ID   M1111_BOMMX             Reviewed;         144 AA.
AC   Q58T51;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Maximins 11/H11;
DE   Contains:
DE     RecName: Full=Maximin-11;
DE   Contains:
DE     RecName: Full=Maximin-H11;
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 44-70 AND 124-143, AND
RP   AMIDATION AT ASN-70 AND ILE-143.
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-11 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-H11 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; AY849009; AAX50230.1; -; mRNA.
DR   AlphaFoldDB; Q58T51; -.
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; Direct protein sequencing;
KW   Fungicide; Hemolysis; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..43
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000003232"
FT   PEPTIDE         44..70
FT                   /note="Maximin-11"
FT                   /id="PRO_0000003233"
FT   PROPEP          74..123
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000003234"
FT   PEPTIDE         124..143
FT                   /note="Maximin-H11"
FT                   /id="PRO_0000003235"
FT   MOD_RES         70
FT                   /note="Asparagine amide"
FT                   /evidence="ECO:0000269|PubMed:15770703"
FT   MOD_RES         143
FT                   /note="Isoleucine amide"
FT                   /evidence="ECO:0000269|PubMed:15770703"
SQ   SEQUENCE   144 AA;  15960 MW;  BE367B6204A4CB58 CRC64;
     MNFKYIVAVS FLIASAYARS EENDEQSLSQ RDVLEEESLR EIRGIGTKII GGLKTAVKGA
     LKELASTYVN GKRTAEDHEV MKRLEAVMRD LDSLDYPEEA SERETRGFNQ EEIANLFTKK
     EKRILGPVLG LVGSALGGLI KKIG