CDN14_RANCH
ID CDN14_RANCH Reviewed; 12 AA.
AC P62581; P56246;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 10-FEB-2021, entry version 26.
DE RecName: Full=Caeridin-1.4;
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 dorsal glands.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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-1.4"
FT /id="PRO_0000043759"
FT MOD_RES 12
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:9516047"
SQ SEQUENCE 12 AA; 1097 MW; 28225503E3772728 CRC64;
GLLDGLLGGL GL