[1]	PROTEIN SEQUENCE, AND MASS SPECTROMETRY. TISSUE=Parotoid gland; Stone D.J.M., Waugh R.J., Bowie J.H., Wallace J.C., Tyler M.J.; "Peptides from Australian frogs. The structures of the caerins from Litoria caerula."; J. Chem. Res. 138:910-936(1993).

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 parotoid and/or rostral glands.
MASS SPECTROMETRY: Mass=2452; Method=FAB; Range=1-22; Source=Ref.1;.
SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Caerin subfamily.

Copyright

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Cross-references

3D structure databases
ModBase	P56241.
Family and domain databases
BLOCKS	P56241.
Phylogenomic databases
HOVERGEN	P56241; -.
Other
ProtoNet	P56241.
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: 22 AA [This is the length of the unprocessed precursor]

Molecular weight: 2455 Da [This is the MW of the unprocessed precursor]

CRC64: 3AB40B2200D43663 [This is a checksum on the sequence]

        10         20 
GLWEKIREKA NELVSGIVEG VK

	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