ID   E2MT2_AMOMA             Reviewed;          76 AA.
AC   E1B242;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Esculentin-2MT2 {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 {ECO:0000312|EMBL:ADM34275.1};
RN   [1] {ECO:0000312|EMBL:ADM34275.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 40-76, FUNCTION,
RP   SUBCELLULAR LOCATION, SYNTHESIS OF 40-76, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND DISULFIDE BOND.
RC   TISSUE=Skin {ECO:0000303|PubMed:24601776}, and
RC   Skin secretion {ECO:0000303|PubMed:24601776};
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. Active against a variety of Gram-
CC       negative and Gram-positive bacterial strains. Active against fungi.
CC       Shows strong hemolytic activity against human erythrocytes.
CC       {ECO:0000269|PubMed:24601776}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255,
CC       ECO:0000269|PubMed:24601776}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:24601776}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Esculentin subfamily. {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HQ128617; ADM34275.1; -; mRNA.
DR   AlphaFoldDB; E1B242; -.
DR   SMR; E1B242; -.
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; IPR012521; Antimicrobial_frog_2.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   Pfam; PF08023; Antimicrobial_2; 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; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..37
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305|PubMed:24601776"
FT                   /id="PRO_0000440082"
FT   PEPTIDE         40..76
FT                   /note="Esculentin-2MT2"
FT                   /evidence="ECO:0000269|PubMed:24601776"
FT                   /id="PRO_0000440083"
FT   DISULFID        70..76
FT                   /evidence="ECO:0000269|PubMed:24601776"
SQ   SEQUENCE   76 AA;  8397 MW;  9AF7D19F295DDDCB CRC64;
     MFTLKKSMLL LFFLGTISLS LCEEERSADE DDGEKEVKRG IFSLIKTAAK FVGKNLLKQA
     GKAGMEHLAC KANNQC