Record in detail


General Info

  • lamp_id:L03A000036
  • Name:MEL_APIME
  • FullName:Melittin
  • Source:Apis mellifera
  • Mass:2847.5 Da
  • Sequence Length:26 aa
  • Isoelectric Point:12.55
  • Activity:Antimicrobial
  • Sequence
        GIGAVLKVLTTGLPALISWIRKKRQQ
  • Function:Melittin: Main toxin of bee venom with strong hemolytic activity. Forms a pore in the cell membrane by inserting into lipid bilayers in an alpha-helical conformation and has multiple effects, probably, as a result of its interaction with negatively charged phospholipids. It inhibits well known transport pumps such as the Na(+)-K(+)-ATPase and the H(+)-K(+)-ATPase. It increases the permeability of cell membranes to ions, particularly Na(+) and indirectly Ca(2+), because of the Na(+)-Ca(2+)-exchange. It acts synergistically with phospholipase A2.

Cross-Linking

  •   Cross-linking
  •   1  Database:Uniprot  P01503
  •   2  Database:AMD  MEL2_APIME

Top similar AMPs

  • Top similar AMPs on LAMP
  • 1. L03A000036    From 1 To 26 E-value: 0.000000003 Score: 52.4
        GIGAVLKVLTTGLPALISWIRKKRQQ
  • 2. L12A09068|    From 41 To 66 E-value: 0.000000003 Score: 52
        GIGAVLKVLTTGLPALISWIKRKRQQ
  • 3. L03A000139    From 44 To 69 E-value: 0.000000005 Score: 51.6
        GIGAVLKVLTTGLPALISWIKRKRQQ
  • 4. L12A07874|    From 44 To 69 E-value: 0.000000006 Score: 51.6
        GIGAVLKVLTTGLPALISWIKRKRQQ
  • 5. L01A001956    From 1 To 26 E-value: 0.00000001 Score: 50.1
        GIGAVLKVLTTGLPALISWIKRKRQQ

Structure

  •   Domains
  •   1  Name:Melittin/Api_allergen    Interpro Link:IPR002116
  •   Structures

Activity

  •   Antibacterial Activities

    •     No MICs found on LAMP database

Toxicity

  •   Toxicity

    •     No toxicity records found on LAMP database

Reference

  •   Reference
  •   [1]  Jentsch J.,Habermann E.,
  •   Title:Sequence analysis of melittin from tryptic and peptic degradation products.
  •   Journal:Hoppe-Seyler"s Z. Physiol. Chem., 1967, 348, 37-50  [MEDLINE:68327913]
  •   [2]  Beetz I.,Lehmann M.,Luebke K.,Schroeder E.,
  •   Title:Haemolytic activity and action on the surface tension of aqueous solutions of synthetic melittins and their derivatives.
  •   Journal:Experientia, 1971, 27, 764-765  [MEDLINE:72098668]
  •   [3]  Kloss G.,Matthes S.,Luebke K.,
  •   Title:Isolation and structure of N 1-formyl melittin.
  •   Journal:Experientia, 1971, 27, 765-767  [MEDLINE:72098669]
  •   [4]  Eisenberg D.,Terwilliger T.C.,
  •   Title:The structure of melittin. II. Interpretation of the structure.
  •   Journal:J. Biol. Chem., 1982, 257, 6016-6022  [MEDLINE:82189959]
  •   [5]  Frischauf A.-M.,Kreil G.,Unger-Ullmann C.,Vlasak R.,
  •   Title:Nucleotide sequence of cloned cDNA coding for honeybee prepromelittin.
  •   Journal:Eur. J. Biochem., 1983, 135, 123-126  [MEDLINE:83287387]
  •   [6]  Dempsey C.E.
  •   Title:The actions of melittin on membranes.
  •   Journal:Biochim. Biophys. Acta, 1990, 1031, 143-161  [MEDLINE:90254148]
  •   [7]  Ishida M.,Nagashima Y.,Yokota H.,Igarashi T.,Shiomi K.,
  •   Title:Isolation and structures of grammistins, peptide toxins from the skin secretion of the soapfish Grammistes sexlineatus.
  •   Journal:Toxicon, 2000, 38, 91-103  [MEDLINE:20132498]
  •   [8]  Orsi R.D.,Junior A.L.,Marques-Porto R.,Sciani J.M.,Ferreira Junior R.S.,
  •   Title:Africanized honey bee (Apis mellifera) venom profiling: Seasonal variation of melittin and phospholipase A(2) levels.
  •   Journal:Toxicon, 2010, 56, 355-362  [PubMed:20403370]
  •   [9]  Junior R.S.,Orsi R.D.,Lourenco A. Jr.,Marques-Porto R.,Sciani J.M.,
  •   Title:Identification of a novel melittin isoform from Africanized Apis mellifera venom.
  •   Journal:Peptides, 2010, 31, 1473-1479  [PubMed:20472009]

Comments

  •   Comments

    •     No comments found on LAMP database



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