Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P01501 (MEL_APIME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Melittin
Alternative name(s):
Allergen Api m 3
Allergen Api m III
Allergen=Api m 4
Gene names
Name:MELT
OrganismApis mellifera (Honeybee) [Reference proteome]
Taxonomic identifier7460 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaHymenopteraApocritaAculeataApoideaApidaeApis

Protein attributes

Sequence length70 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 Ca2+, because of the Na+-Ca2+-exchange. It acts synergistically with phospholipase A2. Ref.3

Melittin-S: 1.4-fold less hemolytic and adopts a less organized secondary structure than melittin. Ref.3

Subunit structure

Monomer and homotetramer.

Subcellular location

Secreted. Target cell membrane. Note: Forms a transmembrane alpha-helix in the target cell membrane. Forms a membrane channel in the prey.

Tissue specificity

Expressed by the venom gland.

Allergenic properties

Causes an allergic reaction in human.

Toxic dose

LC50 is 2.7 µg/ml against killifish. Ref.7

Miscellaneous

N-formyl-melittin major has 80% of the activity of melittin.

Melittin: The secretion of this protein into venom follows a seasonal pattern. This variation is synchronized with phospholipase A2 variation, i.e. their production increase in the same months.

Melittin-S: The secretion of this protein into venom follows a seasonal pattern, the maximum secretion occurring during the (southern) winter months.

Sequence similarities

Belongs to the melittin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121
Propeptide22 – 4322Removed by a dipeptidylpeptidase
PRO_0000035148
Peptide44 – 6926Melittin Ref.2 Ref.3 Ref.4
PRO_0000035149

Amino acid modifications

Modified residue441N-formylglycine; partial
Modified residue691Glutamine amide Ref.2

Natural variations

Natural variant531T → S in melittin-S.
Natural variant641K → S in melittin-2; possibly an artifact.
Natural variant67 – 704RQQG → KRQQ in melittin-2; possibly an artifact.

Secondary structure

..... 70
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01501 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 607F52C091C23BB6

FASTA707,585
        10         20         30         40         50         60 
MKFLVNVALV FMVVYISYIY AAPEPEPAPE PEAEADAEAD PEAGIGAVLK VLTTGLPALI 

        70 
SWIKRKRQQG 

« Hide

References

[1]"Nucleotide sequence of cloned cDNA coding for honeybee prepromelittin."
Vlasak R., Unger-Ullmann C., Kreil G., Frischauf A.-M.
Eur. J. Biochem. 135:123-126(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence analysis of melittin from tryptic and peptic degradation products."
Habermann E., Jentsch J.
Hoppe-Seyler's Z. Physiol. Chem. 348:37-50(1967) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 44-69 (MELITTIN AND MELITTIN-2), AMIDATION AT GLN-69.
[3]"Identification of a novel melittin isoform from Africanized Apis mellifera venom."
Sciani J.M., Marques-Porto R., Lourenco A. Jr., Orsi R.D., Junior R.S., Barraviera B., Pimenta D.C.
Peptides 31:1473-1479(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 44-69 (MELITTIN-S), FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SEASONAL VARIATION, 3D-STRUCTURE MODELING.
Strain: Africanized honey bee.
Tissue: Venom.
[4]"Africanized honey bee (Apis mellifera) venom profiling: Seasonal variation of melittin and phospholipase A(2) levels."
Ferreira Junior R.S., Sciani J.M., Marques-Porto R., Junior A.L., Orsi R.D., Barraviera B., Pimenta D.C.
Toxicon 56:355-362(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 44-69 (MELITTIN), IDENTIFICATION BY MASS SPECTROMETRY, SEASONAL VARIATION.
Strain: Africanized honey bee.
Tissue: Venom.
[5]"Haemolytic activity and action on the surface tension of aqueous solutions of synthetic melittins and their derivatives."
Schroeder E., Luebke K., Lehmann M., Beetz I.
Experientia 27:764-765(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS OF 44-69.
[6]"Isolation and structure of N 1-formyl melittin."
Luebke K., Matthes S., Kloss G.
Experientia 27:765-767(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS OF 44-69, FORMYLATION AT GLY-44.
[7]"Isolation and structures of grammistins, peptide toxins from the skin secretion of the soapfish Grammistes sexlineatus."
Shiomi K., Igarashi T., Yokota H., Nagashima Y., Ishida M.
Toxicon 38:91-103(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: LETHAL CONCENTRATION.
[8]"The structure of melittin. II. Interpretation of the structure."
Terwilliger T.C., Eisenberg D.
J. Biol. Chem. 257:6016-6022(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 44-69.
[9]Barnham K.J., Hewish D., Werkmeister J., Curtain C., Kirkpatrick A., Bartone N., Norton R., Rivett D.
Submitted (JUN-1998) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 44-69.
[10]"The actions of melittin on membranes."
Dempsey C.E.
Biochim. Biophys. Acta 1031:143-161(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Why Pooh luvvs hunny - Issue 12 of July 2001

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02007 mRNA. Translation: CAA26038.1.
PIRMPHB1. A91133.
RefSeqNP_001011607.1. NM_001011607.1.
UniGeneAme.1212.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BH1NMR-A44-69[»]
2MLTX-ray2.00A/B44-69[»]
3QRXX-ray2.20B44-69[»]
ProteinModelPortalP01501.
SMRP01501. Positions 44-69.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid1455502. 1 interaction.
DIPDIP-48928N.
STRING7460.P01501.

Protein family/group databases

Allergome3091. Api m 4.0101.
48. Api m 4.
TCDB1.C.18.1.1. the melittin (melittin) family.

Proteomic databases

PaxDbP01501.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaGB10355-RA; GB10355-PA; GB10355.
GeneID406130.
KEGGame:406130.

Organism-specific databases

CTD38785.

Phylogenomic databases

OMARIKTITS.

Family and domain databases

InterProIPR002116. Melittin/Api_allergen.
[Graphical view]
PfamPF01372. Melittin. 1 hit.
[Graphical view]
ProDomPD014636. Melittin/Api_allergen. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other

EvolutionaryTraceP01501.
PMAP-CutDBP01501.

Entry information

Entry nameMEL_APIME
AccessionPrimary (citable) accession number: P01501
Secondary accession number(s): P01503
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Allergens

Nomenclature of allergens and list of entries