BRK1_BOMVA
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
RC Skin secretion {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=2300.0;
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