P40837 (BR2EA_RANES) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Brevinin-2Ea
Organism	Rana esculenta (Edible frog) (Pelophylax esculentus)
Taxonomic identifier	8401 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amphibia › Batrachia › Anura › Neobatrachia › Ranoidea › Ranidae › Pelophylax

Protein attributes

Sequence length	33 AA.
Sequence status	Complete.
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 in other organism 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 – 33	33	Brevinin-2Ea		PRO_0000044643
Amino acid modifications
	Disulfide bond	27 ↔ 33		Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P40837 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 4C940BDE699FF616	FASTA	33	3,245
	10 20 30 GILDTLKNLA ISAAKGAAQG LVNKASCKLS 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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE, DISULFIDE BOND. Tissue: Skin secretion.

Cross-references

Sequence databases
PIR	A55998.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG107535.
Family and domain databases
InterPro	IPR012521. Antimicrobial_frog_2. [Graphical view]
Pfam	PF08023. Antimicrobial_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BR2EA_RANES

Accession

Primary (citable) accession number: P40837

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	April 3, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program