PROTEIN SEQUENCE, AND DISULFIDE BOND.
TISSUE=Skin secretion;
DOI=10.1016/0014-5793(93)81384-C; PubMed=8508915 [NCBI, ExPASy, EBI, Israel, Japan]
Simmaco M., Mignogna G., Barra D., Bossa F.;
"Novel antimicrobial peptides from skin secretion of the European frog Rana esculenta.";
FEBS Lett. 324:159-161(1993).

Comments

FUNCTION: Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and 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	S33730; S33730.
3D structure databases
ModBase	P32413.
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	P32413.
Phylogenomic databases
HOVERGEN	P32413; -.
Other
ProtoNet	P32413.
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: 3364 Da [This is the MW of the unprocessed precursor]

CRC64: 99140BC640ABB0EE [This is a checksum on the sequence]

        10         20         30 
GIMDTLKNLA KTAGKGALQS LLNKASCKLS GQC

	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