M9H3_BOMMX
ID M9H3_BOMMX Reviewed; 144 AA.
AC Q58T55;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Maximins 9/H3;
DE Contains:
DE RecName: Full=Maximin-9;
DE Contains:
DE RecName: Full=Maximin-H3;
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 TYR-70 AND 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 124-143, AMIDATION AT ILE-143, FUNCTION OF MAXIMIN-H3,
RP AND MASS SPECTROMETRY.
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-9 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-H3 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. {ECO:0000269|PubMed:11835991}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC -!- MASS SPECTROMETRY: [Maximin-H3]: Mass=1944; Method=FAB;
CC Evidence={ECO:0000269|PubMed:11835991};
CC -!- SIMILARITY: Belongs to the bombinin family. {ECO:0000305}.
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DR EMBL; AY848989; AAX50210.1; -; mRNA.
DR EMBL; AY849005; AAX50226.1; -; mRNA.
DR AlphaFoldDB; Q58T55; -.
DR SMR; Q58T55; -.
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_0000003216"
FT PEPTIDE 44..70
FT /note="Maximin-9"
FT /id="PRO_0000003217"
FT PROPEP 74..123
FT /evidence="ECO:0000269|PubMed:11835991"
FT /id="PRO_0000003218"
FT PEPTIDE 124..143
FT /note="Maximin-H3"
FT /id="PRO_0000003219"
FT MOD_RES 70
FT /note="Tyrosine amide"
FT /evidence="ECO:0000269|PubMed:15770703"
FT MOD_RES 143
FT /note="Isoleucine amide"
FT /evidence="ECO:0000269|PubMed:11835991,
FT ECO:0000269|PubMed:15770703"
SQ SEQUENCE 144 AA; 16228 MW; C3D0FF161F650DAE CRC64;
MNFKYIVAVS FLIASAYARS VKNDEQSLSQ RDVLEEESLR EIRGIGRKFL GGVKTTFRCG
VKDFASKHLY GKRTAEEHEV MKRLEAIMRD LDSLDHPEEA SERETRGFNQ DEIANLFTKK
EKRILGPVLG LVGNALGGLI KKIG
