ID   CDN11_RANCH             Reviewed;          12 AA.
AC   P62567; P56245; P81253;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   10-FEB-2021, entry version 29.
DE   RecName: Full=Caeridin-1.1/1.2/1.3;
OS   Ranoidea chloris (Red-eyed tree frog) (Litoria chloris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae; Ranoidea.
OX   NCBI_TaxID=86064;
RN   [1]
RP   PROTEIN SEQUENCE, AND AMIDATION AT LEU-12.
RC   TISSUE=Skin secretion;
RX   PubMed=9516047; DOI=10.1111/j.1399-3011.1998.tb00629.x;
RA   Steinborner S.T., Currie G.J., Bowie J.H., Wallace J.C., Tyler M.J.;
RT   "New antibiotic caerin 1 peptides from the skin secretion of the Australian
RT   tree frog Litoria chloris. Comparison of the activities of the caerin 1
RT   peptides from the genus Litoria.";
RL   J. Pept. Res. 51:121-126(1998).
CC   -!- FUNCTION: Caeridins show neither neuropeptide activity nor antibiotic
CC       activity.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin 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}.
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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_0000043755"
FT   MOD_RES         12
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:9516047"
SQ   SEQUENCE   12 AA;  1141 MW;  2822551A33772728 CRC64;
     GLLDGLLGTL GL