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P01501

- MEL_APIME

UniProt

P01501 - MEL_APIME

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Protein

Melittin

Gene
MELT
Organism
Apis mellifera (Honeybee)
Status
Reviewed - 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

  1. protein kinase inhibitor activity Source: InterPro

GO - Biological processi

  1. hemolysis in other organism Source: UniProtKB-KW
  2. ion transport Source: UniProtKB-KW
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: Unplaced

Subcellular locationi

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

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. other organism cell membrane Source: UniProtKB-SubCell
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.1 Publication

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 dipeptidylpeptidasePRO_0000035148Add
BLAST
Peptidei44 – 6926Melittin3 PublicationsPRO_0000035149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441N-formylglycine; partial
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 – 539
Helixi55 – 6814

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP01501.

Family & Domainsi

Sequence similaritiesi

Belongs to the melittin family.

Keywords - Domaini

Signal, Transmembrane

Phylogenomic databases

OMAiRIKTITS.

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

MKFLVNVALV FMVVYISYIY AAPEPEPAPE PEAEADAEAD PEAGIGAVLK   50
VLTTGLPALI SWIKRKRQQG 70
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:
EMBL
GenBank
DDBJ
Links Updated
X02007 mRNA. Translation: CAA26038.1.
PIRiA91133. MPHB1.
RefSeqiNP_001011607.1. NM_001011607.1.
UniGeneiAme.1212.

Genome annotation databases

EnsemblMetazoaiGB10355-RA; GB10355-PA; GB10355.
GeneIDi406130.
KEGGiame:406130.

Cross-referencesi

Web resourcesi

Protein Spotlight

Why Pooh luvvs hunny - Issue 12 of July 2001

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02007 mRNA. Translation: CAA26038.1 .
PIRi A91133. MPHB1.
RefSeqi NP_001011607.1. NM_001011607.1.
UniGenei Ame.1212.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BH1 NMR - A 44-69 [» ]
2MLT X-ray 2.00 A/B 44-69 [» ]
3QRX X-ray 2.20 B 44-69 [» ]
ProteinModelPortali P01501.
SMRi P01501. Positions 44-69.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 1455502. 1 interaction.
DIPi DIP-48928N.
STRINGi 7460.P01501.

Protein family/group databases

Allergomei 3091. Api m 4.0101.
48. Api m 4.
TCDBi 1.C.18.1.1. the melittin (melittin) family.

Proteomic databases

PaxDbi P01501.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai GB10355-RA ; GB10355-PA ; GB10355 .
GeneIDi 406130.
KEGGi ame:406130.

Organism-specific databases

CTDi 38785.

Phylogenomic databases

OMAi RIKTITS.

Miscellaneous databases

EvolutionaryTracei P01501.
PMAP-CutDB P01501.

Family and domain databases

InterProi IPR002116. Melittin/Api_allergen.
[Graphical view ]
Pfami PF01372. Melittin. 1 hit.
[Graphical view ]
ProDomi PD014636. Melittin/Api_allergen. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
ProtoNeti Search...

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: July 9, 2014
This is version 113 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

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