ID   BRK1_BOMVA              Reviewed;          97 AA.
AC   P83056; Q90W86;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2002, sequence version 2.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Kininogen-1;
DE   AltName: Full=BVK-1;
DE   Contains:
DE     RecName: Full=[Ala3,Thr6]-bradykinin;
DE   Contains:
DE     RecName: Full=Kininogen-1-associated peptide;
DE   Flags: Precursor;
OS   Bombina variegata (Yellow-bellied toad).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Bombinatoridae; Bombina.
OX   NCBI_TaxID=8348;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAC44903.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 51-59, FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Skin {ECO:0000269|PubMed:12230583}, and Skin secretion
RC   {ECO:0000269|PubMed:12230583};
RX   PubMed=12230583; DOI=10.1046/j.1432-1033.2002.03174.x;
RA   Chen T., Orr D.F., Bjourson A.J., McClean S., O'Rourke M., Hirst D.G.,
RA   Rao P., Shaw C.;
RT   "Novel bradykinins and their precursor cDNAs from European yellow-bellied
RT   toad (Bombina variegata) skin.";
RL   Eur. J. Biochem. 269:4693-4700(2002).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 76-97, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:15134346};
RX   PubMed=15134346; DOI=10.1515/bc.2004.027;
RA   Marenah L., Flatt P.R., Orr D.F., McClean S., Shaw C., Abdel-Wahab Y.H.;
RT   "Skin secretion of the toad Bombina variegata contains multiple insulin-
RT   releasing peptides including bombesin and entirely novel insulinotropic
RT   structures.";
RL   Biol. Chem. 385:315-321(2004).
CC   -!- FUNCTION: [Ala3,Thr6]bradykinin: produces in vitro relaxation of rat
CC       arterial smooth muscle and constriction of intestinal smooth muscle.
CC       Possesses insulin-releasing activity. May target bradykinin receptors
CC       (BDKRB). {ECO:0000269|PubMed:12230583, ECO:0000269|PubMed:15134346}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12230583,
CC       ECO:0000269|PubMed:15134346}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:12230583, ECO:0000269|PubMed:15134346}.
CC   -!- MASS SPECTROMETRY: [[Ala3,Thr6]-bradykinin]: Mass=1049.31;
CC       Mass_error=0.08; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:12230583};
CC   -!- MASS SPECTROMETRY: [Kininogen-1-associated peptide]: Mass=2300;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:15134346};
CC   -!- SIMILARITY: Belongs to the bradykinin-related peptide family.
CC       {ECO:0000305}.
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DR   EMBL; AJ320269; CAC44903.1; -; mRNA.
DR   AlphaFoldDB; P83056; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005179; F:hormone activity; NAS:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IDA:UniProtKB.
DR   GO; GO:0045986; P:negative regulation of smooth muscle contraction; IDA:UniProtKB.
DR   GO; GO:0045987; P:positive regulation of smooth muscle contraction; IDA:UniProtKB.
DR   GO; GO:0050796; P:regulation of insulin secretion; IDA:UniProtKB.
DR   GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
DR   InterPro; IPR009608; Bradykinin.
DR   Pfam; PF06753; Bradykinin; 1.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Cleavage on pair of basic residues;
KW   Direct protein sequencing; G-protein coupled receptor impairing toxin;
KW   Repeat; Secreted; Signal; Toxin; Vasoactive; Vasodilator.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..97
FT                   /note="Kininogen-1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003437"
FT   PEPTIDE         51..59
FT                   /note="[Ala3,Thr6]-bradykinin"
FT                   /id="PRO_0000003438"
FT   PEPTIDE         76..97
FT                   /note="Kininogen-1-associated peptide"
FT                   /id="PRO_0000003439"
FT   CONFLICT        95..97
FT                   /note="CKK -> AN (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   97 AA;  11427 MW;  1F038BEFFF0C0908 CRC64;
     MRLWFCLSFL IILCVEHFPG TLAVERNVPE SEEKTEQFLR DLFEISRLQR RPAGFTPFRG
     KFHSQSLRGL SETKRIYNAI WPCKHCNKCK PGLLCKK
//