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Reviewed, UniProtKB/Swiss-Prot P40839 (BR2EC_RANES)

Last modified November 25, 2008. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Brevinin-2Ec
OrganismRana esculenta (Edible frog)
Taxonomic identifier8401 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaRanoideaRanidaeRanaPelophylax

Protein attributes

Sequence length34 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Biological processcytolysis

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 componentextracellular region

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Peptide1 – 3434Brevinin-2Ec
PRO_0000044645

Amino acid modifications

Disulfide bond28 ↔ 34

Sequences

Sequence LengthMass (Da)Tools
P40839-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: EE173F0F4E5A5EFB

FASTA343,521
        10         20         30 
GILLDKLKNF AKTAGKGVLQ SLLNTASCKL SGQC 

« 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: 8163497] [Abstract]
Cited for: PROTEIN SEQUENCE, DISULFIDE BOND.
Tissue: Skin secretion.

Cross-references

Sequence databases

PIRC55998.

3D structure databases

ModBaseSearch...

Phylogenomic databases

HOVERGENP40839.

Family and domain databases

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

Entry information

Entry nameBR2EC_RANES
AccessionPrimary (citable) accession number: P40839
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 25, 2008
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents