BKIP_AGKBI
ID BKIP_AGKBI Reviewed; 11 AA.
AC P85025;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 07-APR-2021, entry version 23.
DE RecName: Full=Bradykinin inhibitor peptide;
DE Short=BIP;
OS Agkistrodon bilineatus (Cantil) (Tropical moccasin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Agkistrodon.
OX NCBI_TaxID=8718;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Venom {ECO:0000269|PubMed:16277978};
RX PubMed=16277978; DOI=10.1016/j.bbrc.2005.10.130;
RA Graham R.L.J., Graham C., McClean S., Chen T., O'Rourke M., Hirst D.,
RA Theakston D., Shaw C.;
RT "Identification and functional analysis of a novel bradykinin inhibitory
RT peptide in the venoms of new world crotalinae pit vipers.";
RL Biochem. Biophys. Res. Commun. 338:1587-1592(2005).
CC -!- FUNCTION: Bradykinin inhibitor peptide antagonizes the vasodilatory
CC actions of bradykinin at the B2 bradykinin receptor (BDKRB2).
CC {ECO:0000269|PubMed:16277978}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16277978}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=1063.18; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16277978};
CC -!- SIMILARITY: Belongs to the bradykinin inhibitor peptide family.
CC {ECO:0000305}.
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DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Bradykinin receptor impairing toxin; Direct protein sequencing;
KW G-protein coupled receptor impairing toxin; Secreted; Toxin; Vasoactive.
FT PEPTIDE 1..11
FT /note="Bradykinin inhibitor peptide"
FT /evidence="ECO:0000269|PubMed:16277978"
FT /id="PRO_0000258038"
SQ SEQUENCE 11 AA; 1063 MW; C4423866CAB7687D CRC64;
TPPAGPDVGP R