ID   M5H43_BOMMX             Reviewed;         144 AA.
AC   Q58T61;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Maximins 5/H4 type 3;
DE   Contains:
DE     RecName: Full=Maximin-5;
DE   Contains:
DE     RecName: Full=Maximin-H4;
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], AND AMIDATION AT LEU-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).
RN   [2]
RP   PROTEIN SEQUENCE OF 44-70, FUNCTION OF MAXIMIN-5, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Skin secretion;
RA   Chen T.B., McClean S., Orr D.F., Bjourson A.J., Rao P.F., Shaw C.;
RT   "Isolation and structural characterisation of antimicrobial peptides from
RT   the venom of the Chinese large-webbed bell toad (Bombina maxima).";
RL   Submitted (JUL-2001) to UniProtKB.
RN   [3]
RP   PROTEIN SEQUENCE OF 44-70 AND 124-143, AMIDATION AT LEU-143, FUNCTION OF
RP   MAXIMIN-5 AND MAXIMIN-H4, AND MASS SPECTROMETRY.
RC   TISSUE=Skin, and Skin secretion;
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-5 shows antibacterial activity against both Gram-
CC       positive and Gram-negative bacteria. The only exception is the
CC       resistance of E.coli. Shows also antimicrobial activity against fungi
CC       C.albicans, A.flavus and P.uticale. It has little hemolytic activity.
CC       It does not possess a significant cytotoxicity against tumor cell
CC       lines. It does not possess a significant anti-HIV activity.
CC   -!- FUNCTION: Maximin-H4 shows antibacterial activity against both Gram-
CC       positive and Gram-negative bacteria. It shows also antimicrobial
CC       activity against the fungus C.albicans. Shows strong hemolytic
CC       activity.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands. {ECO:0000269|Ref.2}.
CC   -!- MASS SPECTROMETRY: [Maximin-5]: Mass=2841; Method=FAB;
CC       Evidence={ECO:0000269|PubMed:11835991};
CC   -!- MASS SPECTROMETRY: [Maximin-H4]: Mass=1960; Method=FAB;
CC       Evidence={ECO:0000269|PubMed:11835991};
CC   -!- SIMILARITY: Belongs to the bombinin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY848999; AAX50220.1; -; mRNA.
DR   AlphaFoldDB; Q58T61; -.
DR   SMR; Q58T61; -.
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                   /id="PRO_0000003188"
FT   PEPTIDE         44..70
FT                   /note="Maximin-5"
FT                   /id="PRO_0000003189"
FT   PROPEP          74..123
FT                   /evidence="ECO:0000269|PubMed:11835991"
FT                   /id="PRO_0000003190"
FT   PEPTIDE         124..143
FT                   /note="Maximin-H4"
FT                   /id="PRO_0000003191"
FT   MOD_RES         143
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:11835991,
FT                   ECO:0000269|PubMed:15770703"
SQ   SEQUENCE   144 AA;  16240 MW;  5630EA463DEFC511 CRC64;
     MNFKYIVAVS FLIASAYARS VQNDEQSLSQ RDVLEEESLR EIRSIGAKIL GGVKTFFKGA
     LKELASTYLQ RKRTAEDHEE MKRLEAVMRD LDSLDYPEEA SERETRGFNQ EEIANLFTKK
     EKRILGPVIS KIGGVLGGLL KNLG