ID   CDN4_RANCA              Reviewed;          15 AA.
AC   P82076;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   10-FEB-2021, entry version 39.
DE   RecName: Full=Caeridin-4;
OS   Ranoidea caerulea (Green tree frog) (Litoria caerulea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae; Ranoidea.
OX   NCBI_TaxID=30344;
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. Structures of the caeridins from Litoria
RT   caerulea.";
RL   J. Chem. Soc. Perkin Trans. I 1:573-576(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=1504; 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-4"
FT                   /id="PRO_0000043763"
FT   MOD_RES         15
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|Ref.1"
SQ   SEQUENCE   15 AA;  1506 MW;  06F1BBEFBBC5195F CRC64;
     GLLDVVGNVL HSLGL