor) (BPP-CNP homolog) [Cleaved into: Bradykinin-potentiating peptide 13a (BPP-13a) (Bradykinin-potentiating peptide S3,1); Bradykinin-potentiating peptide 10c (BPP-10c) (BPP-2) (Bradykinin-potentiating peptide S4,3,1); Bradykinin-potentiating peptide 12b (BPP-12b) (Bradykinin-potentiating peptide S4,3,2); Bradykinin-potentiating peptide 11e (BPP-11e); Bradykinin-potentiating peptide 5a (BPP-5a) (Bradykinin-potentiating peptide S5,2) (Bradykinin-potentiating peptide Va) (BPPVa) (Proline-rich peptide 5a) (PRO-5a); C-type natriuretic peptide (CNP)]

 BNP_BOTIN               Reviewed;         265 AA.
P68515; P01020; P30421; P30422; P30423; P30425; Q8QG91;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
20-MAY-2008, sequence version 2.
22-NOV-2017, entry version 46.
RecName: Full=Bradykinin-potentiating and C-type natriuretic peptides;
AltName: Full=Angiotensin-converting enzyme inhibitor;
AltName: Full=BPP-CNP homolog;
Contains:
RecName: Full=Bradykinin-potentiating peptide 13a {ECO:0000303|PubMed:2386615};
Short=BPP-13a {ECO:0000303|PubMed:2386615};
AltName: Full=Bradykinin-potentiating peptide S3,1 {ECO:0000303|PubMed:2386615};
Contains:
RecName: Full=Bradykinin-potentiating peptide 10c {ECO:0000303|PubMed:2386615};
Short=BPP-10c {ECO:0000303|PubMed:2386615};
Short=BPP-2 {ECO:0000303|PubMed:11994001};
AltName: Full=Bradykinin-potentiating peptide S4,3,1 {ECO:0000303|PubMed:2386615};
Contains:
RecName: Full=Bradykinin-potentiating peptide 12b {ECO:0000250|UniProtKB:Q9PW56};
Short=BPP-12b {ECO:0000250|UniProtKB:Q9PW56};
AltName: Full=Bradykinin-potentiating peptide S4,3,2 {ECO:0000303|PubMed:2386615};
Contains:
RecName: Full=Bradykinin-potentiating peptide 11e {ECO:0000250|UniProtKB:Q9PW56};
Short=BPP-11e {ECO:0000250|UniProtKB:Q9PW56};
Contains:
RecName: Full=Bradykinin-potentiating peptide 5a {ECO:0000303|PubMed:2386615};
Short=BPP-5a {ECO:0000303|PubMed:2386615};
AltName: Full=Bradykinin-potentiating peptide S5,2 {ECO:0000303|PubMed:2386615};
AltName: Full=Bradykinin-potentiating peptide Va {ECO:0000250|UniProtKB:Q6LEM5};
Short=BPPVa {ECO:0000250|UniProtKB:Q6LEM5};
AltName: Full=Proline-rich peptide 5a {ECO:0000303|PubMed:21185808};
Short=PRO-5a {ECO:0000303|PubMed:21185808};
Contains:
RecName: Full=C-type natriuretic peptide;
Short=CNP;
Flags: Precursor;
Bothrops insularis (Golden lancehead) (Lachesis insularis).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
NCBI_TaxID=8723;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
PubMed=12459276; DOI=10.1016/S0378-1119(02)01080-6;
Junqueira-de-Azevedo I.L.M., Ho P.L.;
"A survey of gene expression and diversity in the venom glands of the
pitviper snake Bothrops insularis through the generation of expressed
sequence tags (ESTs).";
Gene 299:279-291(2002).
[2]
PROTEIN SEQUENCE OF 31-43; 51-63; 71-80; 88-99; 121-125 AND 127-131
(BPP-13A; BPP-10C; BPP-12B AND BPP-5A), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND PYROGLUTAMATE FORMATION AT GLN-31; GLN-51; GLN-71;
GLN-88; GLN-121 AND GLN-127.
TISSUE=Venom;
PubMed=2386615; DOI=10.1007/BF01025312;
Cintra A.C.O., Vieira C.A., Giglio J.R.;
"Primary structure and biological activity of bradykinin potentiating
peptides from Bothrops insularis snake venom.";
J. Protein Chem. 9:221-227(1990).
[3]
PROTEIN SEQUENCE OF 31-43; 51-63; 71-80 AND 88-99 (BPP-13A; BPP-10C
AND BPP-12B), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
SPECTROMETRY, AND PYROGLUTAMATE FORMATION AT GLN-31; GLN-51; GLN-71
AND GLN-88.
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).
[4]
PROTEIN SEQUENCE OF 31-43 AND 51-63 (BPP-13A), IDENTIFICATION BY MASS
SPECTROMETRY, SUBCELLULAR LOCATION, AND PYROGLUTAMATE FORMATION AT
GLN-31 AND GLN-51.
TISSUE=Venom;
PubMed=18200607; DOI=10.1002/jms.1351;
Souza G.H.M.F., Catharino R.R., Ifa D.R., Eberlin M.N., Hyslop S.;
"Peptide fingerprinting of snake venoms by direct infusion nano-
electrospray ionization mass spectrometry: potential use in venom
identification and taxonomy.";
J. Mass Spectrom. 43:594-599(2008).
[5]
SYNTHESIS OF 71-80 (BPP-10C), AND FUNCTION.
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).
[6]
FUNCTION (BPP-10C).
PubMed=17475904; DOI=10.1124/jpet.107.120873;
Ianzer D., Santos R.A., Etelvino G.M., Xavier C.H.,
de Almeida Santos J., Mendes E.P., Machado L.T., Prezoto B.C.,
Dive V., de Camargo A.C.;
"Do the cardiovascular effects of angiotensin-converting enzyme (ACE)
I involve ACE-independent mechanisms? new insights from proline-rich
peptides of Bothrops jararaca.";
J. Pharmacol. Exp. Ther. 322:795-805(2007).
[7]
FUNCTION, BIOASSAY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-74;
PRO-76; ILE-78; PRO-79 AND PRO-80.
PubMed=19491403; DOI=10.1074/jbc.M109.021089;
Guerreiro J.R., Lameu C., Oliveira E.F., Klitzke C.F., Melo R.L.,
Linares E., Augusto O., Fox J.W., Lebrun I., Serrano S.M.,
Camargo A.C.;
"Argininosuccinate synthetase is a functional target for a snake venom
anti-hypertensive peptide: role in arginine and nitric oxide
production.";
J. Biol. Chem. 284:20022-20033(2009).
[8]
SYNTHESIS OF 121-125 AND 127-131 (BPP-5A), AND FUNCTION.
PubMed=21185808; DOI=10.1016/j.bcp.2010.12.016;
Morais K.L., Hayashi M.A., Bruni F.M., Lopes-Ferreira M.,
Camargo A.C., Ulrich H., Lameu C.;
"Bj-PRO-5a, a natural angiotensin-converting enzyme inhibitor,
promotes vasodilatation mediated by both bradykinin B(2)and M1
muscarinic acetylcholine receptors.";
Biochem. Pharmacol. 81:736-742(2011).
[9]
SYNTHESIS OF 71-80 (BPP-10C), AND FUNCTION.
PubMed=22869554; DOI=10.1074/mcp.M112.019331;
Tashima A.K., Zelanis A., Kitano E.S., Ianzer D., Melo R.L., Rioli V.,
Sant'anna S.S., Schenberg A.C., Camargo A.C., Serrano S.M.T.;
"Peptidomics of three Bothrops snake venoms: insights into the
molecular diversification of proteomes and peptidomes.";
Mol. Cell. Proteomics 11:1245-1262(2012).
-!- FUNCTION: Bradykinin-potentiating peptide 5a: modestly inhibits
ACE (with highest affinity for the N-site) and reveals strong
bradykinin-potentiating activity. Induces nitric oxide (NO)
production depended on muscarinic acetylcholine receptor M1
subtype (CHRM1) and bradykinin B2 receptor (BDKRB2) activation.
Both these receptors contribute to the vasodilation induced by
this peptide that may have an indirect action on BDKRB2 and a
direct agonistic action on CHRM1.
-!- FUNCTION: Bradykinin-potentiating peptide 10c: peptide with
several activities. It inhibits the activity of the angiotensin-
converting enzyme (ACE) by a preferential interaction with its C-
domain (PubMed:11994001). It evokes transient hypotension (-14
mmHg) similar to that evoked by 0,5 ug of bradykinin, when
injected alone into rats. It has a high bradykinin-potentiating
effect (120%), when 60 nmol of BPP-10c are coinjected with 0.5 ug
of bradykinin into rats (PubMed:22869554). Does not affect
angiotensin-1 pressor effects. Shows potent and long-lasting
antihypertensive activity as well as a reduction of the heart rate
(PubMed:17475904). It also binds and dose-dependently promotes the
activation of cytosolic argininosuccinate synthase (ASS1), an
enzyme that catalyzes the conversion of citrulline, L-aspartate
and ATP to argininosuccinate, AMP and pyrophosphate. It also
enhances ASS1-dependent arginine production in HEK 293 cells, as
well as in spontaneous hypertensive rat (SHR) and Wistar rat
plasma. In addition, it induces the production of nitric-oxide
(NO) by HUVEC cells via the endothelial nitric-oxide synthase
(NOS3), which use arginine as a substrate and produce NO. It has
been shown to be internalized by ASS1-expressing endothelial
(HUVEC) and kidney (HEK 293) cells, and is detected homogenously
distributed within the cell cytoplasm for up to 2 hours
(PubMed:19491403). {ECO:0000269|PubMed:11994001,
ECO:0000269|PubMed:17475904, ECO:0000269|PubMed:19491403,
ECO:0000269|PubMed:22869554}.
-!- 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 {ECO:0000269|PubMed:18200607}.
Cytoplasm, cytosol. Note=BPP-10c is internalized in the cytosol of
prey cells.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
{ECO:0000269|PubMed:15912471, ECO:0000269|PubMed:2386615}.
-!- MASS SPECTROMETRY: Mass=1370.81; Method=MALDI; Range=31-43;
Evidence={ECO:0000269|PubMed:15912471};
-!- MASS SPECTROMETRY: Mass=1370.81; Method=MALDI; Range=51-63;
Evidence={ECO:0000269|PubMed:15912471};
-!- MASS SPECTROMETRY: Mass=1196.41; Method=MALDI; Range=71-80;
Evidence={ECO:0000269|PubMed:15912471};
-!- MASS SPECTROMETRY: Mass=1279.50; Method=MALDI; Range=88-99;
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; AF490531; AAM09690.1; -; mRNA.
PIR; B37196; B37196.
PIR; C37196; C37196.
PIR; G37196; G37196.
SMR; P68515; -.
HOVERGEN; HBG073115; -.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; ISS: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: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; Cytoplasm;
Direct protein sequencing; Disulfide bond;
G-protein coupled acetylcholine receptor impairing toxin;
G-protein coupled receptor impairing toxin; 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:0000305}.
/FTId=PRO_0000334179.
PEPTIDE 31 43 Bradykinin-potentiating peptide 13a.
{ECO:0000269|PubMed:15912471,
ECO:0000269|PubMed:18200607,
ECO:0000269|PubMed:2386615}.
/FTId=PRO_0000043507.
PROPEP 44 50 {ECO:0000305}.
/FTId=PRO_0000334180.
PEPTIDE 51 63 Bradykinin-potentiating peptide 13a.
{ECO:0000269|PubMed:15912471,
ECO:0000269|PubMed:18200607,
ECO:0000269|PubMed:2386615}.
/FTId=PRO_0000334181.
PROPEP 64 70 {ECO:0000305}.
/FTId=PRO_0000334182.
PEPTIDE 71 80 Bradykinin-potentiating peptide 10c.
{ECO:0000269|PubMed:15912471,
ECO:0000269|PubMed:2386615}.
/FTId=PRO_0000043508.
PROPEP 81 87 {ECO:0000305}.
/FTId=PRO_0000334183.
PEPTIDE 88 99 Bradykinin-potentiating peptide 12b.
{ECO:0000269|PubMed:15912471,
ECO:0000269|PubMed:2386615}.
/FTId=PRO_0000043509.
PROPEP 100 106 {ECO:0000305}.
/FTId=PRO_0000334184.
PEPTIDE 107 117 Bradykinin-potentiating peptide 11e.
{ECO:0000250|UniProtKB:Q9PW56}.
/FTId=PRO_0000334185.
PROPEP 118 120 {ECO:0000305}.
/FTId=PRO_0000334186.
PEPTIDE 121 125 Bradykinin-potentiating peptide 5a.
{ECO:0000269|PubMed:2386615}.
/FTId=PRO_0000043511.
PROPEP 126 126 {ECO:0000305}.
/FTId=PRO_0000334187.
PEPTIDE 127 131 Bradykinin-potentiating peptide 5a.
{ECO:0000269|PubMed:2386615}.
/FTId=PRO_0000334188.
PROPEP 132 241 {ECO:0000305}.
/FTId=PRO_0000334189.
PEPTIDE 244 265 C-type natriuretic peptide.
{ECO:0000250}.
/FTId=PRO_0000334190.
COMPBIAS 35 139 Pro-rich.
COMPBIAS 224 264 Gly-rich.
MOD_RES 31 31 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:15912471,
ECO:0000269|PubMed:18200607,
ECO:0000269|PubMed:2386615}.
MOD_RES 51 51 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:15912471,
ECO:0000269|PubMed:18200607,
ECO:0000269|PubMed:2386615}.
MOD_RES 71 71 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:15912471,
ECO:0000269|PubMed:2386615}.
MOD_RES 88 88 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:15912471,
ECO:0000269|PubMed:2386615}.
MOD_RES 107 107 Pyrrolidone carboxylic acid.
{ECO:0000250|UniProtKB:Q9PW56}.
MOD_RES 121 121 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:2386615}.
MOD_RES 127 127 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:2386615}.
DISULFID 249 265 {ECO:0000250|UniProtKB:P23582}.
MUTAGEN 74 74 P->A: Low decrease in ability to enhance
AsS activity.
{ECO:0000269|PubMed:19491403}.
MUTAGEN 76 76 P->A: Low decrease in ability to enhance
AsS activity.
{ECO:0000269|PubMed:19491403}.
MUTAGEN 78 78 I->A: Low decrease in ability to enhance
AsS activity.
{ECO:0000269|PubMed:19491403}.
MUTAGEN 79 79 P->A: Important decrease in ability to
enhance AsS activity.
{ECO:0000269|PubMed:19491403}.
MUTAGEN 80 80 P->A: Important decrease in ability to
enhance AsS activity.
{ECO:0000269|PubMed:19491403}.
CONFLICT 92 92 Missing (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 265 AA; 27763 MW; 0EAE1408B42358BE CRC64;
MVLSRLAASG LLLLALLALS VDGKPVQQWA QGGWPRPGPE IPPLKVQQWA QGGWPRPGPE
IPPLTVQQWA QNWPHPQIPP LTVQQWAQLG PPPRPQIPPL EVQQWAQGRA PHPPIPPAPL
QKWAPVQKWA PLLQPHESPA SGTTALREEL SLGPEAASGV PSAGAEVGRS GSKAPAAPHR
LSKSKGAAAT SAASRPMRDL RPDGKQARQN WGRMVHHDHH AAVGGGGGGG GGGARRLKGL
AKKGAAKGCF GLKLDRIGTM SGLGC


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