BRK2_BOMOR
ID BRK2_BOMOR Reviewed; 161 AA.
AC P83059; Q90W15;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2002, sequence version 2.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Kininogen-2;
DE AltName: Full=BOK-2;
DE Contains:
DE RecName: Full=[Thr6]-bradykinin;
DE Contains:
DE RecName: Full=Bradykinin inhibitor peptide DV-28;
DE Short=DV-28 amide;
DE Flags: Precursor;
OS Bombina orientalis (Oriental fire-bellied toad).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Bombinatoridae; Bombina.
OX NCBI_TaxID=8346 {ECO:0000305};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 87-95 AND 115-123,
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Skin, and Skin secretion;
RX PubMed=12217414; DOI=10.1016/s0196-9781(02)00095-5;
RA Chen T., Orr D.F., Bjourson A.J., McClean S., O'Rourke M., Hirst D.G.,
RA Rao P., Shaw C.;
RT "Bradykinins and their precursor cDNAs from the skin of the fire-bellied
RT toad (Bombina orientalis).";
RL Peptides 23:1547-1555(2002).
RN [2]
RP PROTEIN SEQUENCE OF 133-160, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, MASS SPECTROMETRY, DISULFIDE BOND, AND AMIDATION AT VAL-160.
RC TISSUE=Skin secretion;
RX PubMed=20138946; DOI=10.1016/j.peptides.2010.01.016;
RA Wang L., Chen Y., Yang M., Zhou M., Chen T., Sui D.Y., Shaw C.;
RT "Peptide DV-28 amide: An inhibitor of bradykinin-induced arterial smooth
RT muscle relaxation encoded by Bombina orientalis skin kininogen-2.";
RL Peptides 31:979-982(2010).
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 -!- FUNCTION: [Bradykinin inhibitor peptide DV-28]: Inhibits the
CC bradykinin-induced in vitro relaxation of rat arterial smooth muscle
CC and constriction of intestinal smooth muscle. May target bradykinin
CC receptors (BDKRB). {ECO:0000269|PubMed:12217414,
CC ECO:0000269|PubMed:20138946}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12217414,
CC ECO:0000269|PubMed:20138946, ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000269|PubMed:12217414, ECO:0000269|PubMed:20138946}.
CC -!- MASS SPECTROMETRY: [Bradykinin inhibitor peptide DV-28]: Mass=3198.51;
CC Method=MALDI; Note=The measured mass is that of bradykinin inhibitor
CC peptide DV-28.; Evidence={ECO:0000269|PubMed:20138946};
CC -!- SIMILARITY: Belongs to the bradykinin-related peptide family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ347942; CAC70660.1; -; mRNA.
DR AlphaFoldDB; P83059; -.
DR GO; GO:0005576; C:extracellular region; 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; IDA:UniProtKB.
DR GO; GO:0045776; P:negative regulation of blood pressure; IDA:UniProtKB.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IDA:UniProtKB.
DR InterPro; IPR009608; Bradykinin.
DR Pfam; PF06753; Bradykinin; 2.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Bradykinin receptor impairing toxin;
KW Direct protein sequencing; Disulfide bond;
KW G-protein coupled receptor impairing toxin; Repeat; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..161
FT /note="Kininogen-2"
FT /id="PRO_0000003434"
FT PEPTIDE 87..95
FT /note="[Thr6]-bradykinin"
FT /id="PRO_0000003435"
FT PEPTIDE 115..123
FT /note="[Thr6]-bradykinin"
FT /id="PRO_0000003436"
FT PEPTIDE 133..160
FT /note="Bradykinin inhibitor peptide DV-28"
FT /id="PRO_0000401148"
FT MOD_RES 160
FT /note="Valine amide"
FT /evidence="ECO:0000269|PubMed:20138946"
FT DISULFID 150..156
FT /evidence="ECO:0000269|PubMed:20138946"
SQ SEQUENCE 161 AA; 19042 MW; 200A7235C3657AAC CRC64;
MRLWFCLSFF VVLCLEHFPG TLADERNNRD YPIRTHLHGP HIPRNNRDYP IRTHLHGHHI
PRNVPESEEK TEQFLRDLSE ISRLQRRPPG FTPFRGKFHS QSLRDLSEIS RLQRRPPGFT
PFRGKFHSQS LRDMYEIKGF KSAHGRPRVC PPGEQCPIWV G