M5H41_BOMMX
ID M5H41_BOMMX Reviewed; 145 AA.
AC P83084;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Maximins 5/H4 type 1;
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 {ECO:0000312|EMBL:AAK63258.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 44-70 AND 125-144,
RP AMIDATION AT LEU-144, FUNCTION OF MAXIMIN-5 AND MAXIMIN-H4, AND MASS
RP SPECTROMETRY.
RC TISSUE=Skin {ECO:0000269|PubMed:11835991}, and
RC Skin secretion {ECO:0000269|PubMed:11835991};
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT LEU-144.
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 [3]
RP PROTEIN SEQUENCE OF 44-70, FUNCTION OF MAXIMIN-5, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Skin secretion {ECO:0000269|Ref.3};
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.
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 {ECO:0000269|PubMed:11835991, ECO:0000269|Ref.3}.
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. {ECO:0000269|PubMed:11835991, ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.3}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands. {ECO:0000269|Ref.3}.
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:0000255}.
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DR EMBL; AF378908; AAK63258.1; -; mRNA.
DR AlphaFoldDB; P83084; -.
DR SMR; P83084; -.
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:0000255, ECO:0000269|PubMed:11835991,
FT ECO:0000269|Ref.3"
FT /id="PRO_0000003180"
FT PEPTIDE 44..70
FT /note="Maximin-5"
FT /evidence="ECO:0000269|PubMed:11835991, ECO:0000269|Ref.3"
FT /id="PRO_0000003181"
FT PROPEP 74..124
FT /evidence="ECO:0000269|PubMed:11835991, ECO:0000269|Ref.3"
FT /id="PRO_0000003182"
FT PEPTIDE 125..144
FT /note="Maximin-H4"
FT /evidence="ECO:0000269|PubMed:11835991, ECO:0000269|Ref.3"
FT /id="PRO_0000003183"
FT MOD_RES 144
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:11835991,
FT ECO:0000269|PubMed:15770703"
SQ SEQUENCE 145 AA; 16338 MW; CD7A93483196F7E3 CRC64;
MNFKYIVAVS FLIASAYARS VQNDEQSLSQ RDVLEEESLR EIRSIGAKIL GGVKTFFKGA
LKELASTYLQ RKRTAEEQHE VMKRLEAVMR DLDSLDHPEE ASEREIRGFN QEEIANLFTK
KEKRILGPVI SKIGGVLGGL LKNLG
