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Reviewed, UniProtKB/Swiss-Prot P56241 (CR34_LITCE)

Last modified July 22, 2008. Version 34. 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:
    Caerin-3.4
OrganismLitoria caerulea (Green tree frog)
Taxonomic identifier30344 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaHyloideaHylidaePelodryadinaeLitoria

Protein attributes

Sequence length22 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity.

Subcellular location

Secreted.

Tissue specificity

Expressed by the skin parotoid and/or rostral glands.

Sequence similarities

Belongs to the frog skin active peptide (FSAP) family. Caerin subfamily.

Mass spectrometry

Molecular weight is 2452 Da from positions 1 - 22. Determined by FAB. Ref.1

Ontologies

Keywords

   Cellular componentSecreted
   Molecular functionAmphibian defense peptide
Antibiotic
Antimicrobial
   PTMAmidation
   Technical termDirect protein sequencing

Gene Ontology (GO)

None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Peptide1 – 2222Caerin-3.4

Amino acid modifications

Modified residue221Lysine amide

Sequences

Sequence LengthMass (Da)Tools
P56241-1 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: 3AB40B2200D43663

FASTA222,455
        10         20 
GLWEKIREKA NELVSGIVEG VK 

« Hide

References

[1]"Peptides from Australian frogs. The structures of the caerins from Litoria caerula."
Stone D.J.M., Waugh R.J., Bowie J.H., Wallace J.C., Tyler M.J.
J. Chem. Res. 138:910-936(1993)
Cited for: PROTEIN SEQUENCE, MASS SPECTROMETRY.
Tissue: Parotoid gland.

Cross-references

3D structure databases

ModBaseSearch...

Phylogenomic databases

HOVERGENP56241.

Family and domain databases

ProDomP56241.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

Entry information

Entry nameCR34_LITCE
AccessionPrimary (citable) accession number: P56241
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: July 22, 2008
This is version 34 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