M3H15_BOMMX
ID M3H15_BOMMX Reviewed; 144 AA.
AC Q58T43;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Maximins 3/H15;
DE Contains:
DE RecName: Full=Maximin-3;
DE Contains:
DE RecName: Full=Maximin-H15;
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 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, 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-H15 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; AY849017; AAX50238.1; -; mRNA.
DR AlphaFoldDB; Q58T43; -.
DR SMR; Q58T43; -.
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_0000003112"
FT PEPTIDE 44..70
FT /note="Maximin-3"
FT /id="PRO_0000003113"
FT PROPEP 73..122
FT /evidence="ECO:0000250"
FT /id="PRO_0000003114"
FT PEPTIDE 124..143
FT /note="Maximin-H15"
FT /id="PRO_0000003115"
FT MOD_RES 143
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:15770703"
SQ SEQUENCE 144 AA; 16036 MW; CE812B625495EFF8 CRC64;
MNFKYIVAVS FLIASAYARS VQNDEQSLSQ RDVLEEESLR EIRGIGGKIL SGLKTALKGA
AKELASTYLH RKRTAEEHEV MKRLEAVMRD LDSLDYPEEA SERETRGFNQ DEIANLFTKK
EKRILGPVLG LVGNALGGLL KNLG
