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Reviewed, UniProtKB/Swiss-Prot P32424 (BR2_RANBP)

Last modified June 16, 2009. Version 43. 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-2
OrganismRana brevipoda porsa (Japanese frog)
Taxonomic identifier88447 [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 a very high 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-2
PRO_0000044646

Amino acid modifications

Disulfide bond27 ↔ 33 Ref.1

Sequences

Sequence LengthMass (Da)Tools
P32424-1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: BCD5D32E27DBCB96

FASTA333,254
        10         20         30 
GLLDSLKGFA ATAGKGVLQS LLSTASCKLA KTC 

« Hide

References

[1]"Brevinin-1 and -2, unique antimicrobial peptides from the skin of the frog, Rana brevipoda porsa."
Morikawa N., Hagiwara K., Nakajima T.
Biochem. Biophys. Res. Commun. 189:184-190(1992) [PubMed: 1449472] [Abstract]
Cited for: PROTEIN SEQUENCE, DISULFIDE BOND.
Tissue: Skin secretion.

Cross-references

Sequence databases

PIRJC1356.

3D structure databases

ModBaseSearch...

Phylogenomic databases

HOVERGENP32424.

Family and domain databases

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

Entry information

Entry nameBR2_RANBP
AccessionPrimary (citable) accession number: P32424
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 16, 2009
This is version 43 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