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Reviewed, UniProtKB/Swiss-Prot P81252 (CR19_LITCH)

Last modified June 16, 2009. Version 32. 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-1.9
OrganismLitoria chloris (Blue-thighed frog)
Taxonomic identifier86064 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaHyloideaHylidaePelodryadinaeLitoria

Protein attributes

Sequence length24 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 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-1.9
PRO_0000043740

Amino acid modifications

Modified residue241Lysine amide

Sequences

Sequence LengthMass (Da)Tools
P81252-1 [UniParc].

Last modified December 15, 1998. Version 1.
Checksum: 4BA460BB1469ADB4

FASTA242,481
        10         20 
GLFGVLGSIA KHVLPHVVPV 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...

Phylogenomic databases

HOVERGENP81252.

Family and domain databases

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

Entry information

Entry nameCR19_LITCH
AccessionPrimary (citable) accession number: P81252
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: June 16, 2009
This is version 32 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