PROTEIN SEQUENCE, AND DISULFIDE BOND.
TISSUE=Skin secretion;
DOI=10.1016/0006-291X(92)91542-X; PubMed=1449472 [NCBI, ExPASy, EBI, Israel, Japan]
Morikawa N., Hagiwara K., Nakajima T.;
"Brevinin-1 and -2, unique antimicrobial peptides from the skin of the frog, Rana brevipoda porsa.";
Biochem. Biophys. Res. Commun. 189:184-190(1992).

Comments

FUNCTION: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and a very high hemolytic activity.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the skin glands.
SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily.

Copyright

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

Cross-references

Sequence databases
PIR	JC1356; JC1356.
3D structure databases
ModBase	P32424.
Family and domain databases
InterPro	IPR012521; Antimicrobial_2. Graphical view of domain structure.
Pfam	PF08023; Antimicrobial_2; 1. Pfam graphical view of domain structure.
BLOCKS	P32424.
Phylogenomic databases
HOVERGEN	P32424; -.
Other
ProtoNet	P32424.
UniRef	View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

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

Features

Feature table viewer

Sequence information

Length: 33 AA [This is the length of the unprocessed precursor]

Molecular weight: 3254 Da [This is the MW of the unprocessed precursor]

CRC64: BCD5D32E27DBCB96 [This is a checksum on the sequence]

        10         20         30 
GLLDSLKGFA ATAGKGVLQS LLSTASCKLA KTC

	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