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P01501

- MEL_APIME

UniProt

P01501 - MEL_APIME

Protein

Melittin

Gene

MELT

Organism
Apis mellifera (Honeybee)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    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

    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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01501.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the melittin family.Curated

    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: October 1, 2014
    This is version 114 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