BRK1C_BOMMX
ID BRK1C_BOMMX Reviewed; 152 AA.
AC Q90W88;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 21-NOV-2003, sequence version 2.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Kininogen-1c;
DE AltName: Full=BMK-1;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF MAXIMAKININ, AND SYNTHESIS
RP OF MAXIMAKININ.
RC TISSUE=Skin secretion;
RX PubMed=12948837; DOI=10.1016/s0196-9781(03)00167-0;
RA Chen T., Bjourson A.J., McClean S., Orr D.F., O'Kane E.J., Rao P., Shaw C.;
RT "Cloning of maximakinin precursor cDNAs from Chinese toad, Bombina maxima,
RT venom.";
RL Peptides 24:853-861(2003).
CC -!- FUNCTION: Potent vasodilator. Binds B1 (BDKRB1) and B2 (BDKRB2)
CC bradykinin receptors.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC -!- SIMILARITY: Belongs to the bradykinin-related peptide family.
CC {ECO:0000305}.
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DR EMBL; AJ315488; CAC48026.2; -; mRNA.
DR AlphaFoldDB; Q90W88; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
DR InterPro; IPR009608; Bradykinin.
DR Pfam; PF06753; Bradykinin; 4.
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 Repeat; Secreted; Signal; Toxin; Vasoactive; Vasodilator.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..152
FT /note="Kininogen-1c"
FT /id="PRO_0000003416"
FT PEPTIDE 41..59
FT /note="Maximakinin"
FT /evidence="ECO:0000269|PubMed:12948837"
FT /id="PRO_0000003417"
FT PEPTIDE 51..59
FT /note="Bradykinin"
FT /evidence="ECO:0000269|PubMed:12948837"
FT /id="PRO_0000003418"
FT PEPTIDE 69..87
FT /note="Maximakinin"
FT /evidence="ECO:0000269|PubMed:12948837"
FT /id="PRO_0000003419"
FT PEPTIDE 79..87
FT /note="Bradykinin"
FT /evidence="ECO:0000269|PubMed:12948837"
FT /id="PRO_0000003420"
FT PEPTIDE 97..115
FT /note="Maximakinin"
FT /evidence="ECO:0000269|PubMed:12948837"
FT /id="PRO_0000003421"
FT PEPTIDE 107..115
FT /note="Bradykinin"
FT /evidence="ECO:0000269|PubMed:12948837"
FT /id="PRO_0000003422"
FT PEPTIDE 125..143
FT /note="Maximakinin"
FT /evidence="ECO:0000269|PubMed:12948837"
FT /id="PRO_0000003423"
FT PEPTIDE 135..143
FT /note="Bradykinin"
FT /evidence="ECO:0000269|PubMed:12948837"
FT /id="PRO_0000003424"
FT REGION 28..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 152 AA; 17604 MW; B58B31389D837686 CRC64;
MRLWFCLSLF IVLCLEHFPG TLADERNVPE SEEKTEQFLR DLPKINRKGP RPPGFSPFRG
KFHSQTLRDL PKINRKGPRP PGFSPFRGKF HSQTLRDLPK INRKGPRPPG FSPFRGKFHS
QSLRDLPKIN RKGPRPPGFS PFRGKFHSQS HV