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P40837 (BR2EA_RANES) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Brevinin-2Ea
OrganismRana esculenta (Edible frog) (Pelophylax esculentus)
Taxonomic identifier8401 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaRanoideaRanidaePelophylax

Protein attributes

Sequence length33 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processCytolysis
Hemolysis
   Cellular componentSecreted
   Molecular functionAmphibian defense peptide
Antibiotic
Antimicrobial
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processdefense response to bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

hemolysis in other organism

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Peptide1 – 3333Brevinin-2Ea
PRO_0000044643

Amino acid modifications

Disulfide bond27 ↔ 33 Ref.1

Sequences

Sequence LengthMass (Da)Tools
P40837 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 4C940BDE699FF616

FASTA333,245
        10         20         30 
GILDTLKNLA ISAAKGAAQG LVNKASCKLS GQC 

« Hide

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

PIRA55998.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG107535.

Family and domain databases

InterProIPR012521. Antimicrobial_frog_2.
[Graphical view]
PfamPF08023. Antimicrobial_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBR2EA_RANES
AccessionPrimary (citable) accession number: P40837
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 19, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families