Reviewed, UniProtKB/Swiss-Prot P40839 (BR2EC_RANES)

Names and origin

Protein names	Recommended name:     Brevinin-2Ec
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	34 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
PTM	Disulfide bond
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 erythrocytes Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Peptide	1 – 34	34	Brevinin-2Ec		PRO_0000044645
Amino acid modifications
	Disulfide bond	28 ↔ 34		Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P40839-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: EE173F0F4E5A5EFB	FASTA	34	3,521
	10 20 30 GILLDKLKNF AKTAGKGVLQ SLLNTASCKL SGQC

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	C55998.
3D structure databases
ModBase	Search...
Phylogenomic databases
HOVERGEN	P40839.
Family and domain databases
InterPro	IPR012521. Antimicrobial_2. [Graphical view]
Pfam	PF08023. Antimicrobial_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BR2EC_RANES

Accession

Primary (citable) accession number: P40839

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)