Reviewed, UniProtKB/Swiss-Prot P01501 (MEL_APIME)

Names and origin

Protein names

Recommended name:
    Melittin
Alternative name(s):
    Allergen Api m III
    Allergen=Api m 3

Gene names

Name:

MELT

Organism

Apis mellifera (Honeybee)

Taxonomic identifier

7460 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Hymenoptera › Apocrita › Aculeata › Apoidea › Apidae › Apis

Protein attributes

Sequence length	70 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Cytolysis Hemolysis Ion transport Transport
Cellular component	Membrane Secreted
Disease	Allergen
Domain	Signal Transmembrane
Molecular function	Porin Toxin
PTM	Amidation Formylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cytolysis 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 component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell pore complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	protein kinase inhibitor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Propeptide

22 – 43

22

Removed by a dipeptidylpeptidase

PRO_0000035148

Peptide

44 – 69

26

Melittin Ref.2

PRO_0000035149

Amino acid modifications

Modified residue

44

1

N-formylglycine; partial

Modified residue

69

1

Glutamine amide

Natural variations

Natural variant

64

1

K → S in melittin 2; possibly an artifact.

Natural variant

67 – 70

4

RQQG → KRQQ in melittin-2; possibly an artifact.

Secondary structure

1

.

.

.

.

.

70

Helix Strand Turn

Details...

Helix

45 – 53

9

Helix

55 – 68

14

Sequences

	Sequence		Length	Mass (Da)
	P01501-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 607F52C091C23BB6	FASTA	70	7,585
	10 20 30 40 50 60 MKFLVNVALV FMVVYISYIY AAPEPEPAPE PEAEADAEAD PEAGIGAVLK VLTTGLPALI 70 SWIKRKRQQG

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

EMBLGenBankDDBJ

X02007 mRNA. Translation: CAA26038.1.

PIR

MPHB1. A91133.

RefSeq

NP_001011607.1.

UniGene

Ame.1212

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BH1	NMR	-	A	44-69	[»]
2MLT	X-ray	2.00	A/B	44-69	[»]

ModBase

Search...

Protein family/group databases

TCDB

1.C.18.1.1. melittin family.

Genome annotation databases

GeneID

406130.

KEGG

ame:406130.

Organism-specific databases

CTD

406130.

Family and domain databases

InterPro

IPR002116. Melittin/Api_allergen.
[Graphical view]

Pfam

PF01372. Melittin. 1 hit.
[Graphical view]

ProDom

PD014636. Melittin/Api_allergen. 1 hit.
[Graphical view] [Entries sharing at least one domain]

ProtoNet

Search...

Other Resources

PMAP-CutDB

P01501.

Entry information

Entry name

MEL_APIME

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Tox-Prot (Toxin Annotation Project)