Skip Header

Contribute Send feedback
Read comments (?) or add your own

P81251 (CR18_LITCH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 2, 2010. Version 33. 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-1.8
OrganismLitoria chloris (Blue-thighed frog)
Taxonomic identifier86064 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaHyloideaHylidaePelodryadinaeLitoria

Protein attributes

Sequence length24 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 dorsal glands.

Domain

Contains two amphipathic alpha helix regions separated by a region of less-defined helicity and greater flexibility By similarity.

Sequence similarities

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

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 – 2424Caerin-1.8
PRO_0000043739

Amino acid modifications

Modified residue241Lysine amide

Sequences

Sequence LengthMass (Da)Tools
P81251 [UniParc].

Last modified December 15, 1998. Version 1.
Checksum: A77460A7EFDFEDAC

FASTA242,552
        10         20 
GLFKVLGSVA KHLLPHVVPV IAEK 

« Hide

References

[1]"New antibiotic caerin 1 peptides from the skin secretion of the Australian tree frog Litoria chloris. Comparison of the activities of the caerin 1 peptides from the genus Litoria."
Steinborner S.T., Currie G.J., Bowie J.H., Wallace J.C., Tyler M.J.
J. Pept. Res. 51:121-126(1998) [PubMed: 9516047] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Skin secretion.

Cross-references

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR010000. Caerin_1.
[Graphical view]
PfamPF07440. Caerin_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCR18_LITCH
AccessionPrimary (citable) accession number: P81251
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: March 2, 2010
This is version 33 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