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P82387 (AUR12_LITRA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aurein-1.2
OrganismLitoria raniformis (Southern bell frog)
Taxonomic identifier116057 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaHyloideaHylidaePelodryadinaeLitoria

Protein attributes

Sequence length13 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Antimicrobial activity against B.cereus, L.lactis, L.innocua, M.luteus, P.multocida, S.aureus, S.epidermidis and S.uberis. Probably acts by disturbing membrane functions with its amphipathic structure. Shows anticancer activity. Ref.1

Subcellular location

Secreted.

Tissue specificity

Expressed by the skin dorsal glands.

Ontologies

Keywords
   Cellular componentSecreted
   Molecular functionAmphibian defense peptide
Antibiotic
Antimicrobial
   PTMAmidation
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processdefense response to bacterium

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 – 1313Aurein-1.2
PRO_0000043719

Amino acid modifications

Modified residue131Phenylalanine amide Ref.1

Secondary structure

... 13
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P82387 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 1EACB99DFBC83330

FASTA131,481
        10 
GLFDIIKKIA ESF 

« Hide

References

[1]"The antibiotic and anticancer active aurein peptides from the australian bell frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2."
Rozek T., Wegener K.L., Bowie J.H., Olver I.N., Carver J.A., Wallace J.C., Tyler M.J.
Eur. J. Biochem. 267:5330-5341(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, AMIDATION AT PHE-13, FUNCTION, STRUCTURE BY NMR.
Tissue: Skin secretion.
+Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VM5NMR-A1-13[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR013157. Aurein_antimicrobial_peptide.
[Graphical view]
PfamPF08256. Antimicrobial20. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP82387.

Entry information

Entry nameAUR12_LITRA
AccessionPrimary (citable) accession number: P82387
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 1, 2000
Last modified: October 16, 2013
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references