ID   CDN3_RANGI              Reviewed;          15 AA.
AC   P56248;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   10-FEB-2021, entry version 41.
DE   RecName: Full=Caeridin-3;
OS   Ranoidea gilleni (Centralian tree frog) (Litoria gilleni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae; Ranoidea.
OX   NCBI_TaxID=39405;
RN   [1]
RP   PROTEIN SEQUENCE, AMIDATION AT LEU-15, AND MASS SPECTROMETRY.
RC   TISSUE=Parotoid gland;
RA   Waugh R.J., Stone D.J.M., Bowie J.H., Wallace J.C., Tyler M.J.;
RT   "Peptides from Australian frogs. The structures of the caerins and
RT   caeridins from Litoria gilleni.";
RL   J. Chem. Res. 139:937-961(1993).
CC   -!- FUNCTION: Caeridins show neither neuropeptide activity nor antibiotic
CC       activity.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin parotoid and/or rostral
CC       glands.
CC   -!- MASS SPECTROMETRY: Mass=1428; Method=FAB; Evidence={ECO:0000269|Ref.1};
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Direct protein sequencing; Secreted.
FT   PEPTIDE         1..15
FT                   /note="Caeridin-3"
FT                   /id="PRO_0000043762"
FT   MOD_RES         15
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|Ref.1"
SQ   SEQUENCE   15 AA;  1430 MW;  06E90A797AF70CBF CRC64;
     GLFDAIGNLL GGLGL