BRK1B_BOMMX
ID BRK1B_BOMMX Reviewed; 208 AA.
AC Q90WZ1;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Kininogen-1b;
DE Contains:
DE RecName: Full=Maximakinin;
DE AltName: Full=Bombinakinin M;
DE Contains:
DE RecName: Full=Bradykinin;
DE Flags: Precursor;
OS Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Bombinatoridae; Bombina.
OX NCBI_TaxID=161274;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAL02326.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 41-59, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Skin secretion {ECO:0000312|EMBL:AAL02326.1};
RX PubMed=11500030; DOI=10.1006/bbrc.2001.5359;
RA Lai R., Liu H., Lee W.H., Zhang Y.;
RT "A novel bradykinin-related peptide from skin secretions of toad Bombina
RT maxima and its precursor containing six identical copies of the final
RT product.";
RL Biochem. Biophys. Res. Commun. 286:259-263(2001).
CC -!- FUNCTION: In vitro, produces constriction of guinea pig ileum smooth
CC muscle. May target bradykinin receptors (BDKRB).
CC {ECO:0000269|PubMed:11500030}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11500030}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000269|PubMed:11500030}.
CC -!- MASS SPECTROMETRY: [Maximakinin]: Mass=2179; Mass_error=0.4;
CC Method=FAB; Evidence={ECO:0000269|PubMed:11500030};
CC -!- SIMILARITY: Belongs to the bradykinin-related peptide family.
CC {ECO:0000305}.
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DR EMBL; AY046319; AAL02326.1; -; mRNA.
DR PIR; JC7755; JC7755.
DR AlphaFoldDB; Q90WZ1; -.
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:0045987; P:positive regulation of smooth muscle contraction; IDA:UniProtKB.
DR GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
DR InterPro; IPR009608; Bradykinin.
DR Pfam; PF06753; Bradykinin; 6.
PE 1: Evidence at protein level;
KW Amphibian defense peptide; Direct protein sequencing;
KW G-protein coupled receptor impairing toxin; Repeat; Secreted; Signal;
KW Toxin; Vasoactive; Vasodilator.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..208
FT /note="Kininogen-1b"
FT /evidence="ECO:0000255"
FT /id="PRO_0000003403"
FT PEPTIDE 41..59
FT /note="Maximakinin"
FT /evidence="ECO:0000269|PubMed:11500030"
FT /id="PRO_0000003404"
FT PEPTIDE 51..59
FT /note="Bradykinin"
FT /evidence="ECO:0000269|PubMed:11500030"
FT /id="PRO_0000003405"
FT PEPTIDE 69..87
FT /note="Maximakinin"
FT /evidence="ECO:0000269|PubMed:11500030"
FT /id="PRO_0000003406"
FT PEPTIDE 79..87
FT /note="Bradykinin"
FT /evidence="ECO:0000269|PubMed:11500030"
FT /id="PRO_0000003407"
FT PEPTIDE 97..115
FT /note="Maximakinin"
FT /evidence="ECO:0000269|PubMed:11500030"
FT /id="PRO_0000003408"
FT PEPTIDE 107..115
FT /note="Bradykinin"
FT /evidence="ECO:0000269|PubMed:11500030"
FT /id="PRO_0000003409"
FT PEPTIDE 125..143
FT /note="Maximakinin"
FT /evidence="ECO:0000269|PubMed:11500030"
FT /id="PRO_0000003410"
FT PEPTIDE 135..143
FT /note="Bradykinin"
FT /evidence="ECO:0000269|PubMed:11500030"
FT /id="PRO_0000003411"
FT PEPTIDE 153..171
FT /note="Maximakinin"
FT /evidence="ECO:0000269|PubMed:11500030"
FT /id="PRO_0000003412"
FT PEPTIDE 163..171
FT /note="Bradykinin"
FT /evidence="ECO:0000269|PubMed:11500030"
FT /id="PRO_0000003413"
FT PEPTIDE 181..199
FT /note="Maximakinin"
FT /evidence="ECO:0000269|PubMed:11500030"
FT /id="PRO_0000003414"
FT PEPTIDE 191..199
FT /note="Bradykinin"
FT /evidence="ECO:0000269|PubMed:11500030"
FT /id="PRO_0000003415"
FT REGION 27..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 208 AA; 24104 MW; 4EA9A7773E22711D CRC64;
MRLWFCLSFF IVLCLEHFPE TLADERNVPE SEEKTEQYLR DLPKINRKGP RPPGFSPFRG
KFHSQSLRDL PKINRKGPRP PGFSPFRGKF HSQSLRDLPK INRKGPRPPG FSPFRGKFHS
QSLRDLPKIN RKGPRPPGFS PFRGKFHSQS LRDLPKINRK GPRPPGFSPF RGKFHSQSLR
DLPKINRKGP RPPGFSPFRG KFHSQSHV