ID   BR12_AMOMA              Reviewed;          70 AA.
AC   E1B241;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Brevinin-1MT2 {ECO:0000303|PubMed:24601776};
DE   Flags: Precursor;
OS   Amolops mantzorum (Sichuan torrent frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Amolops.
OX   NCBI_TaxID=167930;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 47-70, SUBCELLULAR
RP   LOCATION, DISULFIDE BOND, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Skin, and Skin secretion;
RX   PubMed=24601776; DOI=10.2108/zsj.31.143;
RA   Hu Y., Yu Z., Xu S., Hu Y., Guo C., Li F., Li J., Liu J., Wang H.;
RT   "Peptidomic analysis of antimicrobial peptides in skin secretions of
RT   Amolops mantzorum.";
RL   Zool. Sci. 31:143-151(2014).
CC   -!- FUNCTION: Antimicrobial peptide with activity against a variety of
CC       Gram-negative and Gram-positive bacteria and against fungi (By
CC       similarity). Shows strong hemolytic activity against human erythrocytes
CC       (By similarity). {ECO:0000250|UniProtKB:E1B240}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24601776}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:24601776}.
CC   -!- MISCELLANEOUS: The primary structure of this peptide is identical to
CC       that of Brevinins-ALa (AC A0SN38). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=00860";
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DR   EMBL; HQ128616; ADM34274.1; -; mRNA.
DR   AlphaFoldDB; E1B241; -.
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   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   InterPro; IPR012520; Antimicrobial_frog_1.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   Pfam; PF08018; Antimicrobial_1; 1.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Cytolysis; Direct protein sequencing;
KW   Disulfide bond; Fungicide; Hemolysis; Immunity; Innate immunity; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..44
FT                   /evidence="ECO:0000305|PubMed:24601776"
FT                   /id="PRO_0000440076"
FT   PEPTIDE         47..70
FT                   /note="Brevinin-1MT2"
FT                   /evidence="ECO:0000269|PubMed:24601776"
FT                   /id="PRO_0000440077"
FT   DISULFID        64..70
FT                   /evidence="ECO:0000269|PubMed:24601776"
SQ   SEQUENCE   70 AA;  8189 MW;  5616BDAE077EAD14 CRC64;
     MFTLKKSMLL LFFLGTINLS LCEQERNADE EERRDDDEMD VEVEKRFLPM LAGLAANFLP
     KLFCKITKKC