BRK1A_BOMMX
ID BRK1A_BOMMX Reviewed; 294 AA.
AC Q7T3L1;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Kininogen-1a;
DE Contains:
DE RecName: Full=Maximakinin;
DE AltName: Full=Bombinakinin M;
DE Contains:
DE RecName: Full=Bradykinin;
DE Contains:
DE RecName: Full=Bombinakinin-GAP;
DE AltName: Full=Bombinakinin M gene-associated protein;
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:AAP47179.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 265-292, SYNTHESIS OF
RP 265-292, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP SPECTROMETRY, DISULFIDE BOND, AND AMIDATION AT VAL-292.
RC TISSUE=Skin secretion {ECO:0000269|PubMed:12668203};
RX PubMed=12668203; DOI=10.1016/s0196-9781(03)00027-5;
RA Lai R., Liu H., Lee W.H., Zhang Y.;
RT "Bombinakinin M gene associated peptide, a novel bioactive peptide from
RT skin secretions of the toad Bombina maxima.";
RL Peptides 24:199-204(2003).
RN [2]
RP SYNTHESIS OF 265-292, AND FUNCTION.
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: [Bombinakinin-GAP]: Plays a role in the control of feeding by
CC the brain; intracerebroventricular administration of the peptide
CC induced significant decrease in food intake in rats. Inhibits the
CC bradykinin-induced in vitro relaxation of rat arterial smooth muscle.
CC May target bradykinin receptors (BDKRB). {ECO:0000269|PubMed:12668203,
CC ECO:0000269|PubMed:20138946}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12668203}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000269|PubMed:12668203}.
CC -!- MASS SPECTROMETRY: [Bombinakinin-GAP]: Mass=3228; Mass_error=0.4;
CC Method=FAB; Evidence={ECO:0000269|PubMed:12668203};
CC -!- SIMILARITY: Belongs to the bradykinin-related peptide family.
CC {ECO:0000305}.
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DR EMBL; AF515613; AAP47179.1; -; mRNA.
DR AlphaFoldDB; Q7T3L1; -.
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:0042755; P:eating behavior; IDA:UniProtKB.
DR GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
DR InterPro; IPR009608; Bradykinin.
DR Pfam; PF06753; Bradykinin; 8.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond;
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..294
FT /note="Kininogen-1a"
FT /evidence="ECO:0000255"
FT /id="PRO_0000003385"
FT PEPTIDE 41..59
FT /note="Maximakinin"
FT /evidence="ECO:0000250|UniProtKB:Q90W88"
FT /id="PRO_0000003386"
FT PEPTIDE 51..66
FT /note="Bradykinin"
FT /evidence="ECO:0000250|UniProtKB:Q90W88"
FT /id="PRO_0000003387"
FT PEPTIDE 69..87
FT /note="Maximakinin"
FT /evidence="ECO:0000250|UniProtKB:Q90W88"
FT /id="PRO_0000003388"
FT PEPTIDE 79..94
FT /note="Bradykinin"
FT /evidence="ECO:0000250|UniProtKB:Q90W88"
FT /id="PRO_0000003389"
FT PEPTIDE 97..115
FT /note="Maximakinin"
FT /evidence="ECO:0000250|UniProtKB:Q90W88"
FT /id="PRO_0000003390"
FT PEPTIDE 107..122
FT /note="Bradykinin"
FT /evidence="ECO:0000250|UniProtKB:Q90W88"
FT /id="PRO_0000003391"
FT PEPTIDE 125..143
FT /note="Maximakinin"
FT /evidence="ECO:0000250|UniProtKB:Q90W88"
FT /id="PRO_0000003392"
FT PEPTIDE 135..150
FT /note="Bradykinin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000003393"
FT PEPTIDE 153..171
FT /note="Maximakinin"
FT /evidence="ECO:0000250|UniProtKB:Q90W88"
FT /id="PRO_0000003394"
FT PEPTIDE 163..178
FT /note="Bradykinin"
FT /evidence="ECO:0000250|UniProtKB:Q90W88"
FT /id="PRO_0000003395"
FT PEPTIDE 181..199
FT /note="Maximakinin"
FT /evidence="ECO:0000250|UniProtKB:Q90W88"
FT /id="PRO_0000003396"
FT PEPTIDE 191..206
FT /note="Bradykinin"
FT /evidence="ECO:0000250|UniProtKB:Q90W88"
FT /id="PRO_0000003397"
FT PEPTIDE 209..227
FT /note="Maximakinin"
FT /evidence="ECO:0000250|UniProtKB:Q90W88"
FT /id="PRO_0000003398"
FT PEPTIDE 219..234
FT /note="Bradykinin"
FT /evidence="ECO:0000250|UniProtKB:Q90W88"
FT /id="PRO_0000003399"
FT PEPTIDE 237..255
FT /note="Maximakinin"
FT /evidence="ECO:0000250|UniProtKB:Q90W88"
FT /id="PRO_0000003400"
FT PEPTIDE 247..262
FT /note="Bradykinin"
FT /evidence="ECO:0000250|UniProtKB:Q90W88"
FT /id="PRO_0000003401"
FT PEPTIDE 265..292
FT /note="Bombinakinin-GAP"
FT /evidence="ECO:0000269|PubMed:12668203"
FT /id="PRO_0000003402"
FT REGION 28..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..257
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"
FT MOD_RES 292
FT /note="Valine amide"
FT /evidence="ECO:0000269|PubMed:12668203"
FT DISULFID 282..288
FT /evidence="ECO:0000269|PubMed:12668203"
SQ SEQUENCE 294 AA; 33857 MW; 7C87B4D88482C530 CRC64;
MRLWFCLSFF IVLCLEHFTG TLADERNVPE SEEKTEQFLR DLPKINRKGP RPPGFSPFRG
KFHSQSLRDL PKINRKGPRP PGFSPFRGKF HSQSLRDLPK INRKGPRPPG FSPFRGKFHS
QSLRDLPKIN RKGPRPPGFS PFRGKFHSQS LRDLPKINRK GPRPPGFSPF RGKFHSQSLR
DLPKINRKGP RPPGFSPFRG KFHSQSLRDL PKINRKGPRP PGFSPFRGKF HSQSLRDLPK
INRKGPRPPG FSPFRGKFHS QSLRDMYEIK QYKTAHGRPP ICAPGEQCPI WVGK