ID   B1CG2_AMOCU             Reviewed;          69 AA.
AC   E1AWD5;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Brevinin-1CG2 {ECO:0000303|PubMed:22951323};
DE   Flags: Precursor;
OS   Amolops chunganensis (Chungan torrent frog) (Hylorana chunganensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Amolops.
OX   NCBI_TaxID=325556 {ECO:0000303|PubMed:22951323};
RN   [1] {ECO:0000312|EMBL:ADM34207.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-69, FUNCTION, SYNTHESIS,
RP   SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Skin secretion {ECO:0000303|PubMed:22951323};
RX   PubMed=22951323; DOI=10.1016/j.peptides.2012.08.008;
RA   Yang X., Xia J., Yu Z., Hu Y., Li F., Meng H., Yang S., Liu J., Wang H.;
RT   "Characterization of diverse antimicrobial peptides in skin secretions of
RT   Chungan torrent frog Amolops chunganensis.";
RL   Peptides 38:41-53(2012).
CC   -!- FUNCTION: Antimicrobial peptide active against a variety of Gram-
CC       positive and some Gram-negative bacterial strains. Has antifungal
CC       activity against C.albicans ATCC 10231 and a slime mold isolate. Has
CC       hemolytic activity against human erythrocytes.
CC       {ECO:0000269|PubMed:22951323}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255,
CC       ECO:0000269|PubMed:22951323}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:22951323}.
CC   -!- MASS SPECTROMETRY: Mass=2586.3; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:22951323};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000255}.
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DR   EMBL; HQ009831; ADM34207.1; -; mRNA.
DR   AlphaFoldDB; E1AWD5; -.
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..43
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305|PubMed:22951323"
FT                   /id="PRO_0000439726"
FT   PEPTIDE         46..69
FT                   /note="Brevinin-1CG2"
FT                   /evidence="ECO:0000269|PubMed:22951323"
FT                   /id="PRO_0000439727"
FT   DISULFID        63..69
FT                   /evidence="ECO:0000250|UniProtKB:P80398"
SQ   SEQUENCE   69 AA;  7973 MW;  045983995B2B5531 CRC64;
     MFTTKKPLLL LFFLGTINLS LCEQERNAEE ERRDDDEMDV EVEKRFLPIV AGLAANFLPK
     IVCKITKKC