ID   M3H16_BOMMX             Reviewed;         144 AA.
AC   Q58T40;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Maximins 3/H16;
DE   Contains:
DE     RecName: Full=Maximin-3;
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 [MRNA], PROTEIN SEQUENCE OF 44-70 AND 124-143,
RP   AMIDATION AT ILE-143, AND MASS SPECTROMETRY.
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).
RN   [2]
RP   PROTEIN SEQUENCE OF 44-70, MASS SPECTROMETRY, AND FUNCTION OF MAXIMIN-3.
RX   PubMed=11835991; DOI=10.1016/s0196-9781(01)00641-6;
RA   Lai R., Zheng Y.-T., Shen J.-H., Liu G.-J., Liu H., Lee W.-H., Tang S.-Z.,
RA   Zhang Y.;
RT   "Antimicrobial peptides from skin secretions of Chinese red belly toad
RT   Bombina maxima.";
RL   Peptides 23:427-435(2002).
CC   -!- FUNCTION: Maximin-3 shows antibacterial activity against both Gram-
CC       positive and Gram-negative bacteria. It shows also antimicrobial
CC       activity against the fungus C.albicans, but not against A.flavus nor
CC       P.uticale. It has little hemolytic activity. It possess a significant
CC       cytotoxicity against tumor cell lines. It possess a significant anti-
CC       HIV activity. It shows high spermicidal activity.
CC       {ECO:0000269|PubMed:11835991}.
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   -!- MASS SPECTROMETRY: [Maximin-3]: Mass=2698; Method=FAB;
CC       Evidence={ECO:0000269|PubMed:11835991};
CC   -!- SIMILARITY: Belongs to the bombinin family. {ECO:0000305}.
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DR   EMBL; AY849020; AAX50241.1; -; mRNA.
DR   AlphaFoldDB; Q58T40; -.
DR   SMR; Q58T40; -.
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:0000269|PubMed:11835991"
FT                   /id="PRO_0000003116"
FT   PEPTIDE         44..70
FT                   /note="Maximin-3"
FT                   /id="PRO_0000003117"
FT   PROPEP          73..122
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000003118"
FT   PEPTIDE         124..143
FT                   /note="Maximin-H16"
FT                   /id="PRO_0000003119"
FT   MOD_RES         143
FT                   /note="Isoleucine amide"
FT                   /evidence="ECO:0000269|PubMed:15770703"
SQ   SEQUENCE   144 AA;  16080 MW;  CE865C1253E5FEBC CRC64;
     MNFKYIVAVS FLIASAYARS VQNDEQSLSQ RDVLEEESLR EIRGIGGKIL SGLKTALKGA
     AKELASTYLH RKRTAEEHEV MKRLEAVMRD LDSLDYPEEA SERETRGFNQ DEIANLFTKK
     EKRILGPVLS LVGNALGGLI KKIG