M4H31_BOMMX
ID M4H31_BOMMX Reviewed; 144 AA.
AC P83083; Q58T63;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Maximins 4/H3 type 1;
DE Contains:
DE RecName: Full=Maximin-4;
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 {ECO:0000312|EMBL:AAK63257.1};
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAK63257.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 44-70 AND 124-143,
RP AMIDATION AT ASN-70 AND ILE-143, FUNCTION OF MAXIMIN-4 AND MAXIMIN-H3, AND
RP MASS 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 ASN-70 AND ILE-143.
RC TISSUE=Skin {ECO:0000269|PubMed:15770703};
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] {ECO:0000305}
RP PROTEIN SEQUENCE OF 44-70, FUNCTION OF MAXIMIN-4, 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-4 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 does not possess a
CC significant cytotoxicity against tumor cell lines. It does not possess
CC a significant anti-HIV activity.
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, 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-4]: Mass=2612; Method=FAB;
CC Evidence={ECO:0000269|PubMed:11835991};
CC -!- MASS SPECTROMETRY: [Maximin-H3]: Mass=1944; Method=FAB;
CC Evidence={ECO:0000269|PubMed:11835991};
CC -!- SIMILARITY: Belongs to the bombinin family. {ECO:0000255}.
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DR EMBL; AF378907; AAK63257.1; -; mRNA.
DR EMBL; AY848997; AAX50218.1; -; mRNA.
DR EMBL; AY848982; AAX50203.1; -; mRNA.
DR AlphaFoldDB; P83083; -.
DR SMR; P83083; -.
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_0000003152"
FT PEPTIDE 44..70
FT /note="Maximin-4"
FT /evidence="ECO:0000269|PubMed:11835991, ECO:0000269|Ref.3"
FT /id="PRO_0000003153"
FT PROPEP 74..123
FT /evidence="ECO:0000269|PubMed:11835991, ECO:0000269|Ref.3"
FT /id="PRO_0000003154"
FT PEPTIDE 124..143
FT /note="Maximin-H3"
FT /evidence="ECO:0000269|PubMed:11835991, ECO:0000269|Ref.3"
FT /id="PRO_0000003155"
FT MOD_RES 70
FT /note="Asparagine amide"
FT /evidence="ECO:0000269|PubMed:11835991,
FT 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; 15903 MW; 7DD93E668808E5ED CRC64;
MNFKYIIAVS FFIASAYARS EEKDVQSLSQ RDVLEEESLR EIRGIGGVLL SAGKAALKGL
AKVLAEKYAN GKRTAEDHEV MKRLEAVMRD LDSLDHPEEA SERETRGFNQ EEIANLFTKK
EKRILGPVLG LVGNALGGLI KKIG
