ID   BPPDA_BOTNU             Reviewed;          13 AA.
AC   P0C7S2;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   29-SEP-2021, entry version 20.
DE   RecName: Full=Bradykinin-potentiating peptide 13a {ECO:0000250|UniProtKB:Q6LEM5};
DE            Short=BPP-13a {ECO:0000250|UniProtKB:Q6LEM5};
DE   AltName: Full=BPP-III {ECO:0000303|PubMed:9588953};
OS   Bothrops neuwiedi (Neuwied's lancehead).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=95648;
RN   [1]
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=9588953; DOI=10.1023/a:1022545020764;
RA   Ferreira L.A.F., Galle A., Raida M., Schrader M., Lebrun I., Habermehl G.;
RT   "Isolation: analysis and properties of three bradykinin-potentiating
RT   peptides (BPP-II, BPP-III, and BPP-V) from Bothrops neuwiedi venom.";
RL   J. Protein Chem. 17:285-289(1998).
RN   [2]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, AND PYROGLUTAMATE FORMATION AT GLN-1.
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).
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.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15912471}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:15912471}.
CC   -!- MASS SPECTROMETRY: Mass=1372; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:9588953};
CC   -!- MASS SPECTROMETRY: Mass=1370.85; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15912471};
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: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.
FT   PEPTIDE         1..13
FT                   /note="Bradykinin-potentiating peptide 13a"
FT                   /evidence="ECO:0000269|PubMed:15912471,
FT                   ECO:0000269|PubMed:9588953"
FT                   /id="PRO_0000343186"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:15912471"
SQ   SEQUENCE   13 AA;  1388 MW;  6824FC97D83D6774 CRC64;
     QGGWPRPGPE IPP