BNP_BOTJR
ID BNP_BOTJR Reviewed; 144 AA.
AC Q7T1M3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Bradykinin-potentiating and C-type natriuretic peptides isoform 2;
DE AltName: Full=BPP-CNP;
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 10a {ECO:0000250|UniProtKB:Q6LEM5};
DE Short=BPP-10a {ECO:0000250|UniProtKB:Q6LEM5};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 6a {ECO:0000250|UniProtKB:Q6LEM5};
DE Short=BPP-6a {ECO:0000250|UniProtKB:Q6LEM5};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 13a {ECO:0000250|UniProtKB:Q6LEM5};
DE Short=BPP-13a {ECO:0000250|UniProtKB:Q6LEM5};
DE AltName: Full=Bradykinin-potentiating peptide XIIIa {ECO:0000303|PubMed:18400032};
DE Short=BPP-XIIIa {ECO:0000303|PubMed:18400032};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 10c {ECO:0000303|PubMed:17475904};
DE Short=BPP-10c {ECO:0000303|PubMed:17475904};
DE Short=BPP-2 {ECO:0000303|PubMed:11994001};
DE AltName: Full=Bradykinin-potentiating peptide Xc {ECO:0000303|PubMed:18400032};
DE Short=BPP-Xc {ECO:0000303|PubMed:18400032};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 10c-F {ECO:0000250|UniProtKB:Q6LEM5};
DE Short=BPP-10c-F {ECO:0000250|UniProtKB:Q6LEM5};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 11b {ECO:0000250|UniProtKB:Q6LEM5};
DE Short=BPP-11b {ECO:0000250|UniProtKB:Q6LEM5};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide AP {ECO:0000303|PubMed:18400032};
DE Short=BPP-AP {ECO:0000303|PubMed:18400032};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 11e {ECO:0000250|UniProtKB:Q9PW56};
DE Short=BPP-11e {ECO:0000250|UniProtKB:Q9PW56};
DE AltName: Full=Bradykinin-potentiating peptide XIe {ECO:0000303|PubMed:18400032};
DE Short=BPP-XIe {ECO:0000303|PubMed:18400032};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 5a {ECO:0000250|UniProtKB:P68515};
DE Short=BPP-5a {ECO:0000250|UniProtKB:P68515};
DE AltName: Full=Bradykinin-potentiating peptide Va {ECO:0000250|UniProtKB:Q6LEM5};
DE Short=BPPVa {ECO:0000250|UniProtKB:Q6LEM5};
DE Flags: Precursor; Fragment;
OS Bothrops jararacussu (Jararacussu).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8726;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Hayashi M.A.F., Lameu C., Radis-Baptista G., Yamane T., Camargo A.C.M.;
RT "Cloning and sequence analysis of a Bothrops jararacussu BPPs precursor.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 48-60; 68-77; 85-95 AND 103-113 (BPP-13A; BPP-10C;
RP BPP-11B AND BPP-11E), SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP PYROGLUTAMATE FORMATION AT GLN-48; GLN-68; GLN-85 AND GLN-103.
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 103-115 (BPP-AP), SYNTHESIS OF 103-115, FUNCTION,
RP SUBCELLULAR LOCATION, PYROGLUTAMATE FORMATION AT GLN-103, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=18400032; DOI=10.1111/j.1742-4658.2008.06389.x;
RA Rioli V., Prezoto B.C., Konno K., Melo R.L., Klitzke C.F., Ferro E.S.,
RA Ferreira-Lopes M., Camargo A.C.M., Portaro F.C.V.;
RT "A novel bradykinin potentiating peptide isolated from Bothrops jararacussu
RT venom using catallytically inactive oligopeptidase EP24.15.";
RL FEBS J. 275:2442-2454(2008).
RN [5]
RP FUNCTION, AND SYNTHESIS OF 68-77 (BPP-10C).
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 [6]
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 [7]
RP FUNCTION, BIOASSAY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-71;
RP PRO-73; ILE-75; PRO-76 AND PRO-77.
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 [8]
RP FUNCTION, AND SYNTHESIS OF 68-77 (BPP-10C).
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).
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 11e]: Acts as indirect
CC hypotensive agent. Increases leukocyte rolling flux and adhesion by
CC five-fold in post-capillary venules, without any increments in
CC vasodilation of arterioles.
CC -!- FUNCTION: [Bradykinin-potentiating peptide AP]: Acts as indirect
CC hypotensive agent. Potently induces vasodilation of arterioles, with
CC only a small increase in leukocyte rolling flux.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15912471,
CC ECO:0000269|PubMed:18200607, ECO:0000269|PubMed:18400032}. Cytoplasm,
CC cytosol. Note=BPP-10c is internalized in the cytosol of prey cells.
CC -!- TISSUE SPECIFICITY: Expressed by venom gland.
CC {ECO:0000305|PubMed:15912471, ECO:0000305|PubMed:18200607,
CC ECO:0000305|PubMed:18400032}.
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 13a]: Mass=1370.75;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:15912471};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 10c]: Mass=1196.65;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:15912471};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 11b]: Mass=1095.66;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:15912471};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 11e]: Mass=1189.71;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:15912471};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 11e]: Mass=1189.6;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:18400032};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide AP]: Mass=1357.7;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:18400032};
CC -!- SIMILARITY: In the N-terminal section; belongs to the bradykinin-
CC potentiating peptide family. {ECO:0000305}.
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DR EMBL; AY310915; AAP83422.1; -; mRNA.
DR AlphaFoldDB; Q7T1M3; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Hypotensive agent;
KW Metalloenzyme inhibitor; Metalloprotease inhibitor; Protease inhibitor;
KW Pyrrolidone carboxylic acid; Secreted; Signal; Toxin; Vasoactive.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..30
FT /evidence="ECO:0000305"
FT /id="PRO_0000335880"
FT PEPTIDE 31..40
FT /note="Bradykinin-potentiating peptide 10a"
FT /evidence="ECO:0000250|UniProtKB:Q6LEM5"
FT /id="PRO_0000335881"
FT PEPTIDE 31..36
FT /note="Bradykinin-potentiating peptide 6a"
FT /evidence="ECO:0000250|UniProtKB:Q6LEM5"
FT /id="PRO_0000335882"
FT PROPEP 41..47
FT /evidence="ECO:0000305"
FT /id="PRO_0000335883"
FT PEPTIDE 48..60
FT /note="Bradykinin-potentiating peptide 13a"
FT /evidence="ECO:0000269|PubMed:15912471,
FT ECO:0000269|PubMed:18200607"
FT /id="PRO_0000335884"
FT PROPEP 61..67
FT /evidence="ECO:0000305"
FT /id="PRO_0000335885"
FT PEPTIDE 68..77
FT /note="Bradykinin-potentiating peptide 10c"
FT /evidence="ECO:0000269|PubMed:15912471"
FT /id="PRO_0000335886"
FT PEPTIDE 68..73
FT /note="Bradykinin-potentiating peptide 10c-F"
FT /evidence="ECO:0000250|UniProtKB:Q6LEM5"
FT /id="PRO_0000335887"
FT PROPEP 78..84
FT /evidence="ECO:0000305"
FT /id="PRO_0000335888"
FT PEPTIDE 85..95
FT /note="Bradykinin-potentiating peptide 11b"
FT /evidence="ECO:0000269|PubMed:15912471"
FT /id="PRO_0000335889"
FT PROPEP 96..102
FT /evidence="ECO:0000305"
FT /id="PRO_0000335890"
FT PEPTIDE 103..115
FT /note="Bradykinin-potentiating peptide AP"
FT /evidence="ECO:0000269|PubMed:18400032"
FT /id="PRO_0000335891"
FT PEPTIDE 103..113
FT /note="Bradykinin-potentiating peptide 11e"
FT /evidence="ECO:0000269|PubMed:15912471"
FT /id="PRO_0000335892"
FT PROPEP 114..116
FT /evidence="ECO:0000305"
FT /id="PRO_0000335893"
FT PEPTIDE 117..121
FT /note="Bradykinin-potentiating peptide 5a"
FT /evidence="ECO:0000250|UniProtKB:P68515"
FT /id="PRO_0000335894"
FT PROPEP 122
FT /evidence="ECO:0000305"
FT /id="PRO_0000335895"
FT PEPTIDE 123..127
FT /note="Bradykinin-potentiating peptide 5a"
FT /evidence="ECO:0000250|UniProtKB:P68515"
FT /id="PRO_0000335896"
FT PROPEP 128..>144
FT /evidence="ECO:0000305"
FT /id="PRO_0000335897"
FT REGION 81..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:Q6LEM5"
FT MOD_RES 48
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15912471,
FT ECO:0000269|PubMed:18200607"
FT MOD_RES 68
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15912471"
FT MOD_RES 85
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15912471"
FT MOD_RES 103
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15912471,
FT ECO:0000269|PubMed:18400032"
FT MOD_RES 117
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P68515"
FT MOD_RES 123
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P68515"
FT MUTAGEN 71
FT /note="P->A: Low decrease in ability to enhance AsS
FT activity."
FT /evidence="ECO:0000269|PubMed:19491403"
FT MUTAGEN 73
FT /note="P->A: Low decrease in ability to enhance AsS
FT activity."
FT /evidence="ECO:0000269|PubMed:19491403"
FT MUTAGEN 75
FT /note="I->A: Low decrease in ability to enhance AsS
FT activity."
FT /evidence="ECO:0000269|PubMed:19491403"
FT MUTAGEN 76
FT /note="P->A: Important decrease in ability to enhance AsS
FT activity."
FT /evidence="ECO:0000269|PubMed:19491403"
FT MUTAGEN 77
FT /note="P->A: Important decrease in ability to enhance AsS
FT activity."
FT /evidence="ECO:0000269|PubMed:19491403"
FT NON_TER 144
FT /evidence="ECO:0000305"
SQ SEQUENCE 144 AA; 15982 MW; B23FED5230A84910 CRC64;
MVLSRLAASG LLLLALLALS VDGKPVQQWA QSWPGPNIPQ LLVQQWAQGG WPRPGPEIPP
LTVQQWAQNW PHPQIPPLTV QQWAQGRPPG PPIPPLTVQQ WAQARPPHPP IPPAPLQKWA
PVQKWAPVQK WAPVQKWAPL LQPT
