ID   CR13_LITCE              Reviewed;          25 AA.
AC   P56228;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   22-JUL-2008, entry version 35.
DE   RecName: Full=Caerin-1.3;
OS   Litoria caerulea (Green tree frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae;
OC   Pelodryadinae; Litoria.
OX   NCBI_TaxID=30344;
RN   [1]
RP   PROTEIN SEQUENCE, 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. The structures of the caerins from
RT   Litoria caerula.";
RL   J. Chem. Res. 138:910-936(1993).
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   -!- DOMAIN: Contains two amphipathic alpha helix regions separated by
CC       a region of less-defined helicity and greater flexibility (By
CC       similarity).
CC   -!- MASS SPECTROMETRY: Mass=2582; Method=FAB; Range=1-25;
CC       Source=Ref.1;
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Caerin subfamily.
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DR   HOVERGEN; P56228; -.
DR   InterPro; IPR010000; Caerin_1.
DR   Pfam; PF07440; Caerin_1; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Direct protein sequencing; Secreted.
FT   PEPTIDE       1     25       Caerin-1.3.
FT                                /FTId=PRO_0000043737.
FT   MOD_RES      25     25       Leucine amide.
SQ   SEQUENCE   25 AA;  2585 MW;  D8A5A460BB0EA2F2 CRC64;
     GLLSVLGSVA QHVLPHVVPV IAEHL
//