ID   CDN11_RANSP             Reviewed;          12 AA.
AC   P62565; P56245; P81253;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   10-FEB-2021, entry version 27.
DE   RecName: Full=Caeridin-1.1/1.2/1.3;
OS   Ranoidea splendida (Magnificent tree frog) (Litoria splendida).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae; Ranoidea.
OX   NCBI_TaxID=30345;
RN   [1]
RP   PROTEIN SEQUENCE, AMIDATION AT LEU-12, AND MASS SPECTROMETRY.
RC   TISSUE=Parotoid gland;
RA   Stone D.J.M., Waugh R.J., Bowie J.H., Wallace J.C., Tyler M.J.;
RT   "Peptides from Australian frogs. Structures of the caerins and caeridin 1
RT   from Litoria splendida.";
RL   J. Chem. Soc. Perkin Trans. I 1:3173-3178(1992).
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   -!- PTM: Isomerization alpha-beta of the Asp-4 residue in caeridin 1.2; a
CC       cyclic succinimide may be formed between Asp-4 and Gly-5 residues in
CC       caeridin 1.3. {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=1139; 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..12
FT                   /note="Caeridin-1.1/1.2/1.3"
FT                   /id="PRO_0000043757"
FT   MOD_RES         12
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|Ref.1"
SQ   SEQUENCE   12 AA;  1141 MW;  2822551A33772728 CRC64;
     GLLDGLLGTL GL