BRK2_PELRI
ID BRK2_PELRI Reviewed; 11 AA.
AC P86157;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 23-FEB-2022, entry version 22.
DE RecName: Full=[Thr6]-bradykinin RA-11 {ECO:0000303|PubMed:18855342};
DE Contains:
DE RecName: Full=[Thr6]-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] {ECO:0000305}
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Skin secretion {ECO:0000303|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).
RN [2]
RP PROTEIN SEQUENCE OF 1-9, 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).
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 (By similarity).
CC {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: [[Thr6]-bradykinin RA-11]: Mass=1258;
CC Method=Electrospray; Note=[Thr6]-Bradykinin RA-11.;
CC Evidence={ECO:0000269|PubMed:18855342};
CC -!- MASS SPECTROMETRY: [[Thr6]-bradykinin]: Mass=1073; Method=Electrospray;
CC Note=[Thr6]-Bradykinin.; Evidence={ECO:0000269|PubMed:18855342};
CC -!- MASS SPECTROMETRY: [[Thr6]-bradykinin]: Mass=1073.6;
CC Method=Electrospray; Note=[Thr6]-Bradykinin.;
CC Evidence={ECO:0000269|PubMed:28012108};
CC -!- SIMILARITY: Belongs to the bradykinin-related peptide family.
CC {ECO:0000305}.
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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.
PE 1: Evidence at protein level;
KW Amphibian defense peptide; Bradykinin receptor impairing toxin;
KW Direct protein sequencing; G-protein coupled receptor impairing toxin;
KW Secreted; Toxin.
FT PEPTIDE 1..11
FT /note="[Thr6]-bradykinin RA-11"
FT /evidence="ECO:0000269|PubMed:18855342"
FT /id="PRO_0000361083"
FT PEPTIDE 1..9
FT /note="[Thr6]-bradykinin"
FT /evidence="ECO:0000269|PubMed:18855342,
FT ECO:0000269|PubMed:28012108"
FT /id="PRO_0000361084"
SQ SEQUENCE 11 AA; 1258 MW; 33851393D771A9C8 CRC64;
RPPGFTPFRI A