ID   JNG1A_AMOJI             Reviewed;          66 AA.
AC   G3ETQ2;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Jindongenin-1a {ECO:0000303|PubMed:21816202};
DE   AltName: Full=Jindongenin-1 {ECO:0000312|EMBL:AEN14487.1};
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;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AEN14487.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 43-66, FUNCTION,
RP   SUBCELLULAR LOCATION, SYNTHESIS, AND MASS SPECTROMETRY.
RC   TISSUE=Skin {ECO:0000312|EMBL:AEN14487.1}, and
RC   Skin secretion {ECO:0000269|PubMed:21816202};
RX   PubMed=21816202; DOI=10.1016/j.biochi.2011.07.021;
RA   Chen Z., Yang X., Liu Z., Zeng L., Lee W., Zhang Y.;
RT   "Two novel families of antimicrobial peptides from skin secretions of the
RT   Chinese torrent frog, Amolops jingdongensis.";
RL   Biochimie 94:328-334(2012).
CC   -!- FUNCTION: Displays broad-spectrum antibacterial activity against a
CC       range of Gram-positive and Gram-negative bacteria. Also displays
CC       antifungal activity against C.albicans ATCC 2002. Has low hemolytic
CC       activity, low cytotoxicity and low antioxidant activity.
CC       {ECO:0000269|PubMed:21816202}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21816202}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:21816202}.
CC   -!- MASS SPECTROMETRY: Mass=2594.8; Method=FAB;
CC       Evidence={ECO:0000269|PubMed:21816202};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000255}.
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DR   EMBL; JF412290; AEN14487.1; -; mRNA.
DR   AlphaFoldDB; G3ETQ2; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0044179; P:hemolysis in another organism; IDA:UniProtKB.
DR   GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Antibiotic; Antimicrobial; Antioxidant;
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..40
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:21816202"
FT                   /id="PRO_0000415404"
FT   PEPTIDE         43..66
FT                   /note="Jindongenin-1a"
FT                   /evidence="ECO:0000269|PubMed:21816202"
FT                   /id="PRO_0000415405"
FT   DISULFID        60..66
FT                   /evidence="ECO:0000250|UniProtKB:A7WNV6"
SQ   SEQUENCE   66 AA;  7392 MW;  D227FB20F62AE4FF CRC64;
     MFTLKKPLLL LFFLGTVSLS LCEQERAADD DEGEVIEEEV KRDSMGAVKL AKLLIDKMKC
     EVTKAC