ID   CR31_RANSP              Reviewed;          22 AA.
AC   P62562; P56238;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Caerin-3.1;
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 LYS-22, 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: Antibacterial peptide, that adopts an alpha helical
CC       conformation which can disrupt bacterial membranes. Each caerin
CC       displays a different antimicrobial specificity.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin parotoid and/or rostral
CC       glands.
CC   -!- MASS SPECTROMETRY: Mass=2382; Method=FAB; Evidence={ECO:0000269|Ref.1};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Caerin subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P62562; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Direct protein sequencing; Secreted.
FT   PEPTIDE         1..22
FT                   /note="Caerin-3.1"
FT                   /id="PRO_0000043748"
FT   MOD_RES         22
FT                   /note="Lysine amide"
FT                   /evidence="ECO:0000269|Ref.1"
SQ   SEQUENCE   22 AA;  2385 MW;  1D4411E2E9D43739 CRC64;
     GLWQKIKDKA SELVSGIVEG VK