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Protein

Melittin

Gene

MELT

Organism
Apis mellifera (Honeybee)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 A2.1 Publication
Melittin-S: 1.4-fold less hemolytic and adopts a less organized secondary structure than melittin.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Toxin

Keywords - Biological processi

Cytolysis, Hemolysis, Ion transport, Transport

Protein family/group databases

TCDBi1.C.18.1.1. the melittin (melittin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Melittin
Alternative name(s):
Allergen Api m 3
Allergen Api m III
Allergen: Api m 4
Gene namesi
Name:MELT
OrganismiApis mellifera (Honeybee)
Taxonomic identifieri7460 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaHymenopteraApocritaAculeataApoideaApidaeApis
ProteomesiUP000005203 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Secreted, Target cell membrane, Target membrane

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human.

Toxic dosei

LC(50) is 2.7 µg/ml against killifish.

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei3091. Api m 4.0101.
48. Api m 4.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Add
BLAST
Propeptidei22 – 4322Removed by a dipeptidylpeptidase3 PublicationsPRO_0000035148Add
BLAST
Peptidei44 – 6926MelittinPRO_0000035149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441N-formylglycine; partial1 Publication
Modified residuei69 – 691Glutamine amide1 Publication

Keywords - PTMi

Amidation, Formylation

Proteomic databases

PaxDbiP01501.

Miscellaneous databases

PMAP-CutDBP01501.

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Monomer and homotetramer.

Protein-protein interaction databases

BioGridi1455502. 1 interaction.
DIPiDIP-48928N.
STRINGi7460.P01501.

Structurei

Secondary structure

1
70
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi45 – 539Combined sources
Helixi55 – 6814Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BH1NMR-A44-69[»]
2MLTX-ray2.00A/B44-69[»]
3QRXX-ray2.20B44-69[»]
ProteinModelPortaliP01501.
SMRiP01501. Positions 44-69.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01501.

Family & Domainsi

Sequence similaritiesi

Belongs to the melittin family.Curated

Keywords - Domaini

Signal, Transmembrane

Family and domain databases

InterProiIPR002116. Melittin/Api_allergen.
[Graphical view]
PfamiPF01372. Melittin. 1 hit.
[Graphical view]
ProDomiPD014636. Melittin/Api_allergen. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01501-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFLVNVALV FMVVYISYIY AAPEPEPAPE PEAEADAEAD PEAGIGAVLK
60 70
VLTTGLPALI SWIKRKRQQG
Length:70
Mass (Da):7,585
Last modified:July 21, 1986 - v1
Checksum:i607F52C091C23BB6
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti53 – 531T → S in melittin-S.
Natural varianti64 – 641K → S in melittin-2; possibly an artifact.
Natural varianti67 – 704RQQG → KRQQ in melittin-2; possibly an artifact.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02007 mRNA. Translation: CAA26038.1.
PIRiA91133. MPHB1.
RefSeqiNP_001011607.1. NM_001011607.1.
UniGeneiAme.1212.

Genome annotation databases

EnsemblMetazoaiGB44112-RA; GB44112-PA; GB44112.
GeneIDi406130.
KEGGiame:406130.

Cross-referencesi

Web resourcesi

Protein Spotlight

Why Pooh luvvs hunny - Issue 12 of July 2001

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02007 mRNA. Translation: CAA26038.1.
PIRiA91133. MPHB1.
RefSeqiNP_001011607.1. NM_001011607.1.
UniGeneiAme.1212.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BH1NMR-A44-69[»]
2MLTX-ray2.00A/B44-69[»]
3QRXX-ray2.20B44-69[»]
ProteinModelPortaliP01501.
SMRiP01501. Positions 44-69.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1455502. 1 interaction.
DIPiDIP-48928N.
STRINGi7460.P01501.

Protein family/group databases

Allergomei3091. Api m 4.0101.
48. Api m 4.
TCDBi1.C.18.1.1. the melittin (melittin) family.

Proteomic databases

PaxDbiP01501.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiGB44112-RA; GB44112-PA; GB44112.
GeneIDi406130.
KEGGiame:406130.

Organism-specific databases

CTDi38785.

Miscellaneous databases

EvolutionaryTraceiP01501.
PMAP-CutDBP01501.

Family and domain databases

InterProiIPR002116. Melittin/Api_allergen.
[Graphical view]
PfamiPF01372. Melittin. 1 hit.
[Graphical view]
ProDomiPD014636. Melittin/Api_allergen. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

  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. Cited for: STRUCTURE BY NMR OF 44-69.
  10. Cited for: REVIEW.

Entry informationi

Entry nameiMEL_APIME
AccessioniPrimary (citable) accession number: P01501
Secondary accession number(s): P01503
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 27, 2015
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.