BNP1_BOTJA
ID BNP1_BOTJA Reviewed; 256 AA.
AC Q6LEM5; P01020; P30421; P68516;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Bradykinin-potentiating and C-type natriuretic peptides;
DE AltName: Full=BPP-CNP;
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 6a {ECO:0000303|PubMed:15245866};
DE Short=BPP-6a {ECO:0000303|PubMed:15245866};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 10a {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:20146532};
DE Short=BPP-10a {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:20146532};
DE AltName: Full=Bradykinin-potentiating peptide IV-1-A {ECO:0000303|PubMed:4334402, ECO:0000303|PubMed:9037028};
DE Short=BPPIV-1-A {ECO:0000303|PubMed:9037028};
DE AltName: Full=Bradykinin-potentiating peptide V-8 {ECO:0000303|PubMed:4334402};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 13a+QQWA {ECO:0000303|PubMed:20146532};
DE Short=BPP-13a+QQWA {ECO:0000303|PubMed:20146532};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 13a+QWA {ECO:0000303|PubMed:20146532};
DE Short=BPP-13a+QWA {ECO:0000303|PubMed:20146532};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 13a {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:20146532, ECO:0000303|PubMed:22869554};
DE Short=BPP-13a {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:20146532, ECO:0000303|PubMed:22869554};
DE AltName: Full=Bradykinin-potentiating peptide III-1-A {ECO:0000303|PubMed:4334402, ECO:0000303|PubMed:9037028};
DE Short=III-1-A {ECO:0000303|PubMed:9037028};
DE AltName: Full=Bradykinin-potentiating peptide V-9 {ECO:0000303|PubMed:4334402};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 10c+QQWA {ECO:0000303|PubMed:20146532};
DE Short=BPP-10c+QQWA {ECO:0000303|PubMed:20146532};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 10c {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:22869554};
DE Short=BPP-10c {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:22869554};
DE Short=BPP-2 {ECO:0000303|PubMed:11994001};
DE AltName: Full=Bradykinin-potentiating peptide IV-1-Bbeta {ECO:0000303|PubMed:9037028};
DE Short=BPP IV-1-Bbeta {ECO:0000303|PubMed:9037028};
DE AltName: Full=Bradykinin-potentiating peptide V-7 {ECO:0000303|PubMed:4334402};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 10c-F {ECO:0000305|PubMed:17315274};
DE Short=BPP-10c-F {ECO:0000305|PubMed:17315274};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 11b {ECO:0000303|PubMed:15245866};
DE Short=BPP-11b {ECO:0000303|PubMed:15245866};
DE AltName: Full=Bradykinin-potentiating peptide IIa;
DE Short=BPP-IIa;
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide IIb {ECO:0000305|PubMed:9037028};
DE Short=BPP-IIb {ECO:0000305|PubMed:9037028};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 5a {ECO:0000303|PubMed:15245866};
DE Short=BPP-5a {ECO:0000303|PubMed:15245866};
DE AltName: Full=Bradykinin-potentiating peptide Va {ECO:0000303|PubMed:9037028};
DE Short=BPPVa {ECO:0000303|PubMed:9037028};
DE AltName: Full=Proline-rich peptide 5a {ECO:0000303|PubMed:21185808};
DE Short=Bj-PRO-5a {ECO:0000303|PubMed:21185808};
DE Short=PRO-5a {ECO:0000303|PubMed:21185808};
DE Contains:
DE RecName: Full=Poly-His-poly-Gly peptide 1 {ECO:0000303|PubMed:22869554};
DE Short=pHpG-1 {ECO:0000303|PubMed:22869554};
DE Contains:
DE RecName: Full=C-type natriuretic peptide {ECO:0000303|PubMed:9037028};
DE AltName: Full=Bj-CNP {ECO:0000303|PubMed:9037028};
DE Flags: Precursor;
OS Bothrops jararaca (Jararaca) (Bothrops jajaraca).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8724;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PYROGLUTAMATE FORMATION AT GLN-103, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Venom gland;
RX PubMed=9037028; DOI=10.1073/pnas.94.4.1189;
RA Murayama N., Hayashi M.A.F., Ohi H., Ferreira L.A.F., Hermann V.V.,
RA Saito H., Fujita Y., Higuchi S., Fernandes B.L., Yamane T.,
RA de Camargo A.C.M.;
RT "Cloning and sequence analysis of a Bothrops jararaca cDNA encoding a
RT precursor of seven bradykinin-potentiating peptides and a C-type
RT natriuretic peptide.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:1189-1193(1997).
RN [2]
RP PROTEIN SEQUENCE OF 31-40; 48-60 AND 68-77 (BPP-10A; BPP-10C AND BPP-13A),
RP FUNCTION, SUBCELLULAR LOCATION, AND PYROGLUTAMATE FORMATION AT GLN-31;
RP GLN-48 AND GLN-68.
RC TISSUE=Venom;
RX PubMed=4334402; DOI=10.1021/bi00798a004;
RA Ondetti M.A., Williams N.J., Sabo E.F., Pluscec J., Weaver E.R., Kocy O.;
RT "Angiotensin-converting enzyme inhibitors from the venom of Bothrops
RT jararaca. Isolation, elucidation of structure, and synthesis.";
RL Biochemistry 10:4033-4039(1971).
RN [3]
RP PROTEIN SEQUENCE OF 31-40; 31-36; 48-60; 68-77; 85-95; 117-121 AND 123-127
RP (BPP-5A; BPP6A; BPP-10A; BPP-10C; BPP-11B AND BPP-13A), FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND
RP PYROGLUTAMATE FORMATION AT GLN-31; GLN-48; GLN-68; GLN-85; GLN-117 AND
RP GLN-123.
RC TISSUE=Venom;
RX PubMed=15245866; DOI=10.1016/j.peptides.2004.04.006;
RA Ianzer D., Konno K., Marques-Porto R., Portaro F.C.V., Stoecklin R.,
RA de Camargo A.C.M., Pimenta D.C.;
RT "Identification of five new bradykinin potentiating peptides (BPPs) from
RT Bothrops jararaca crude venom by using electrospray ionization tandem mass
RT spectrometry after a two-step liquid chromatography.";
RL Peptides 25:1085-1092(2004).
RN [4]
RP PROTEIN SEQUENCE OF 31-40; 44-60; 45-60; 48-60 AND 64-77 (BPP-10A;
RP BPP-13A+QQWA; BPP-13A+QWA; BBP-13A AND BPP-10C+QQWA), PYROGLUTAMATE
RP FORMATION AT GLN-31 GLN-44; GLN-45; GLN-48 AND GLN-64, DEVELOPMENTAL STAGE
RP (BPP-10A; BPP-10C+QQWA; BPP-13A; BPP-13A+QWA AND BPP-13A+QQWA), AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=20146532; DOI=10.1021/pr901027r;
RA Zelanis A., Tashima A.K., Rocha M.M., Furtado M.F., Camargo A.C., Ho P.L.,
RA Serrano S.M.;
RT "Analysis of the ontogenetic variation in the venom proteome/peptidome of
RT Bothrops jararaca reveals different strategies to deal with prey.";
RL J. Proteome Res. 9:2278-2291(2010).
RN [5]
RP PROTEIN SEQUENCE OF 48-60 AND 68-77 (BPP-10C AND BPP-13A), SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND PYROGLUTAMATE
RP FORMATION AT GLN-48 AND GLN-68.
RC TISSUE=Venom;
RX PubMed=15912471; DOI=10.1002/rcm.1973;
RA Wermelinger L.S., Dutra D.L., Oliveira-Carvalho A.L., Soares M.R.,
RA Bloch C. Jr., Zingali R.B.;
RT "Fast analysis of low molecular mass compounds present in snake venom:
RT identification of ten new pyroglutamate-containing peptides.";
RL Rapid Commun. Mass Spectrom. 19:1703-1708(2005).
RN [6]
RP PROTEIN SEQUENCE OF 48-60 (BPP-13A), IDENTIFICATION BY MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, AND PYROGLUTAMATE FORMATION AT GLN-48.
RC TISSUE=Venom;
RX PubMed=18200607; DOI=10.1002/jms.1351;
RA Souza G.H.M.F., Catharino R.R., Ifa D.R., Eberlin M.N., Hyslop S.;
RT "Peptide fingerprinting of snake venoms by direct infusion nano-
RT electrospray ionization mass spectrometry: potential use in venom
RT identification and taxonomy.";
RL J. Mass Spectrom. 43:594-599(2008).
RN [7]
RP PROTEIN SEQUENCE OF 68-73 (BPP-10C-F), FUNCTION, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, AND PYROGLUTAMATE FORMATION AT GLN-68.
RC TISSUE=Venom;
RX PubMed=17315274; DOI=10.1002/rcm.2931;
RA Pimenta D.C., Prezoto B.C., Konno K., de Melo R.L., Furtado M.F.,
RA de Camargo A.C.M., Serrano S.M.T.;
RT "Mass spectrometric analysis of the individual variability of Bothrops
RT jararaca venom peptide fraction. Evidence for sex-based variation among the
RT bradykinin-potentiating peptides.";
RL Rapid Commun. Mass Spectrom. 21:1034-1042(2007).
RN [8]
RP PROTEIN SEQUENCE OF 48-60; 68-77 AND 208-225 (BPP-10C; BPP-13A AND PHPG-1),
RP SYNTHESIS OF 68-77 (BPP-10C), FUNCTION, PYROGLUTAMATE FORMATION AT GLN-48
RP AND GLN-68, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=22869554; DOI=10.1074/mcp.m112.019331;
RA Tashima A.K., Zelanis A., Kitano E.S., Ianzer D., Melo R.L., Rioli V.,
RA Sant'anna S.S., Schenberg A.C., Camargo A.C., Serrano S.M.T.;
RT "Peptidomics of three Bothrops snake venoms: insights into the molecular
RT diversification of proteomes and peptidomes.";
RL Mol. Cell. Proteomics 11:1245-1262(2012).
RN [9]
RP SYNTHESIS OF 68-77 (BPP-10C), AND FUNCTION.
RX PubMed=11994001; DOI=10.1021/bi012121x;
RA Cotton J., Hayashi M.A., Cuniasse P., Vazeux G., Ianzer D.,
RA De Camargo A.C., Dive V.;
RT "Selective inhibition of the C-domain of angiotensin I converting enzyme by
RT bradykinin potentiating peptides.";
RL Biochemistry 41:6065-6071(2002).
RN [10]
RP FUNCTION (BPP-10C).
RX PubMed=17475904; DOI=10.1124/jpet.107.120873;
RA Ianzer D., Santos R.A., Etelvino G.M., Xavier C.H., de Almeida Santos J.,
RA Mendes E.P., Machado L.T., Prezoto B.C., Dive V., de Camargo A.C.;
RT "Do the cardiovascular effects of angiotensin-converting enzyme (ACE) I
RT involve ACE-independent mechanisms? new insights from proline-rich peptides
RT of Bothrops jararaca.";
RL J. Pharmacol. Exp. Ther. 322:795-805(2007).
RN [11]
RP FUNCTION, BIOASSAY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-34;
RP PRO-36; ILE-38; PRO-39 AND PRO-40.
RX PubMed=19491403; DOI=10.1074/jbc.m109.021089;
RA Guerreiro J.R., Lameu C., Oliveira E.F., Klitzke C.F., Melo R.L.,
RA Linares E., Augusto O., Fox J.W., Lebrun I., Serrano S.M., Camargo A.C.;
RT "Argininosuccinate synthetase is a functional target for a snake venom
RT anti-hypertensive peptide: role in arginine and nitric oxide production.";
RL J. Biol. Chem. 284:20022-20033(2009).
RN [12]
RP SYNTHESIS OF 117-121 AND 123-127 (BPP-5A), AND FUNCTION.
RX PubMed=21185808; DOI=10.1016/j.bcp.2010.12.016;
RA Morais K.L., Hayashi M.A., Bruni F.M., Lopes-Ferreira M., Camargo A.C.,
RA Ulrich H., Lameu C.;
RT "Bj-PRO-5a, a natural angiotensin-converting enzyme inhibitor, promotes
RT vasodilatation mediated by both bradykinin B(2)and M1 muscarinic
RT acetylcholine receptors.";
RL Biochem. Pharmacol. 81:736-742(2011).
CC -!- FUNCTION: [Bradykinin-potentiating peptide 5a]: Modestly inhibits ACE
CC (with highest affinity for the N-site) and reveals strong bradykinin-
CC potentiating activity. Induces nitric oxide (NO) production depended on
CC muscarinic acetylcholine receptor M1 subtype (CHRM1) and bradykinin B2
CC receptor (BDKRB2) activation. Both these receptors contribute to the
CC vasodilation induced by this peptide that may have an indirect action
CC on BDKRB2 and a direct agonistic action on CHRM1.
CC -!- FUNCTION: [Bradykinin-potentiating peptide 10c]: Peptide with several
CC activities. It inhibits the activity of the angiotensin-converting
CC enzyme (ACE) by a preferential interaction with its C-domain
CC (PubMed:11994001). It evokes transient hypotension (-14 mmHg) similar
CC to that evoked by 0,5 ug of bradykinin, when injected alone into rats.
CC It has a high bradykinin-potentiating effect (120%), when 60 nmol of
CC BPP-10c are coinjected with 0.5 ug of bradykinin into rats
CC (PubMed:22869554). Does not affect angiotensin-1 pressor effects. Shows
CC potent and long-lasting antihypertensive activity as well as a
CC reduction of the heart rate (PubMed:17475904). It also binds and dose-
CC dependently promotes the activation of cytosolic argininosuccinate
CC synthase (ASS1), an enzyme that catalyzes the conversion of citrulline,
CC L-aspartate and ATP to argininosuccinate, AMP and pyrophosphate. It
CC also enhances ASS1-dependent arginine production in HEK 293 cells, as
CC well as in spontaneous hypertensive rat (SHR) and Wistar rat plasma. In
CC addition, it induces the production of nitric-oxide (NO) by HUVEC cells
CC via the endothelial nitric-oxide synthase (NOS3), which use arginine as
CC a substrate and produce NO. It has been shown to be internalized by
CC ASS1-expressing endothelial (HUVEC) and kidney (HEK 293) cells, and is
CC detected homogenously distributed within the cell cytoplasm for up to 2
CC hours (PubMed:19491403). {ECO:0000269|PubMed:11994001,
CC ECO:0000269|PubMed:17475904, ECO:0000269|PubMed:19491403,
CC ECO:0000269|PubMed:22869554}.
CC -!- FUNCTION: [Bradykinin-potentiating peptide 10c-F]: Has much lower
CC activity than the full-length bradykinin-potentiating peptides.
CC {ECO:0000269|PubMed:17315274}.
CC -!- FUNCTION: [Poly-His-poly-Gly peptide 1]: May serve as a
CC metalloproteinase inhibitor during glandular storage. Their inhibition
CC may be instantly disengaged, by dilution or physiochemical change, when
CC venom is injected into tissue of the victim.
CC {ECO:0000250|UniProtKB:A8YPR6}.
CC -!- FUNCTION: Snake venom natriuretic peptide that exhibits hypotensive and
CC vasodepressor activity. Acts by activating natriuretic receptors (NPR1
CC and/or NPR2 and/or NPR3) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18200607}.
CC Cytoplasm, cytosol. Note=BPP-10c is internalized in the cytosol of prey
CC cells.
CC -!- TISSUE SPECIFICITY: Expressed in venom gland.
CC {ECO:0000269|PubMed:15245866, ECO:0000269|PubMed:15912471,
CC ECO:0000269|PubMed:17315274, ECO:0000269|PubMed:9037028}.
CC -!- DEVELOPMENTAL STAGE: BPP-10a, BPP-10c+QQWA, BPP-13a, BPP-13+QWA and
CC BPP-13A+QQWA seem to be found in both adult and newborn B.jararaca
CC venoms. {ECO:0000269|PubMed:20146532}.
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 5a]: Mass=611.7;
CC Method=Electrospray; Note=BPP-5a.;
CC Evidence={ECO:0000269|PubMed:15245866};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 6a]: Mass=653.7;
CC Method=Electrospray; Note=BPP-6a.;
CC Evidence={ECO:0000269|PubMed:15245866};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 10a]: Mass=1075.2;
CC Method=Electrospray; Note=BPP-10a.;
CC Evidence={ECO:0000269|PubMed:15245866};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 10c]: Mass=1196.3;
CC Method=Electrospray; Note=BPP-10c.;
CC Evidence={ECO:0000269|PubMed:15245866};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 10c]: Mass=1196.65;
CC Method=MALDI; Note=BPP-10c.; Evidence={ECO:0000269|PubMed:15912471};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 10c]: Mass=1195.6;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:22869554};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 10c-F]:
CC Mass=760.33; Method=MALDI; Note=BPP-10c-F.;
CC Evidence={ECO:0000269|PubMed:17315274};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 11b]: Mass=1069.2;
CC Method=Electrospray; Note=BPP-11b.;
CC Evidence={ECO:0000269|PubMed:15245866};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 13a]: Mass=1370.76;
CC Method=MALDI; Note=BPP-13a.; Evidence={ECO:0000269|PubMed:15912471};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 13a]: Mass=1370.5;
CC Method=Electrospray; Note=BPP-13a.;
CC Evidence={ECO:0000269|PubMed:15245866};
CC -!- MISCELLANEOUS: Does not bind to type-1 angiotensin-2 receptor (AGTR1).
CC {ECO:0000305|PubMed:17475904}.
CC -!- MISCELLANEOUS: Bradykinin-potentiating peptide 10c-F is present only in
CC female snakes. {ECO:0000305|PubMed:17315274}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the bradykinin-
CC potentiating peptide family. {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the pHpG family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the natriuretic
CC peptide family. {ECO:0000255}.
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DR EMBL; D85843; BAA12879.1; -; mRNA.
DR PIR; A01253; XAVI9B.
DR AlphaFoldDB; Q6LEM5; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0060422; F:peptidyl-dipeptidase inhibitor activity; NAS:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0097746; P:blood vessel diameter maintenance; NAS:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; NAS:UniProtKB.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
DR GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
DR InterPro; IPR000663; Natr_peptide.
DR InterPro; IPR030480; Natr_peptide_CS.
DR Pfam; PF00212; ANP; 1.
DR PRINTS; PR00710; NATPEPTIDES.
DR SMART; SM00183; NAT_PEP; 1.
DR PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; G-protein coupled receptor impairing toxin;
KW Hypotensive agent; Metalloenzyme inhibitor; Metalloprotease inhibitor;
KW Protease inhibitor; Pyrrolidone carboxylic acid; Secreted; Signal; Toxin;
KW Vasoactive; Vasodilator.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..30
FT /evidence="ECO:0000305"
FT /id="PRO_0000252050"
FT PEPTIDE 31..40
FT /note="Bradykinin-potentiating peptide 10a"
FT /evidence="ECO:0000269|PubMed:15245866,
FT ECO:0000269|PubMed:20146532, ECO:0000269|PubMed:4334402"
FT /id="PRO_0000252051"
FT PEPTIDE 31..36
FT /note="Bradykinin-potentiating peptide 6a"
FT /evidence="ECO:0000269|PubMed:15245866"
FT /id="PRO_0000292029"
FT PROPEP 41..43
FT /evidence="ECO:0000269|PubMed:20146532"
FT /id="PRO_0000252052"
FT PEPTIDE 44..60
FT /note="Bradykinin-potentiating peptide 13a+QQWA"
FT /evidence="ECO:0000269|PubMed:20146532"
FT /id="PRO_0000422961"
FT PEPTIDE 45..60
FT /note="Bradykinin-potentiating peptide 13a+QWA"
FT /evidence="ECO:0000269|PubMed:20146532"
FT /id="PRO_0000422962"
FT PEPTIDE 48..60
FT /note="Bradykinin-potentiating peptide 13a"
FT /evidence="ECO:0000269|PubMed:15245866,
FT ECO:0000269|PubMed:15912471, ECO:0000269|PubMed:18200607,
FT ECO:0000269|PubMed:20146532, ECO:0000269|PubMed:22869554,
FT ECO:0000269|PubMed:4334402"
FT /id="PRO_0000252053"
FT PROPEP 61..63
FT /evidence="ECO:0000305"
FT /id="PRO_0000252054"
FT PEPTIDE 64..77
FT /note="Bradykinin-potentiating peptide 10c+QQWA"
FT /evidence="ECO:0000269|PubMed:20146532"
FT /id="PRO_0000422963"
FT PEPTIDE 68..77
FT /note="Bradykinin-potentiating peptide 10c"
FT /evidence="ECO:0000269|PubMed:15245866,
FT ECO:0000269|PubMed:15912471, ECO:0000269|PubMed:22869554,
FT ECO:0000269|PubMed:4334402"
FT /id="PRO_0000252055"
FT PEPTIDE 68..73
FT /note="Bradykinin-potentiating peptide 10c-F"
FT /evidence="ECO:0000269|PubMed:17315274"
FT /id="PRO_0000292030"
FT PROPEP 78..84
FT /evidence="ECO:0000269|PubMed:15245866"
FT /id="PRO_0000252056"
FT PEPTIDE 85..95
FT /note="Bradykinin-potentiating peptide 11b"
FT /evidence="ECO:0000269|PubMed:15245866,
FT ECO:0000305|PubMed:9037028"
FT /id="PRO_0000252057"
FT PROPEP 96..102
FT /evidence="ECO:0000305"
FT /id="PRO_0000252058"
FT PEPTIDE 103..113
FT /note="Bradykinin-potentiating peptide IIb"
FT /evidence="ECO:0000305|PubMed:9037028"
FT /id="PRO_0000252059"
FT PROPEP 114..116
FT /evidence="ECO:0000305"
FT /id="PRO_0000252060"
FT PEPTIDE 117..121
FT /note="Bradykinin-potentiating peptide 5a"
FT /evidence="ECO:0000269|PubMed:15245866"
FT /id="PRO_0000252061"
FT PROPEP 122
FT /evidence="ECO:0000305"
FT /id="PRO_0000252062"
FT PEPTIDE 123..127
FT /note="Bradykinin-potentiating peptide 5a"
FT /evidence="ECO:0000269|PubMed:15245866"
FT /id="PRO_0000252063"
FT PROPEP 128..207
FT /evidence="ECO:0000305"
FT /id="PRO_0000252064"
FT PEPTIDE 208..225
FT /note="Poly-His-poly-Gly peptide 1"
FT /evidence="ECO:0000269|PubMed:22869554"
FT /id="PRO_0000421887"
FT PROPEP 226..234
FT /evidence="ECO:0000305"
FT /id="PRO_0000421888"
FT PEPTIDE 235..256
FT /note="C-type natriuretic peptide"
FT /evidence="ECO:0000305|PubMed:9037028"
FT /id="PRO_0000252065"
FT REGION 149..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15245866,
FT ECO:0000269|PubMed:20146532, ECO:0000269|PubMed:4334402"
FT MOD_RES 44
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:20146532"
FT MOD_RES 45
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:20146532"
FT MOD_RES 48
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15245866,
FT ECO:0000269|PubMed:15912471, ECO:0000269|PubMed:18200607,
FT ECO:0000269|PubMed:20146532, ECO:0000269|PubMed:22869554,
FT ECO:0000269|PubMed:4334402"
FT MOD_RES 64
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:20146532"
FT MOD_RES 68
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15245866,
FT ECO:0000269|PubMed:15912471, ECO:0000269|PubMed:17315274,
FT ECO:0000269|PubMed:22869554, ECO:0000269|PubMed:4334402"
FT MOD_RES 85
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15245866"
FT MOD_RES 103
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000305|PubMed:9037028"
FT MOD_RES 117
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15245866"
FT MOD_RES 123
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15245866"
FT DISULFID 240..256
FT /evidence="ECO:0000250|UniProtKB:P23582"
FT MUTAGEN 34
FT /note="P->A: Low decrease in ability to enhance AsS
FT activity."
FT /evidence="ECO:0000269|PubMed:19491403"
FT MUTAGEN 36
FT /note="P->A: Low decrease in ability to enhance AsS
FT activity."
FT /evidence="ECO:0000269|PubMed:19491403"
FT MUTAGEN 38
FT /note="I->A: Low decrease in ability to enhance AsS
FT activity."
FT /evidence="ECO:0000269|PubMed:19491403"
FT MUTAGEN 39
FT /note="P->A: Important decrease in ability to enhance AsS
FT activity."
FT /evidence="ECO:0000269|PubMed:19491403"
FT MUTAGEN 40
FT /note="P->A: Important decrease in ability to enhance AsS
FT activity."
FT /evidence="ECO:0000269|PubMed:19491403"
SQ 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
