ID   BPPF_AGKPI              Reviewed;          10 AA.
AC   P0C7R6;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   29-SEP-2021, entry version 19.
DE   RecName: Full=Bradykinin-potentiating peptide F;
DE            Short=AppF;
DE            Short=BPP-F;
OS   Agkistrodon piscivorus piscivorus (Eastern cottonmouth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Agkistrodon.
OX   NCBI_TaxID=8716;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, AND PYROGLUTAMATE FORMATION AT GLN-1.
RX   PubMed=8599182; DOI=10.1016/0041-0101(95)00071-s;
RA   Ferreira L.A.F., Moellring T., Lebrun F.L.A.S., Raida M., Znottka R.,
RA   Habermehl G.G.;
RT   "Structure and effects of a kinin potentiating fraction F (AppF) isolated
RT   from Agkistrodon piscivorus piscivorus venom.";
RL   Toxicon 33:1313-1319(1995).
RN   [2]
RP   SYNTHESIS, AND STRUCTURE BY NMR.
RX   PubMed=10082165; DOI=10.1016/s0041-0101(98)00208-6;
RA   Ferreira L.A.F., Auer H., Haslinger E., Fedele C., Habermehl G.G.;
RT   "Spatial structures of the bradykinin potentiating peptide F from
RT   Agkistrodon piscivorus piscivoris venom.";
RL   Toxicon 37:661-676(1999).
CC   -!- FUNCTION: This peptide potentiates the effect of bradykinin on the
CC       isolated guinea-pig ileum, does not potentiate the effects of
CC       bradykinin upon blood pressure and inhibits the angiotensin-converting
CC       enzyme (ACE) from rat plasma. {ECO:0000269|PubMed:8599182}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8599182}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:8599182}.
CC   -!- MASS SPECTROMETRY: Mass=1224.2; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:8599182};
CC   -!- MISCELLANEOUS: Exists in two forms, due to cis-trans isomerization at
CC       Trp-3-Pro-4.
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..10
FT                   /note="Bradykinin-potentiating peptide F"
FT                   /id="PRO_0000343180"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:8599182"
SQ   SEQUENCE   10 AA;  1240 MW;  324F3551F7741773 CRC64;
     QLWPRPHIPP