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Bradykinin-potentiating and C-type natriuretic peptides (BPP-CNP) [Cleaved into: Bradykinin-potentiating peptide 6a (BPP-6a); Bradykinin-potentiating peptide 10a (BPP-10a) (Bradykinin-potentiating peptide IV-1-A) (BPPIV-1-A) (Bradykinin-potentiating peptide V-8); Bradykinin-potentiating peptide 13a QQWA (BPP-13a QQWA); Bradykinin-potentiating peptide 13a QWA (BPP-13a QWA); Bradykinin-potentiating peptide 13a (BPP-13a) (Bradykinin-potentiating peptide III-1-A) (III-1-A) (Bradykinin-potentiating peptide V-9); Bradykinin-potentiating peptide 10c QQWA (BPP-10c QQWA); Bradykinin-potentiating peptide 10c (BPP-10c) (BPP-2) (Bradykinin-potentiating peptide IV-1-Bbeta) (BPP IV-1-Bbeta) (Bradykinin-potentiating peptide V-7); Bradykinin-potentiating peptide 10c-F (BPP-10c-F); Bradykinin-potentiating peptide 11b (BPP-11b) (Bradykinin-potentiating peptide IIa) (BPP-IIa); Bradykinin-potentiating peptide IIb (BPP-IIb); Bradykinin-potentiating peptide 5a (BPP-5a) (Bradykinin-potentiating peptide Va) (BPPVa) (Proline-rich peptide 5a) (Bj-PRO-5a) (PRO-5a); Poly-His-poly-Gly peptide 1 (pHpG-1); C-type natriuretic peptide (Bj-CNP)]

 BNP1_BOTJA              Reviewed;         256 AA.
Q6LEM5; P01020; P30421; P68516;
03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
22-NOV-2017, entry version 47.
RecName: Full=Bradykinin-potentiating and C-type natriuretic peptides;
AltName: Full=BPP-CNP;
Contains:
RecName: Full=Bradykinin-potentiating peptide 6a {ECO:0000303|PubMed:15245866};
Short=BPP-6a {ECO:0000303|PubMed:15245866};
Contains:
RecName: Full=Bradykinin-potentiating peptide 10a {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:20146532};
Short=BPP-10a {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:20146532};
AltName: Full=Bradykinin-potentiating peptide IV-1-A {ECO:0000303|PubMed:4334402, ECO:0000303|PubMed:9037028};
Short=BPPIV-1-A {ECO:0000303|PubMed:9037028};
AltName: Full=Bradykinin-potentiating peptide V-8 {ECO:0000303|PubMed:4334402};
Contains:
RecName: Full=Bradykinin-potentiating peptide 13a+QQWA {ECO:0000303|PubMed:20146532};
Short=BPP-13a+QQWA {ECO:0000303|PubMed:20146532};
Contains:
RecName: Full=Bradykinin-potentiating peptide 13a+QWA {ECO:0000303|PubMed:20146532};
Short=BPP-13a+QWA {ECO:0000303|PubMed:20146532};
Contains:
RecName: Full=Bradykinin-potentiating peptide 13a {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:20146532, ECO:0000303|PubMed:22869554};
Short=BPP-13a {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:20146532, ECO:0000303|PubMed:22869554};
AltName: Full=Bradykinin-potentiating peptide III-1-A {ECO:0000303|PubMed:4334402, ECO:0000303|PubMed:9037028};
Short=III-1-A {ECO:0000303|PubMed:9037028};
AltName: Full=Bradykinin-potentiating peptide V-9 {ECO:0000303|PubMed:4334402};
Contains:
RecName: Full=Bradykinin-potentiating peptide 10c+QQWA {ECO:0000303|PubMed:20146532};
Short=BPP-10c+QQWA {ECO:0000303|PubMed:20146532};
Contains:
RecName: Full=Bradykinin-potentiating peptide 10c {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:22869554};
Short=BPP-10c {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:22869554};
Short=BPP-2 {ECO:0000303|PubMed:11994001};
AltName: Full=Bradykinin-potentiating peptide IV-1-Bbeta {ECO:0000303|PubMed:9037028};
Short=BPP IV-1-Bbeta {ECO:0000303|PubMed:9037028};
AltName: Full=Bradykinin-potentiating peptide V-7 {ECO:0000303|PubMed:4334402};
Contains:
RecName: Full=Bradykinin-potentiating peptide 10c-F {ECO:0000305|PubMed:17315274};
Short=BPP-10c-F {ECO:0000305|PubMed:17315274};
Contains:
RecName: Full=Bradykinin-potentiating peptide 11b {ECO:0000303|PubMed:15245866};
Short=BPP-11b {ECO:0000303|PubMed:15245866};
AltName: Full=Bradykinin-potentiating peptide IIa;
Short=BPP-IIa;
Contains:
RecName: Full=Bradykinin-potentiating peptide IIb {ECO:0000305|PubMed:9037028};
Short=BPP-IIb {ECO:0000305|PubMed:9037028};
Contains:
RecName: Full=Bradykinin-potentiating peptide 5a {ECO:0000303|PubMed:15245866};
Short=BPP-5a {ECO:0000303|PubMed:15245866};
AltName: Full=Bradykinin-potentiating peptide Va {ECO:0000303|PubMed:9037028};
Short=BPPVa {ECO:0000303|PubMed:9037028};
AltName: Full=Proline-rich peptide 5a {ECO:0000303|PubMed:21185808};
Short=Bj-PRO-5a {ECO:0000303|PubMed:21185808};
Short=PRO-5a {ECO:0000303|PubMed:21185808};
Contains:
RecName: Full=Poly-His-poly-Gly peptide 1 {ECO:0000303|PubMed:22869554};
Short=pHpG-1 {ECO:0000303|PubMed:22869554};
Contains:
RecName: Full=C-type natriuretic peptide {ECO:0000303|PubMed:9037028};
AltName: Full=Bj-CNP {ECO:0000303|PubMed:9037028};
Flags: Precursor;
Bothrops jararaca (Jararaca) (Bothrops jajaraca).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
NCBI_TaxID=8724;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PYROGLUTAMATE FORMATION AT GLN-103, AND
TISSUE SPECIFICITY.
TISSUE=Venom gland;
PubMed=9037028; DOI=10.1073/pnas.94.4.1189;
Murayama N., Hayashi M.A.F., Ohi H., Ferreira L.A.F., Hermann V.V.,
Saito H., Fujita Y., Higuchi S., Fernandes B.L., Yamane T.,
de Camargo A.C.M.;
"Cloning and sequence analysis of a Bothrops jararaca cDNA encoding a
precursor of seven bradykinin-potentiating peptides and a C-type
natriuretic peptide.";
Proc. Natl. Acad. Sci. U.S.A. 94:1189-1193(1997).
[2]
PROTEIN SEQUENCE OF 31-40; 48-60 AND 68-77 (BPP-10A; BPP-10C AND
BPP-13A), FUNCTION, SUBCELLULAR LOCATION, AND PYROGLUTAMATE FORMATION
AT GLN-31; GLN-48 AND GLN-68.
TISSUE=Venom;
PubMed=4334402; DOI=10.1021/bi00798a004;
Ondetti M.A., Williams N.J., Sabo E.F., Pluscec J., Weaver E.R.,
Kocy O.;
"Angiotensin-converting enzyme inhibitors from the venom of Bothrops
jararaca. Isolation, elucidation of structure, and synthesis.";
Biochemistry 10:4033-4039(1971).
[3]
PROTEIN SEQUENCE OF 31-40; 31-36; 48-60; 68-77; 85-95; 117-121 AND
123-127 (BPP-5A; BPP6A; BPP-10A; BPP-10C; BPP-11B AND BPP-13A),
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY,
AND PYROGLUTAMATE FORMATION AT GLN-31; GLN-48; GLN-68; GLN-85; GLN-117
AND GLN-123.
TISSUE=Venom;
PubMed=15245866; DOI=10.1016/j.peptides.2004.04.006;
Ianzer D., Konno K., Marques-Porto R., Portaro F.C.V., Stoecklin R.,
de Camargo A.C.M., Pimenta D.C.;
"Identification of five new bradykinin potentiating peptides (BPPs)
from Bothrops jararaca crude venom by using electrospray ionization
tandem mass spectrometry after a two-step liquid chromatography.";
Peptides 25:1085-1092(2004).
[4]
PROTEIN SEQUENCE OF 31-40; 44-60; 45-60; 48-60 AND 64-77 (BPP-10A;
BPP-13A+QQWA; BPP-13A+QWA; BBP-13A AND BPP-10C+QQWA), PYROGLUTAMATE
FORMATION AT GLN-31 GLN-44; GLN-45; GLN-48 AND GLN-64, DEVELOPMENTAL
STAGE (BPP-10A; BPP-10C+QQWA; BPP-13A; BPP-13A+QWA AND BPP-13A+QQWA),
AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Venom;
PubMed=20146532; DOI=10.1021/pr901027r;
Zelanis A., Tashima A.K., Rocha M.M., Furtado M.F., Camargo A.C.,
Ho P.L., Serrano S.M.;
"Analysis of the ontogenetic variation in the venom proteome/peptidome
of Bothrops jararaca reveals different strategies to deal with prey.";
J. Proteome Res. 9:2278-2291(2010).
[5]
PROTEIN SEQUENCE OF 48-60 AND 68-77 (BPP-10C AND BPP-13A), SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND PYROGLUTAMATE
FORMATION AT GLN-48 AND GLN-68.
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).
[6]
PROTEIN SEQUENCE OF 48-60 (BPP-13A), IDENTIFICATION BY MASS
SPECTROMETRY, SUBCELLULAR LOCATION, AND PYROGLUTAMATE FORMATION AT
GLN-48.
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).
[7]
PROTEIN SEQUENCE OF 68-73 (BPP-10C-F), FUNCTION, SUBCELLULAR LOCATION,
MASS SPECTROMETRY, AND PYROGLUTAMATE FORMATION AT GLN-68.
TISSUE=Venom;
PubMed=17315274; DOI=10.1002/rcm.2931;
Pimenta D.C., Prezoto B.C., Konno K., de Melo R.L., Furtado M.F.,
de Camargo A.C.M., Serrano S.M.T.;
"Mass spectrometric analysis of the individual variability of Bothrops
jararaca venom peptide fraction. Evidence for sex-based variation
among the bradykinin-potentiating peptides.";
Rapid Commun. Mass Spectrom. 21:1034-1042(2007).
[8]
PROTEIN SEQUENCE OF 48-60; 68-77 AND 208-225 (BPP-10C; BPP-13A AND
PHPG-1), SYNTHESIS OF 68-77 (BPP-10C), FUNCTION, PYROGLUTAMATE
FORMATION AT GLN-48 AND GLN-68, AND MASS SPECTROMETRY.
TISSUE=Venom;
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).
[9]
SYNTHESIS OF 68-77 (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).
[10]
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).
[11]
FUNCTION, BIOASSAY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-34;
PRO-36; ILE-38; PRO-39 AND PRO-40.
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).
[12]
SYNTHESIS OF 117-121 AND 123-127 (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).
-!- 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: Bradykinin-potentiating peptide 10c-F: has much lower
activity than the full-length bradykinin-potentiating peptides.
{ECO:0000269|PubMed:17315274}.
-!- FUNCTION: Poly-His-poly-Gly peptide 1: may serve as a
metalloproteinase inhibitor during glandular storage. Their
inhibition may be instantly disengaged, by dilution or
physiochemical change, when venom is injected into tissue of the
victim. {ECO:0000250|UniProtKB:A8YPR6}.
-!- 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:18200607}.
Cytoplasm, cytosol. Note=BPP-10c is internalized in the cytosol of
prey cells.
-!- TISSUE SPECIFICITY: Expressed in venom gland.
{ECO:0000269|PubMed:15245866, ECO:0000269|PubMed:15912471,
ECO:0000269|PubMed:17315274, ECO:0000269|PubMed:9037028}.
-!- DEVELOPMENTAL STAGE: BPP-10a, BPP-10c+QQWA, BPP-13a, BPP-13+QWA
and BPP-13A+QQWA seem to be found in both adult and newborn
B.jararaca venoms. {ECO:0000269|PubMed:20146532}.
-!- MASS SPECTROMETRY: Mass=611.7; Method=Electrospray; Range=117-121;
Note=BPP-5a.; Evidence={ECO:0000269|PubMed:15245866};
-!- MASS SPECTROMETRY: Mass=653.7; Method=Electrospray; Range=31-36;
Note=BPP-6a.; Evidence={ECO:0000269|PubMed:15245866};
-!- MASS SPECTROMETRY: Mass=1075.2; Method=Electrospray; Range=31-40;
Note=BPP-10a.; Evidence={ECO:0000269|PubMed:15245866};
-!- MASS SPECTROMETRY: Mass=1196.3; Method=Electrospray; Range=68-77;
Note=BPP-10c.; Evidence={ECO:0000269|PubMed:15245866};
-!- MASS SPECTROMETRY: Mass=1196.65; Method=MALDI; Range=68-77;
Note=BPP-10c.; Evidence={ECO:0000269|PubMed:15912471};
-!- MASS SPECTROMETRY: Mass=1195.6; Method=Electrospray; Range=68-77;
Evidence={ECO:0000269|PubMed:22869554};
-!- MASS SPECTROMETRY: Mass=760.33; Method=MALDI; Range=68-73;
Note=BPP-10c-F.; Evidence={ECO:0000269|PubMed:17315274};
-!- MASS SPECTROMETRY: Mass=1069.2; Method=Electrospray; Range=85-95;
Note=BPP-11b.; Evidence={ECO:0000269|PubMed:15245866};
-!- MASS SPECTROMETRY: Mass=1370.76; Method=MALDI; Range=48-60;
Note=BPP-13a.; Evidence={ECO:0000269|PubMed:15912471};
-!- MASS SPECTROMETRY: Mass=1370.5; Method=Electrospray; Range=48-60;
Note=BPP-13a.; Evidence={ECO:0000269|PubMed:15245866};
-!- MISCELLANEOUS: Does not bind to type-1 angiotensin-2 receptor
(AGTR1). {ECO:0000305|PubMed:17475904}.
-!- MISCELLANEOUS: Bradykinin-potentiating peptide 10c-F is present
only in female snakes. {ECO:0000305|PubMed:17315274}.
-!- SIMILARITY: In the N-terminal section; belongs to the bradykinin-
potentiating peptide family. {ECO:0000305}.
-!- SIMILARITY: In the central section; belongs to the pHpG family.
{ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the natriuretic
peptide family. {ECO:0000255}.
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EMBL; D85843; BAA12879.1; -; mRNA.
PIR; A01253; XAVI9B.
SMR; Q6LEM5; -.
HOVERGEN; HBG073115; -.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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:0060422; F:peptidyl-dipeptidase inhibitor activity; NAS:UniProtKB.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0006469; P:negative regulation of protein kinase activity; NAS:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
GO; GO:0050880; P:regulation of blood vessel size; NAS: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; Cytoplasm;
Direct protein sequencing; Disulfide bond;
G-protein coupled receptor impairing toxin; Hypotensive agent;
Metalloenzyme inhibitor; Metalloprotease inhibitor;
Protease inhibitor; Pyrrolidone carboxylic acid; Secreted; Signal;
Toxin; Vasoactive; Vasodilator.
SIGNAL 1 23 {ECO:0000255}.
PROPEP 24 30 {ECO:0000305}.
/FTId=PRO_0000252050.
PEPTIDE 31 40 Bradykinin-potentiating peptide 10a.
{ECO:0000269|PubMed:15245866,
ECO:0000269|PubMed:20146532,
ECO:0000269|PubMed:4334402}.
/FTId=PRO_0000252051.
PEPTIDE 31 36 Bradykinin-potentiating peptide 6a.
{ECO:0000269|PubMed:15245866}.
/FTId=PRO_0000292029.
PROPEP 41 43 {ECO:0000269|PubMed:20146532}.
/FTId=PRO_0000252052.
PEPTIDE 44 60 Bradykinin-potentiating peptide 13a+QQWA.
{ECO:0000269|PubMed:20146532}.
/FTId=PRO_0000422961.
PEPTIDE 45 60 Bradykinin-potentiating peptide 13a+QWA.
{ECO:0000269|PubMed:20146532}.
/FTId=PRO_0000422962.
PEPTIDE 48 60 Bradykinin-potentiating peptide 13a.
{ECO:0000269|PubMed:15245866,
ECO:0000269|PubMed:15912471,
ECO:0000269|PubMed:18200607,
ECO:0000269|PubMed:20146532,
ECO:0000269|PubMed:22869554,
ECO:0000269|PubMed:4334402}.
/FTId=PRO_0000252053.
PROPEP 61 63 {ECO:0000305}.
/FTId=PRO_0000252054.
PEPTIDE 64 77 Bradykinin-potentiating peptide 10c+QQWA.
{ECO:0000269|PubMed:20146532}.
/FTId=PRO_0000422963.
PEPTIDE 68 77 Bradykinin-potentiating peptide 10c.
{ECO:0000269|PubMed:15245866,
ECO:0000269|PubMed:15912471,
ECO:0000269|PubMed:22869554,
ECO:0000269|PubMed:4334402}.
/FTId=PRO_0000252055.
PEPTIDE 68 73 Bradykinin-potentiating peptide 10c-F.
{ECO:0000269|PubMed:17315274}.
/FTId=PRO_0000292030.
PROPEP 78 84 {ECO:0000269|PubMed:15245866}.
/FTId=PRO_0000252056.
PEPTIDE 85 95 Bradykinin-potentiating peptide 11b.
{ECO:0000269|PubMed:15245866,
ECO:0000305|PubMed:9037028}.
/FTId=PRO_0000252057.
PROPEP 96 102 {ECO:0000305}.
/FTId=PRO_0000252058.
PEPTIDE 103 113 Bradykinin-potentiating peptide IIb.
{ECO:0000305|PubMed:9037028}.
/FTId=PRO_0000252059.
PROPEP 114 116 {ECO:0000305}.
/FTId=PRO_0000252060.
PEPTIDE 117 121 Bradykinin-potentiating peptide 5a.
{ECO:0000269|PubMed:15245866}.
/FTId=PRO_0000252061.
PROPEP 122 122 {ECO:0000305}.
/FTId=PRO_0000252062.
PEPTIDE 123 127 Bradykinin-potentiating peptide 5a.
{ECO:0000269|PubMed:15245866}.
/FTId=PRO_0000252063.
PROPEP 128 207 {ECO:0000305}.
/FTId=PRO_0000252064.
PEPTIDE 208 225 Poly-His-poly-Gly peptide 1.
{ECO:0000269|PubMed:22869554}.
/FTId=PRO_0000421887.
PROPEP 226 234 {ECO:0000305}.
/FTId=PRO_0000421888.
PEPTIDE 235 256 C-type natriuretic peptide.
{ECO:0000305|PubMed:9037028}.
/FTId=PRO_0000252065.
COMPBIAS 34 135 Pro-rich. {ECO:0000255}.
COMPBIAS 216 255 Gly-rich. {ECO:0000255}.
MOD_RES 31 31 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:15245866,
ECO:0000269|PubMed:20146532,
ECO:0000269|PubMed:4334402}.
MOD_RES 44 44 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:20146532}.
MOD_RES 45 45 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:20146532}.
MOD_RES 48 48 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:15245866,
ECO:0000269|PubMed:15912471,
ECO:0000269|PubMed:18200607,
ECO:0000269|PubMed:20146532,
ECO:0000269|PubMed:22869554,
ECO:0000269|PubMed:4334402}.
MOD_RES 64 64 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:20146532}.
MOD_RES 68 68 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:15245866,
ECO:0000269|PubMed:15912471,
ECO:0000269|PubMed:17315274,
ECO:0000269|PubMed:22869554,
ECO:0000269|PubMed:4334402}.
MOD_RES 85 85 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:15245866}.
MOD_RES 103 103 Pyrrolidone carboxylic acid.
{ECO:0000305|PubMed:9037028}.
MOD_RES 117 117 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:15245866}.
MOD_RES 123 123 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:15245866}.
DISULFID 240 256 {ECO:0000250|UniProtKB:P23582}.
MUTAGEN 34 34 P->A: Low decrease in ability to enhance
AsS activity.
{ECO:0000269|PubMed:19491403}.
MUTAGEN 36 36 P->A: Low decrease in ability to enhance
AsS activity.
{ECO:0000269|PubMed:19491403}.
MUTAGEN 38 38 I->A: Low decrease in ability to enhance
AsS activity.
{ECO:0000269|PubMed:19491403}.
MUTAGEN 39 39 P->A: Important decrease in ability to
enhance AsS activity.
{ECO:0000269|PubMed:19491403}.
MUTAGEN 40 40 P->A: Important decrease in ability to
enhance AsS activity.
{ECO:0000269|PubMed:19491403}.
SEQUENCE 256 AA; 26814 MW; 85DBDBA0A9520A45 CRC64;
MVLSRLAASG LLLLALLALS VDGKPVQQWA QSWPGPNIPP LKVQQWAQGG WPRPGPEIPP
LTVQQWAQNW PHPQIPPLTV QQWAQGRAPG PPIPPLTVQQ WAQGRAPHPP IPPAPLQKWA
PLQKWAPLLQ PHESPASGTT ALREELSLGP EAASGVPSAG AEVGRSGSKA PAAPHRLSKS
KGAAATRPMR DLRPDGKQAR QNWGRMAHHD HHAAAGGGGG GGGGARRLKG LAKKGAAKGC
FGLKLDRIGT MSGLGC


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