ID   BMNL5_BOMOR             Reviewed;         132 AA.
AC   A0A219CMY0;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2017, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=Bombinin-like peptides {ECO:0000303|PubMed:29098406};
DE   Contains:
DE     RecName: Full=Bombinin-BO1 {ECO:0000303|PubMed:29098406};
DE   Contains:
DE     RecName: Full=Bombinin H-BO1 {ECO:0000303|PubMed:29098406};
DE   Flags: Precursor;
GN   Name=BLP8-BH9 {ECO:0000312|EMBL:SJN60137.1};
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:0000312|EMBL:SJN60137.1};
RN   [1] {ECO:0000312|EMBL:SJN60137.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 44-68 AND 115-131,
RP   FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AMIDATION AT PHE-68 AND
RP   LEU-131, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Skin secretion {ECO:0000303|PubMed:29098406};
RX   PubMed=29098406; DOI=10.1007/s00726-017-2509-z;
RA   Peng X., Zhou C., Hou X., Liu Y., Wang Z., Peng X., Zhang Z., Wang R.,
RA   Kong D.;
RT   "Molecular characterization and bioactivity evaluation of two novel
RT   bombinin peptides from the skin secretion of Oriental fire-bellied toad,
RT   Bombina orientalis.";
RL   Amino Acids 50:241-253(2018).
CC   -!- FUNCTION: [Bombinin-BO1]: Has antimicrobial activity against Gram-
CC       negative bacterium E.coli (MIC=26.3 uM), Gram-positive bacterium
CC       S.aureus (MIC=26.3 uM) and yeast C.albicans (MIC=52.5 uM). Has moderate
CC       hemolytic activity towards human erythrocytes at a concentration of
CC       52.2 uM. {ECO:0000269|PubMed:29098406}.
CC   -!- FUNCTION: [Bombinin H-BO1]: Has no antimicrobial activity at
CC       concentrations up to 161 uM. Has moderate hemolytic activity towards
CC       human erythrocytes at a concentration of 40.3 uM.
CC       {ECO:0000269|PubMed:29098406}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255,
CC       ECO:0000269|PubMed:29098406}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:29098406}.
CC   -!- MASS SPECTROMETRY: [Bombinin-BO1]: Mass=2437.89; Method=Electrospray;
CC       Note=Bombinin-BO1.; Evidence={ECO:0000269|PubMed:29098406};
CC   -!- MASS SPECTROMETRY: [Bombinin H-BO1]: Mass=1589.02; Method=Electrospray;
CC       Note=Bombinin H-BO1.; Evidence={ECO:0000269|PubMed:29098406};
CC   -!- SIMILARITY: Belongs to the bombinin family. {ECO:0000255}.
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DR   EMBL; LT732575; SJN60137.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A219CMY0; -.
DR   SMR; A0A219CMY0; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0051715; P:cytolysis in another organism; IDA:UniProtKB.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR   InterPro; IPR007962; Bombinin.
DR   Pfam; PF05298; Bombinin; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Cytolysis; Direct protein sequencing;
KW   Fungicide; Hemolysis; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..42
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000443728"
FT   PEPTIDE         44..68
FT                   /note="Bombinin-BO1"
FT                   /evidence="ECO:0000269|PubMed:29098406"
FT                   /id="PRO_0000443729"
FT   PROPEP          72..112
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000443730"
FT   PEPTIDE         115..131
FT                   /note="Bombinin H-BO1"
FT                   /evidence="ECO:0000269|PubMed:29098406"
FT                   /id="PRO_0000443731"
FT   MOD_RES         68
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:29098406"
FT   MOD_RES         131
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:29098406"
SQ   SEQUENCE   132 AA;  14598 MW;  01326222B8CB78FB CRC64;
     MNFKYIIAVS FLIASAYARS EEYDIQSLSQ RDVLEEESLR KIRGIGSAIL SAGKSIIKGL
     AKGLAEHFGK RTAEDHEVMK RLEAAMRDLD SLDYPEEASE RETRGFNQEE KEKRIIGPVL
     GLVGKALGGL LG