ID CR24_LITCE Reviewed; 25 AA. AC P56236; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 22-JUL-2008, entry version 33. DE RecName: Full=Caerin-2.4; 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 -!- MASS SPECTROMETRY: Mass=2450; Method=FAB; Range=1-25; CC Source=Ref.1; CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. CC Caerin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR HOVERGEN; P56236; -. PE 1: Evidence at protein level; KW Amphibian defense peptide; Antibiotic; Antimicrobial; KW Direct protein sequencing; Secreted. FT PEPTIDE 1 25 Caerin-2.4. FT /FTId=PRO_0000043745. SQ SEQUENCE 25 AA; 2452 MW; DDD82C35D49596B8 CRC64; GLVSSIGKAL GGLLADVVKT KEQPA //