ID   BMNH1_BOMVA             Reviewed;          21 AA.
AC   P82282; P82283;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Bombinin-H1/H3;
OS   Bombina variegata (Yellow-bellied toad).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Bombinatoridae; Bombina.
OX   NCBI_TaxID=8348;
RN   [1]
RP   PROTEIN SEQUENCE, D-AMINO ACID AT ILE-2, AND AMIDATION AT ILE-20.
RC   TISSUE=Skin secretion;
RX   PubMed=8223491; DOI=10.1002/j.1460-2075.1993.tb06172.x;
RA   Mignogna G., Simmaco M., Kreil G., Barra D.;
RT   "Antibacterial and haemolytic peptides containing D-alloisoleucine from the
RT   skin of Bombina variegata.";
RL   EMBO J. 12:4829-4832(1993).
CC   -!- FUNCTION: Has antimicrobial and hemolytic activities.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC   -!- SIMILARITY: Belongs to the bombinin family. {ECO:0000305}.
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DR   PIR; B44581; B44581.
DR   AlphaFoldDB; P82282; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial; Cytolysis;
KW   D-amino acid; Direct protein sequencing; Hemolysis; Secreted.
FT   PEPTIDE         1..20
FT                   /note="Bombinin-H1/H3"
FT                   /id="PRO_0000003077"
FT   MOD_RES         2
FT                   /note="D-allo-isoleucine; in form H3"
FT                   /evidence="ECO:0000269|PubMed:8223491"
FT   MOD_RES         20
FT                   /note="Isoleucine amide"
FT                   /evidence="ECO:0000269|PubMed:8223491"
SQ   SEQUENCE   21 AA;  1994 MW;  08C7281E1BDAB6BD CRC64;
     IIGPVLGMVG SALGGLLKKI G