M1H1_BOMMX
ID M1H1_BOMMX Reviewed; 144 AA.
AC P83080; P83085; Q58T88;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Maximins 1/H1;
DE Contains:
DE RecName: Full=Maximin-1;
DE Contains:
DE RecName: Full=Maximin-H1;
DE AltName: Full=Maximin-6;
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] {ECO:0000312|EMBL:AAK63254.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 44-70 AND 124-143,
RP AMIDATION AT ASN-70 AND LEU-143, FUNCTION OF MAXIMIN-1 AND MAXIMIN-H1, MASS
RP SPECTROMETRY, AND TOXIC DOSE.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT ASN-70 AND 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 [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 44-70, FUNCTION OF MAXIMIN-1 AND MAXIMIN-H1,
RP SUBCELLULAR LOCATION, AND 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.
CC -!- FUNCTION: Maximin-1 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 does not possess a
CC significant anti-HIV activity. It shows high spermicidal activity.
CC {ECO:0000269|Ref.3}.
CC -!- FUNCTION: Maximin-H1 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|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-1]: Mass=2674; Method=FAB;
CC Evidence={ECO:0000269|PubMed:11835991};
CC -!- MASS SPECTROMETRY: [Maximin-H1]: Mass=1933; Method=FAB;
CC Evidence={ECO:0000269|PubMed:11835991};
CC -!- TOXIC DOSE: LD(50) is 8.2 mg/kg by intraperitoneal injection into mice.
CC {ECO:0000269|PubMed:11835991}.
CC -!- SIMILARITY: Belongs to the bombinin family. {ECO:0000255}.
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DR EMBL; AF378904; AAK63254.1; -; mRNA.
DR EMBL; AY848972; AAX50193.1; -; mRNA.
DR PDB; 7OVZ; NMR; -; M=44-70.
DR PDBsum; 7OVZ; -.
DR AlphaFoldDB; P83080; -.
DR SMR; P83080; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
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 3D-structure; Amidation; Amphibian defense peptide; Antibiotic;
KW Antimicrobial; Cleavage on pair of basic residues; Cytolysis;
KW Direct protein sequencing; Fungicide; Hemolysis; Secreted; Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..43
FT /evidence="ECO:0000255, ECO:0000269|Ref.3"
FT /id="PRO_0000003080"
FT PEPTIDE 44..70
FT /note="Maximin-1"
FT /evidence="ECO:0000269|Ref.3"
FT /id="PRO_0000003081"
FT PROPEP 74..123
FT /evidence="ECO:0000269|PubMed:11835991"
FT /id="PRO_0000003082"
FT PEPTIDE 124..143
FT /note="Maximin-H1"
FT /id="PRO_0000003083"
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="Leucine amide"
FT /evidence="ECO:0000269|PubMed:11835991,
FT ECO:0000269|PubMed:15770703"
FT CONFLICT 105
FT /note="T -> S (in Ref. 2; AAX50193)"
FT /evidence="ECO:0000305"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:7OVZ"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:7OVZ"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:7OVZ"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:7OVZ"
SQ SEQUENCE 144 AA; 15976 MW; F770F6870543020E CRC64;
MNFKYIVAVS FLLASAYARS EENDEQSLSQ RDVLEEESLR EIRGIGTKIL GGVKTALKGA
LKELASTYAN GKRTAEEHEV MKRLEAVMRD LDSLDYPEEA AERETRSFNQ EEIANLFTKK
EKRILGPVIS TIGGVLGGLL KNLG
