Reviewed, UniProtKB/Swiss-Prot P40838 (BR2EB_RANES)

Names and origin

Protein names	Recommended name:     Brevinin-2Eb
Organism	Rana esculenta (Edible frog)
Taxonomic identifier	8401 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Neobatrachia › Ranoidea › Ranidae › Rana › Pelophylax

Protein attributes

Sequence length	33 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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.
Sequence similarities	Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily.

Ontologies

Keywords
Biological process	Cytolysis Hemolysis
Cellular component	Secreted
Molecular function	Amphibian defense peptide Antibiotic Antimicrobial
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW hemolysis by symbiont of host red blood cells Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Peptide	1 – 33	33	Brevinin-2Eb		PRO_0000044644
Amino acid modifications
	Disulfide bond	27 ↔ 33

Sequences

	Sequence		Length	Mass (Da)
	P40838-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 83A3918BB2BAF5FE	FASTA	33	3,319
	10 20 30 GILDTLKNLA KTAGKGALQG LVKMASCKLS GQC

References

[1]

"Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides." Simmaco M., Mignogna G., Barra D., Bossa F. J. Biol. Chem. 269:11956-11961(1994) [PubMed: 8163497] [Abstract] Cited for: PROTEIN SEQUENCE, DISULFIDE BOND. Tissue: Skin secretion.

Cross-references

Sequence databases
PIR	B55998.
3D structure databases
ModBase	Search...
Phylogenomic databases
HOVERGEN	P40838.
Family and domain databases
InterPro	IPR012521. Antimicrobial_2. [Graphical view]
Pfam	PF08023. Antimicrobial_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BR2EB_RANES

Accession

Primary (citable) accession number: P40838

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	November 25, 2008
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)