ID   J1MT1_AMOMA             Reviewed;          63 AA.
AC   E1B245;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Jingdongin-1-MT1 {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:ADM34278.1};
RN   [1] {ECO:0000312|EMBL:ADM34278.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 47-63, FUNCTION, SYNTHESIS
RP   OF 40-76, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   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 some Gram-negative and
CC       a variety of Gram-positive bacterial strains. Active against fungus
CC       C.glabrata 090902 but not against C.neoformans 201211. Shows hemolytic
CC       activity against human erythrocytes. {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       Brevinin subfamily. {ECO:0000255}.
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DR   EMBL; HQ128620; ADM34278.1; -; mRNA.
DR   AlphaFoldDB; E1B245; -.
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; 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; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..44
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305|PubMed:24601776"
FT                   /id="PRO_0000440086"
FT   PEPTIDE         47..63
FT                   /note="Jingdongin-1-MT1"
FT                   /evidence="ECO:0000269|PubMed:24601776"
FT                   /id="PRO_0000440087"
FT   DISULFID        57..63
FT                   /evidence="ECO:0000250|UniProtKB:P32412"
SQ   SEQUENCE   63 AA;  7452 MW;  7070AF7705B16C6F CRC64;
     MFTLKKSLLL LFFLGTINLS LCEQERDADE EERRDDDEMD VEVEKRFLPL FLPKIICAIT
     KKC