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Reviewed, UniProtKB/Swiss-Prot P32413 (BR2E_RANES)

Last modified June 16, 2009. Version 41. 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-2E
OrganismRana esculenta (Edible frog)
Taxonomic identifier8401 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaRanoideaRanidaeRanaPelophylax

Protein attributes

Sequence length33 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
   PTMDisulfide bond
   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 erythrocytes

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-2E
PRO_0000044642

Amino acid modifications

Disulfide bond27 ↔ 33 Ref.1

Sequences

Sequence LengthMass (Da)Tools
P32413-1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 99140BC640ABB0EE

FASTA333,364
        10         20         30 
GIMDTLKNLA KTAGKGALQS LLNKASCKLS GQC 

« Hide

References

[1]"Novel antimicrobial peptides from skin secretion of the European frog Rana esculenta."
Simmaco M., Mignogna G., Barra D., Bossa F.
FEBS Lett. 324:159-161(1993) [PubMed: 8508915] [Abstract]
Cited for: PROTEIN SEQUENCE, DISULFIDE BOND.
Tissue: Skin secretion.

Cross-references

Sequence databases

PIRS33730.

3D structure databases

ModBaseSearch...

Phylogenomic databases

HOVERGENP32413.

Family and domain databases

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

Entry information

Entry nameBR2E_RANES
AccessionPrimary (citable) accession number: P32413
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 16, 2009
This is version 41 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