BPP5_BOTNU
ID BPP5_BOTNU Reviewed; 11 AA.
AC P0C7S3;
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 5;
DE Short=BPP-5;
DE AltName: Full=BPP-V;
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).
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.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=1078; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:9588953};
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; Secreted.
FT PEPTIDE 1..11
FT /note="Bradykinin-potentiating peptide 5"
FT /id="PRO_0000343187"
SQ SEQUENCE 11 AA; 1080 MW; 2C8C96C6777775B8 CRC64;
EEGGSPPPVV I