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P56239

- CR32_LITCE

UniProt

P56239 - CR32_LITCE

Protein

Caerin-3.2

Gene
N/A
Organism
Litoria caerulea (Green tree frog)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. 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

    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

    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

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    GLWEKIKEKA SELVSGIVEG VK                                 22
    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

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    ProtoNeti Search...

    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: October 1, 2014
    This is version 38 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