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Protein

Caerin-3.2

Gene
N/A
Organism
Litoria caerulea (Green tree frog)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Biological processi

  1. defense response to bacterium Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Amphibian defense peptide, Antibiotic, Antimicrobial

Names & Taxonomyi

Protein namesi
Recommended name:
Caerin-3.2
OrganismiLitoria caerulea (Green tree frog)
Taxonomic identifieri30344 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaHyloideaHylidaePelodryadinaeLitoria

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Peptidei1 – 2222Caerin-3.2PRO_0000043749Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei22 – 221Lysine amide

Keywords - PTMi

Amidation

Expressioni

Tissue specificityi

Expressed by the skin parotoid and/or rostral glands.

Family & Domainsi

Sequence similaritiesi

Sequencei

Sequence statusi: Complete.

P56239-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20 
GLWEKIKEKA SELVSGIVEG VK
Length:22
Mass (Da):2,400
Last modified:July 15, 1998 - v1
Checksum:i1D440B3829D4367C
GO

Mass spectrometryi

Molecular mass is 2397 Da from positions 1 - 22. Determined by FAB. 1 Publication

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiCR32_LITCE
AccessioniPrimary (citable) accession number: P56239
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: January 7, 2015
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.