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P56239 (CR32_LITCE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 2, 2010. Version 37. 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:
Caerin-3.2
OrganismLitoria caerulea (Green tree frog)
Taxonomic identifier30344 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaHyloideaHylidaePelodryadinaeLitoria

Protein attributes

Sequence length22 AA.
Sequence statusComplete.
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 mass is 2397 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)
   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 – 2222Caerin-3.2
PRO_0000043749

Amino acid modifications

Modified residue221Lysine amide

Sequences

Sequence LengthMass (Da)Tools
P56239 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: 1D440B3829D4367C

FASTA222,400
        10         20 
GLWEKIKEKA SELVSGIVEG 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...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameCR32_LITCE
AccessionPrimary (citable) accession number: P56239
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: March 2, 2010
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families