ID   JD1_AMOJI               Reviewed;          63 AA.
AC   K7ZGS2;
DT   22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2013, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=Jingdongin-1 {ECO:0000303|PubMed:22828809};
DE   Flags: Precursor;
OS   Amolops jingdongensis (Chinese torrent frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Amolops.
OX   NCBI_TaxID=1077530 {ECO:0000312|EMBL:AFY06638.1};
RN   [1] {ECO:0000312|EMBL:AFY06638.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 47-63, FUNCTION,
RP   SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Skin {ECO:0000303|PubMed:22828809}, and
RC   Skin secretion {ECO:0000303|PubMed:22828809};
RX   PubMed=22828809; DOI=10.1007/s00726-012-1358-z;
RA   He X., Yang S., Wei L., Liu R., Lai R., Rong M.;
RT   "Antimicrobial peptide diversity in the skin of the torrent frog, Amolops
RT   jingdongensis.";
RL   Amino Acids 44:481-487(2013).
CC   -!- FUNCTION: The synthetic peptide has antimicrobial activity against
CC       Gram-negative bacterium B.dysenteriae (MIC=35 ug/ml), against Gram-
CC       positive bacteria S.aureus ATCC 2592 (MIC=4.7 ug/ml) and B.subtilis
CC       ATCC 6633 (MIC=9.38 ug/ml) and against fungus C.albicans (MIC=18.75
CC       ug/ml). Has no activity against Gram-negative bacterium E.coli ATCC
CC       25922 but exhibits low hemolytic activity at concentrations up to 200
CC       ug/ml. {ECO:0000269|PubMed:22828809}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22828809}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:22828809}.
CC   -!- MASS SPECTROMETRY: Mass=1974.6; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:22828809};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000305}.
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DR   EMBL; JQ681300; AFY06638.1; -; mRNA.
DR   AlphaFoldDB; K7ZGS2; -.
DR   TCDB; 1.C.52.1.32; the dermaseptin (dermaseptin) family.
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; IPR004275; Frog_antimicrobial_propeptide.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
DR   PROSITE; PS00387; PPASE; 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   CHAIN           23..63
FT                   /note="Jingdongin-1"
FT                   /id="PRO_0000433604"
FT   PROPEP          23..44
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000433605"
FT   PEPTIDE         47..63
FT                   /note="Jingdongin-1"
FT                   /evidence="ECO:0000269|PubMed:22828809"
FT                   /id="PRO_0000433606"
FT   DISULFID        57..63
FT                   /evidence="ECO:0000250|UniProtKB:P32412"
SQ   SEQUENCE   63 AA;  7464 MW;  CF9E4E7605A4766E CRC64;
     MLTLKKSMLL LFFLGTINLS LCEQERDADE EERRDDDEMD VEVEKRFLPL FLPKIICVIT
     KKC