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Reviewed, UniProtKB/Swiss-Prot P01501 (MEL_APIME)

Last modified November 24, 2009. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

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

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

Main toxin of bee venom with strong hemolytic activity. Integrates into cell membranes 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. Increases the permeability of cell membranes to ions, particularly Na+ and indirectly Ca2+, because of the Na+-Ca2+-exchange.

Subunit structure

Monomer and homotetramer.

Subcellular location

Secreted. Membrane. Note: Forms a membrane channel in the prey.

Tissue specificity

Expressed by the venom gland.

Allergenic properties

Causes an allergic reaction in human.

Toxic dose

LC(50) is 2.7 µg/ml against killifish. Ref.5

Miscellaneous

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

Sequence similarities

Belongs to the melittin family.

Ontologies

Keywords
   Biological processCytolysis
Hemolysis
Ion transport
Transport
   Cellular componentMembrane
Secreted
   DiseaseAllergen
   DomainSignal
Transmembrane
   Molecular functionPorin
Toxin
   PTMAmidation
Formylation
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processcytolysis

Inferred from electronic annotation. Source: UniProtKB-KW

hemolysis by symbiont of host erythrocytes

Inferred from electronic annotation. Source: UniProtKB-KW

ion transport

Inferred from electronic annotation. Source: UniProtKB-KW

pathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

pore complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionprotein kinase inhibitor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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
PRO_0000035149

Amino acid modifications

Modified residue441N-formylglycine; partial
Modified residue691Glutamine amide

Natural variations

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
P01501-1 [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: 6309516] [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: 5592400] [Abstract]
Cited for: PROTEIN SEQUENCE OF 44-69 (MELITTIN 1 AND 2), AMIDATION AT GLN-69.
[3]"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: 5139482] [Abstract]
Cited for: SYNTHESIS OF 44-69.
[4]"Isolation and structure of N 1-formyl melittin."
Luebke K., Matthes S., Kloss G.
Experientia 27:765-767(1971) [PubMed: 5139483] [Abstract]
Cited for: SYNTHESIS OF 44-69.
[5]"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: 10669014] [Abstract]
Cited for: LETHAL CONCENTRATION.
[6]"The structure of melittin. II. Interpretation of the structure."
Terwilliger T.C., Eisenberg D.
J. Biol. Chem. 257:6016-6022(1982) [PubMed: 7076662] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 44-69.
[7]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.
[8]"The actions of melittin on membranes."
Dempsey C.E.
Biochim. Biophys. Acta 1031:143-161(1990) [PubMed: 2187536] [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

X02007 mRNA. Translation: CAA26038.1.
PIRMPHB1. A91133.
RefSeqNP_001011607.1.
UniGeneAme.1212

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1BH1NMR-A44-69[»]
2MLTX-ray2.00A/B44-69[»]
ModBaseSearch...

Protein family/group databases

TCDB1.C.18.1.1. melittin family.

Genome annotation databases

GeneID406130.
KEGGame:406130.

Organism-specific databases

CTD406130.

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 Resources

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: November 24, 2009
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectTox-Prot (Toxin Annotation Project)

Relevant documents

Allergens

Nomenclature of allergens and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents