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Melittin major precursor (anion selective).  Its bacteriocidal activity against Listeria and its cytotoxicity to animal cells have been studied (Wu et al. 2016). In zwitterionic membranes, melittin forms transmembrane toroidal homomeric pores supported by four to eight peptides. Its ability to diffuse freely in a 1,2-dimyristoyl-SN-glycero-3-phosphocholine membrane leads to dynamic pores of vaious diameters with varying molecularity containing from 4 to peptides/channel (Pino-Angeles and Lazaridis 2018).

Accession Number:P01501
Protein Name:MEL aka MELT
Molecular Weight:7585.00
Species:Apis mellifera (Honeybee), and Apis cerana (Indian honeybee) [7460]
Number of TMSs:2
Location1 / Topology2 / Orientation3: Secreted1
Substrate small molecules, electrolytes, water

Cross database links:

RefSeq: NP_001011607.1   
Entrez Gene ID: 406130   
Pfam: PF01372   
KEGG: ame:406130   

Gene Ontology

GO:0005576 C:extracellular region
GO:0046930 C:pore complex
GO:0004860 F:protein kinase inhibitor activity
GO:0019835 P:cytolysis
GO:0019836 P:hemolysis by symbiont of host erythrocytes
GO:0006811 P:ion transport
GO:0009405 P:pathogenesis

References (7)

[1] “Nucleotide sequence of cloned cDNA coding for honeybee prepromelittin.”  Vlasak   6309516
[2] “Sequence analysis of melittin from tryptic and peptic degradation products.”  Habermann   5592400
[3] “Haemolytic activity and action on the surface tension of aqueous solutions of synthetic melittins and their derivatives.”  Schroeder   5139482
[4] “Isolation and structure of N 1-formyl melittin.”  Luebke   5139483
[5] “Isolation and structures of grammistins, peptide toxins from the skin secretion of the soapfish Grammistes sexlineatus.”  Shiomi   10669014
[6] “The structure of melittin. II. Interpretation of the structure.”  Terwilliger   7076662
[7] “The actions of melittin on membranes.”  Dempsey   2187536
1BH1   2MLT   2MW6   3QRX   6DST   6O4M     

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