Record in detail


General Info

  • lamp_id:L03A000042
  • Name:CR19_LITCH
  • FullName:Caerin-1.9
  • Source:Litoria chloris
  • Mass:2552.1 Da
  • Sequence Length:24 aa
  • Isoelectric Point:10.51
  • Activity:Antimicrobial
  • Sequence
        GLFKVLGSIAKHLLPHVVPVVAEK
  • Function:Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity.

Cross-Linking

  •   Cross-linking
  •   1  Database:Uniprot  P81252
  •   2  Database:AMD  CR19_LITCH

Top similar AMPs

  • Top similar AMPs on LAMP
  • 1. L03A000042    From 1 To 24 E-value: 0.00000008 Score: 47.4
        GLFKVLGSIAKHLLPHVVPVVAEK
  • 2. L13A023566    From 1 To 24 E-value: 0.0000002 Score: 46.6
        GLFKVLGSVAKHLLPHVVPVIAEK
  • 3. L01A000413    From 1 To 24 E-value: 0.0000002 Score: 46.6
        GLFKVLGSVAKHLLPHVVPVIAEK
  • 4. L01A000529    From 1 To 24 E-value: 0.0000004 Score: 45.1
        GLFKVLGSVAKHLLPHVAPVIAEK
  • 5. L01A002352    From 1 To 24 E-value: 0.0000004 Score: 45.1
        GLFKVLGSVAKHLLPHVAPVIAEK

Structure

  •   Domains
  •   1  Name:Caerin_1    Interpro Link:IPR010000
  •   Structures

        No structs found on LAMP database

Activity

  •   Antibacterial Activities

    •     No MICs found on LAMP database

Toxicity

  •   Toxicity

    •     No toxicity records found on LAMP database

Reference

  •   Reference
  •   [1]  Tyler M.J.,Wallace J.C.,Bowie J.H.,Currie G.J.,Steinborner S.T.,
  •   Title: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.
  •   Journal:J. Pept. Res., 1998, 51, 121-126  [MEDLINE:98175802]

Comments

  •   Comments

    •     No comments found on LAMP database



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