PROTEIN SEQUENCE.
TISSUE=Skin secretion;
PubMed=9516047 [NCBI, ExPASy, EBI, Israel, Japan]
Steinborner S.T., Currie G.J., Bowie J.H., Wallace J.C., Tyler M.J.;
"New antibiotic caerin 1 peptides from the skin secretion of the Australian tree frog Litoria chloris. Comparison of the activities of the caerin 1 peptides from the genus Litoria.";
J. Pept. Res. 51:121-126(1998).

Comments

FUNCTION: Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the skin dorsal glands.
DOMAIN: Contains two amphipathic alpha helix regions separated by a region of less-defined helicity and greater flexibility (By similarity).
SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Caerin subfamily.

Copyright

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Cross-references

3D structure databases
ModBase	P81252.
Family and domain databases
InterPro	IPR010000; Caerin_1. Graphical view of domain structure.
Pfam	PF07440; Caerin_1; 1. Pfam graphical view of domain structure.
BLOCKS	P81252.
Phylogenomic databases
HOVERGEN	P81252; -.
Other
ProtoNet	P81252.
UniRef	View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial; Direct protein sequencing; Secreted.

Features

Feature table viewer

Sequence information

Length: 24 AA [This is the length of the unprocessed precursor]

Molecular weight: 2481 Da [This is the MW of the unprocessed precursor]

CRC64: 4BA460BB1469ADB4 [This is a checksum on the sequence]

        10         20 
GLFGVLGSIA KHVLPHVVPV IAEK

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools