[1]	PROTEIN SEQUENCE, AND MASS SPECTROMETRY. TISSUE=Parotoid gland; Waugh R.J., Stone D.J.M., Bowie J.H., Wallace J.C., Tyler M.J.; "Peptides from Australian frogs. The structures of the caerins and caeridins from Litoria gilleni."; J. Chem. Res. 139:937-961(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=2448; Method=FAB; Range=1-25; 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

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0042742;	Biological process: defense response to bacterium (inferred from electronic annotation from UniProtKB-KW).
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Family and domain databases

Phylogenomic databases

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`PEPTIDE`	`1 25`	`25`		`Caerin-2.5.`	`PRO_0000043746`

Sequence information

Length: 25 AA [This is the length of the unprocessed precursor]

Molecular weight: 2450 Da [This is the MW of the unprocessed precursor]

CRC64: DDCA9BC5D48F8758 [This is a checksum on the sequence]

        10         20 
GLVASIGRAL GGLLADVVKS KEQPA

	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