ID   BPPBD_BOTJA             Reviewed;          11 AA.
AC   P85161;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   29-SEP-2021, entry version 31.
DE   RecName: Full=Bradykinin-potentiating peptide 11d;
DE            Short=BPP-11d;
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   PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-1, 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).
CC   -!- FUNCTION: This peptide both inhibits the activity of the angiotensin-
CC       converting enzyme (ACE) and enhances the action of bradykinin by
CC       inhibiting the peptidases that inactivate it. It acts as an indirect
CC       hypotensive agent. {ECO:0000269|PubMed:15245866}.
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=1095.3; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15245866};
CC   -!- MASS SPECTROMETRY: Mass=1094.6; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:22869554};
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: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   Direct protein sequencing; Hypotensive agent; Metalloenzyme inhibitor;
KW   Metalloprotease inhibitor; Protease inhibitor; Pyrrolidone carboxylic acid;
KW   Secreted; Toxin.
FT   PEPTIDE         1..11
FT                   /note="Bradykinin-potentiating peptide 11d"
FT                   /evidence="ECO:0000269|PubMed:15245866"
FT                   /id="PRO_0000292920"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:15245866,
FT                   ECO:0000269|PubMed:22869554"
SQ   SEQUENCE   11 AA;  1112 MW;  30BABF1277686777 CRC64;
     QGRPPGPPIP P