ID   BPPAP_BOTFO             Reviewed;          13 AA.
AC   P0DKZ9;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2013, sequence version 1.
DT   29-SEP-2021, entry version 15.
DE   RecName: Full=Bradykinin-potentiating peptide AP;
DE            Short=BPP-AP;
DE   Contains:
DE     RecName: Full=Bradykinin-potentiating peptide 11e;
DE              Short=BPP-11e;
OS   Bothrops fonsecai (Fonseca's lancehead) (Rhinocerophis fonsecai).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=157549;
RN   [1]
RP   PROTEIN SEQUENCE (BPP-AP AND BPP-11E), FUNCTION, PYROGLUTAMATE FORMATION AT
RP   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 (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:22869554}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide AP]: Mass=1356.5;
CC       Method=Electrospray; 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..13
FT                   /note="Bradykinin-potentiating peptide AP"
FT                   /id="PRO_0000421911"
FT   PEPTIDE         1..11
FT                   /note="Bradykinin-potentiating peptide 11e"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000421912"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:22869554"
FT   UNSURE          9
FT                   /note="Assigned by comparison with orthologs"
SQ   SEQUENCE   13 AA;  1375 MW;  EA3890BD21127761 CRC64;
     QARPPHPPIP PAP