ID   BRKC_CYPDO              Reviewed;          11 AA.
AC   P83659;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2013, sequence version 2.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Cyphokinin {ECO:0000303|PubMed:19716363};
DE   AltName: Full=Bradykinin-related peptide {ECO:0000303|PubMed:19716363};
DE   Contains:
DE     RecName: Full=Thr6-bradykinin {ECO:0000303|PubMed:11306139, ECO:0000303|PubMed:19716363};
DE              Short=Thr6-BK {ECO:0000303|PubMed:11306139, ECO:0000303|PubMed:19716363};
OS   Cyphononyx dorsalis (Spider wasp) (Cyphononyx fulvognathus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Pompiloidea;
OC   Pompilidae; Pepsinae; Cyphononyx.
OX   NCBI_TaxID=246266;
RN   [1]
RP   PROTEIN SEQUENCE, SYNTHESIS, FUNCTION, BIOASSAY, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=19716363; DOI=10.1016/j.bcp.2009.08.020;
RA   Picolo G., Hisada M., Moura A.B., Machado M.F., Sciani J.M.,
RA   Conceicao I.M., Melo R.L., Oliveira V., Lima-Landman M.T., Cury Y.,
RA   Konno K., Hayashi M.A.;
RT   "Bradykinin-related peptides in the venom of the solitary wasp Cyphononyx
RT   fulvognathus.";
RL   Biochem. Pharmacol. 79:478-486(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 3-11, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=11306139; DOI=10.1016/s0041-0101(00)00262-2;
RA   Konno K., Hisada M., Naoki H., Itagaki Y., Yasuhara T., Juliano M.A.,
RA   Juliano L., Palma M.S., Yamane T., Nakajima T.;
RT   "Isolation and sequence determination of peptides in the venom of the
RT   spider wasp (Cyphononyx dorsalis) guided by matrix-assisted laser
RT   desorption/ionization time of flight (MALDI-TOF) mass spectrometry.";
RL   Toxicon 39:1257-1260(2001).
RN   [3]
RP   REVIEW.
RX   PubMed=27096870; DOI=10.3390/toxins8040114;
RA   Konno K., Kazuma K., Nihei K.;
RT   "Peptide toxins in solitary wasp venoms.";
RL   Toxins 8:114-114(2016).
CC   -!- FUNCTION: [Cyphokinin]: Inhibits angiotensin-converting enzyme (ACE)
CC       with a Ki of 2.2 uM and targets B2 bradykinin receptor (BDKRB2). Also
CC       provokes contraction of smooth muscle preparation (ileum). In vivo,
CC       induces hyperalgesic effects in living rats after intraplantar
CC       injection. {ECO:0000269|PubMed:19716363}.
CC   -!- FUNCTION: [Thr6-bradykinin]: Inhibits ACE with a Ki of 1.6 uM, and
CC       targets B2 bradykinin receptor (BDKRB2). Provokes contraction of smooth
CC       muscle preparation (ileum). In vivo, induces an early hyperalgesic
CC       effects in living rats after intraplantar injection.
CC       {ECO:0000269|PubMed:19716363}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11306139}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:11306139}.
CC   -!- MASS SPECTROMETRY: [Cyphokinin]: Mass=1290.6; Method=MALDI;
CC       Note=Monoisotopic mass.; Evidence={ECO:0000269|PubMed:19716363};
CC   -!- MASS SPECTROMETRY: [Thr6-bradykinin]: Mass=1074.58; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11306139};
CC   -!- MISCELLANEOUS: Cyphokinin is hydrolyzed by ACE by only 27.3% (compared
CC       to bradykinin). {ECO:0000305|PubMed:19716363}.
CC   -!- MISCELLANEOUS: [Thr6]-bradykinin is hydrolyzed by ACE by only 22.7%
CC       (compared to bradykinin). {ECO:0000305|PubMed:19716363}.
CC   -!- SIMILARITY: Belongs to the bradykinin-related peptide family.
CC       {ECO:0000305}.
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DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IEA:InterPro.
DR   GO; GO:0045776; P:negative regulation of blood pressure; ISS:UniProtKB.
DR   GO; GO:0045987; P:positive regulation of smooth muscle contraction; ISS:UniProtKB.
DR   InterPro; IPR009608; Bradykinin.
DR   Pfam; PF06753; Bradykinin; 1.
PE   1: Evidence at protein level;
KW   Bradykinin receptor impairing toxin; Direct protein sequencing;
KW   G-protein coupled receptor impairing toxin; Secreted; Toxin.
FT   PEPTIDE         1..11
FT                   /note="Cyphokinin"
FT                   /evidence="ECO:0000269|PubMed:19716363"
FT                   /id="PRO_0000424140"
FT   PEPTIDE         3..11
FT                   /note="Thr6-bradykinin"
FT                   /evidence="ECO:0000269|PubMed:11306139"
FT                   /id="PRO_0000043521"
SQ   SEQUENCE   11 AA;  1290 MW;  33D38725A9C86777 CRC64;
     DTRPPGFTPF R