BPP7A_BOTJA
ID BPP7A_BOTJA Reviewed; 7 AA.
AC P85160;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 26-FEB-2020, entry version 25.
DE RecName: Full=Bradykinin-potentiating peptide 7a;
DE Short=BPP-7a;
DE AltName: Full=Proline-rich peptide 7a;
DE Short=BjPRO-7a;
DE Short=PRO-7a;
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] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP SPECTROMETRY, AND PYROGLUTAMATE FORMATION AT GLN-1.
RC TISSUE=Venom {ECO:0000269|PubMed:15245866};
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 [2]
RP FUNCTION.
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 [3]
RP SYNTHESIS, AND FUNCTION.
RX PubMed=20814884; DOI=10.1002/cyto.a.20963;
RA Negraes P.D., Lameu C., Hayashi M.A., Melo R.L., Camargo A.C., Ulrich H.;
RT "The snake venom peptide Bj-PRO-7a is a M1 muscarinic acetylcholine
RT receptor agonist.";
RL Cytometry A 79:77-83(2011).
CC -!- FUNCTION: This peptide shows potent and long-lasting antihypertensive
CC activity as well as a reduction of the heart rate. These effects may be
CC explained by the agonistic activities of this peptide for the
CC muscarinic acetylcholine receptor M1 (CHRM1) (EC(50)=0.25-0.31 uM),
CC since these types of G-protein coupled receptor have been demonstrated
CC to be active in the blood pressure control.
CC {ECO:0000269|PubMed:15245866, ECO:0000269|PubMed:17475904,
CC ECO:0000269|PubMed:20814884}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15245866}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:15245866}.
CC -!- MASS SPECTROMETRY: Mass=705.8; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15245866};
CC -!- MISCELLANEOUS: This peptide weakly inhibits angiotensin-converting
CC enzyme (ACE) with no clear preference for either C- or N-domains. It
CC does not potentiate bradykinin, and does not affect angiotensin-1
CC pressor effects. It does not bind to type-1 angiotensin-2 receptor
CC (AGTR1) (PubMed:17475904). It does not bind to the muscarinic
CC acetylcholine receptor M3 (CHRM3) (PubMed:20814884).
CC {ECO:0000305|PubMed:17475904, ECO:0000305|PubMed:20814884}.
CC -!- SIMILARITY: Belongs to the bradykinin-potentiating peptide family.
CC {ECO:0000305}.
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DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 Direct protein sequencing;
KW G-protein coupled acetylcholine receptor impairing toxin;
KW G-protein coupled receptor impairing toxin; Hypotensive agent;
KW Pyrrolidone carboxylic acid; Secreted; Toxin.
FT PEPTIDE 1..7
FT /note="Bradykinin-potentiating peptide 7a"
FT /evidence="ECO:0000269|PubMed:15245866"
FT /id="PRO_0000292914"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15245866"
SQ SEQUENCE 7 AA; 723 MW; 77776047687AB6B0 CRC64;
QDGPIPP