ID   MYH16_BOMMX             Reviewed;         142 AA.
AC   Q58T93;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Maximins y/H16;
DE   Contains:
DE     RecName: Full=Maximin-y;
DE   Contains:
DE     RecName: Full=Maximin-H16;
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 [GENOMIC DNA], AND AMIDATION AT ILE-141.
RC   TISSUE=Skin;
RX   PubMed=15770703; DOI=10.1002/eji.200425615;
RA   Lee W.-H., Li Y., Lai R., Li S., Zhang Y., Wang W.;
RT   "Variety of antimicrobial peptides in the Bombina maxima toad and evidence
RT   of their rapid diversification.";
RL   Eur. J. Immunol. 35:1220-1229(2005).
CC   -!- FUNCTION: Maximin-y shows antimicrobial activity against bacteria and
CC       against the fungus C.albicans. It has little hemolytic activity (By
CC       similarity). {ECO:0000250}.
CC   -!- FUNCTION: Maximin-H16 shows antimicrobial activity against bacteria and
CC       against the fungus C.albicans. Shows strong hemolytic activity (By
CC       similarity). {ECO:0000250}.
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   EMBL; AY847751; AAX50245.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q58T93; -.
DR   SMR; Q58T93; -.
DR   PRIDE; Q58T93; -.
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:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
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; Fungicide; Hemolysis;
KW   Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..43
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000003240"
FT   PEPTIDE         44..68
FT                   /note="Maximin-y"
FT                   /id="PRO_0000003241"
FT   PROPEP          72..121
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000003242"
FT   PEPTIDE         122..141
FT                   /note="Maximin-H16"
FT                   /id="PRO_0000003243"
FT   MOD_RES         68
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         141
FT                   /note="Isoleucine amide"
FT                   /evidence="ECO:0000269|PubMed:15770703"
SQ   SEQUENCE   142 AA;  15624 MW;  7D374A9059F54D88 CRC64;
     MNFKYIVAVS FLIASGYARS VKNDEQSLSQ REVLEEESLR EIRGIGGALL SVGKSALKGL
     AKGFAEHFGK RTAEDHEVMK RLEAVIRDLD SLDHPEEASE REARGFNQEE IANLFTKKDK
     RILGPVLSLV GNALGGLIKK IG