ID   BRK1_PELRI              Reviewed;          16 AA.
AC   P86156;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2018, sequence version 2.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Bradykinin RL-16-1 {ECO:0000303|PubMed:28012108};
DE   Contains:
DE     RecName: Full=Bradykinin RS-14 {ECO:0000303|PubMed:18855342};
DE     AltName: Full=Bradykinin RS-14-2 {ECO:0000303|PubMed:28012108};
DE   Contains:
DE     RecName: Full=Bradykinin RA-11 {ECO:0000303|PubMed:18855342};
DE     AltName: Full=Bradykinin RA-11-2 {ECO:0000303|PubMed:28012108};
DE   Contains:
DE     RecName: Full=Bradykinin RI-10 {ECO:0000303|PubMed:18855342};
DE   Contains:
DE     RecName: Full=Bradykinin {ECO:0000303|PubMed:18855342};
OS   Pelophylax ridibundus (Marsh frog) (Rana ridibunda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX   NCBI_TaxID=8406;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Skin secretion {ECO:0000303|PubMed:28012108};
RX   PubMed=28012108; DOI=10.1007/s00216-016-0143-3;
RA   Samgina T.Y., Artemenko K.A., Bergquist J., Trebse P., Torkar G.,
RA   Tolpina M.D., Lebedev A.T.;
RT   "Differentiation of frogs from two populations belonging to the Pelophylax
RT   esculentus complex by LC-MS/MS comparison of their skin peptidomes.";
RL   Anal. Bioanal. Chem. 409:1951-1961(2017).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-14, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:18855342};
RX   PubMed=18855342; DOI=10.1002/rcm.3759;
RA   Samgina T.Y., Artemenko K.A., Gorshkov V.A., Ogourtsov S.V., Zubarev R.A.,
RA   Lebedev A.T.;
RT   "De novo sequencing of peptides secreted by the skin glands of the
RT   caucasian green frog Rana ridibunda.";
RL   Rapid Commun. Mass Spectrom. 22:3517-3525(2008).
CC   -!- FUNCTION: Induces relaxation of arterial smooth muscle, by targeting
CC       bradykinin receptors (BDKRB). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18855342,
CC       ECO:0000269|PubMed:28012108}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:28012108}.
CC   -!- MASS SPECTROMETRY: [Bradykinin RL-16-1]: Mass=1699.9;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:28012108};
CC   -!- MASS SPECTROMETRY: [Bradykinin RS-14]: Mass=1498.8;
CC       Method=Electrospray; Note=Bradykinin RS-14.;
CC       Evidence={ECO:0000269|PubMed:28012108};
CC   -!- MASS SPECTROMETRY: [Bradykinin RS-14]: Mass=1499; Method=Electrospray;
CC       Note=Bradykinin RS-14.; Evidence={ECO:0000269|PubMed:18855342};
CC   -!- MASS SPECTROMETRY: [Bradykinin RA-11]: Mass=1244; Method=Electrospray;
CC       Note=Bradykinin RA-11.; Evidence={ECO:0000269|PubMed:18855342};
CC   -!- MASS SPECTROMETRY: [Bradykinin RI-10]: Mass=1173; Method=Electrospray;
CC       Note=Bradykinin RI-10.; Evidence={ECO:0000269|PubMed:18855342};
CC   -!- MASS SPECTROMETRY: [Bradykinin]: Mass=1060; Method=Electrospray;
CC       Note=Bradykinin.; Evidence={ECO:0000269|PubMed:18855342};
CC   -!- SIMILARITY: Belongs to the bradykinin-related peptide family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P86156; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Direct protein sequencing;
KW   G-protein coupled receptor impairing toxin; Secreted; Toxin; Vasoactive;
KW   Vasodilator.
FT   PEPTIDE         1..16
FT                   /note="Bradykinin RL-16-1"
FT                   /evidence="ECO:0000269|PubMed:28012108"
FT                   /id="PRO_0000443419"
FT   PEPTIDE         1..14
FT                   /note="Bradykinin RS-14"
FT                   /evidence="ECO:0000269|PubMed:18855342,
FT                   ECO:0000269|PubMed:28012108"
FT                   /id="PRO_0000361079"
FT   PEPTIDE         1..11
FT                   /note="Bradykinin RA-11"
FT                   /evidence="ECO:0000269|PubMed:18855342"
FT                   /id="PRO_0000361080"
FT   PEPTIDE         1..10
FT                   /note="Bradykinin RI-10"
FT                   /evidence="ECO:0000269|PubMed:18855342"
FT                   /id="PRO_0000361081"
FT   PEPTIDE         1..9
FT                   /note="Bradykinin"
FT                   /evidence="ECO:0000269|PubMed:18855342"
FT                   /id="PRO_0000361082"
SQ   SEQUENCE   16 AA;  1700 MW;  A64EF3344EB38513 CRC64;
     RPPGFSPFRI APASSL