[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.
DOMAIN: Contains two amphipathic alpha helix regions separated by a region of less-defined helicity and greater flexibility (By similarity).
MASS SPECTROMETRY: Mass=2552; Method=FAB; Range=1-25; Source=Ref.1;.
SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Caerin subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

3D structure databases
ModBase	P56227.
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	P56227.
Phylogenomic databases
HOVERGEN	P56227; -.
Other
ProtoNet	P56227.
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: 25 AA [This is the length of the unprocessed precursor]

Molecular weight: 2555 Da [This is the MW of the unprocessed precursor]

CRC64: D8A5A460BB1464C0 [This is a checksum on the sequence]

        10         20 
GLLGVLGSVA KHVLPHVVPV IAEHL

	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