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Melittin (Allergen Api m 3) (Allergen Api m III) (allergen Api m 4)

 MEL_APIME               Reviewed;          70 AA.
P01501; P01503;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-APR-2018, entry version 133.
RecName: Full=Melittin;
AltName: Full=Allergen Api m 3;
AltName: Full=Allergen Api m III;
AltName: Allergen=Api m 4;
Flags: Precursor;
Name=MELT;
Apis mellifera (Honeybee).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata;
Apoidea; Apidae; Apis.
NCBI_TaxID=7460;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6309516; DOI=10.1111/j.1432-1033.1983.tb07626.x;
Vlasak R., Unger-Ullmann C., Kreil G., Frischauf A.-M.;
"Nucleotide sequence of cloned cDNA coding for honeybee
prepromelittin.";
Eur. J. Biochem. 135:123-126(1983).
[2]
PROTEIN SEQUENCE OF 44-69 (MELITTIN AND MELITTIN-2), AND AMIDATION AT
GLN-69.
PubMed=5592400;
Habermann E., Jentsch J.;
"Sequence analysis of melittin from tryptic and peptic degradation
products.";
Hoppe-Seyler's Z. Physiol. Chem. 348:37-50(1967).
[3]
PROTEIN SEQUENCE OF 44-69 (MELITTIN-S), FUNCTION, IDENTIFICATION BY
MASS SPECTROMETRY, SEASONAL VARIATION, AND 3D-STRUCTURE MODELING.
STRAIN=Africanized honey bee; TISSUE=Venom;
PubMed=20472009; DOI=10.1016/j.peptides.2010.05.001;
Sciani J.M., Marques-Porto R., Lourenco A. Jr., Orsi R.D.,
Junior R.S., Barraviera B., Pimenta D.C.;
"Identification of a novel melittin isoform from Africanized Apis
mellifera venom.";
Peptides 31:1473-1479(2010).
[4]
PROTEIN SEQUENCE OF 44-69 (MELITTIN), IDENTIFICATION BY MASS
SPECTROMETRY, AND SEASONAL VARIATION.
STRAIN=Africanized honey bee; TISSUE=Venom;
PubMed=20403370; DOI=10.1016/j.toxicon.2010.03.023;
Ferreira Junior R.S., Sciani J.M., Marques-Porto R., Junior A.L.,
Orsi R.D., Barraviera B., Pimenta D.C.;
"Africanized honey bee (Apis mellifera) venom profiling: Seasonal
variation of melittin and phospholipase A(2) levels.";
Toxicon 56:355-362(2010).
[5]
SYNTHESIS OF 44-69.
PubMed=5139482; DOI=10.1007/BF02136851;
Schroeder E., Luebke K., Lehmann M., Beetz I.;
"Haemolytic activity and action on the surface tension of aqueous
solutions of synthetic melittins and their derivatives.";
Experientia 27:764-765(1971).
[6]
SYNTHESIS OF 44-69, AND FORMYLATION AT GLY-44.
PubMed=5139483; DOI=10.1007/BF02136852;
Luebke K., Matthes S., Kloss G.;
"Isolation and structure of N 1-formyl melittin.";
Experientia 27:765-767(1971).
[7]
LETHAL CONCENTRATION.
PubMed=10669014; DOI=10.1016/S0041-0101(99)00136-1;
Shiomi K., Igarashi T., Yokota H., Nagashima Y., Ishida M.;
"Isolation and structures of grammistins, peptide toxins from the skin
secretion of the soapfish Grammistes sexlineatus.";
Toxicon 38:91-103(2000).
[8]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 44-69.
PubMed=7076662;
Terwilliger T.C., Eisenberg D.;
"The structure of melittin. II. Interpretation of the structure.";
J. Biol. Chem. 257:6016-6022(1982).
[9]
STRUCTURE BY NMR OF 44-69.
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.
[10]
REVIEW.
PubMed=2187536; DOI=10.1016/0304-4157(90)90006-X;
Dempsey C.E.;
"The actions of melittin on membranes.";
Biochim. Biophys. Acta 1031:143-161(1990).
-!- FUNCTION: 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 Ca(2+), because of the Na(+)-Ca(2+)-exchange. It acts
synergistically with phospholipase A2.
{ECO:0000269|PubMed:20472009}.
-!- FUNCTION: Melittin-S: 1.4-fold less hemolytic and adopts a less
organized secondary structure than melittin.
{ECO:0000269|PubMed:20472009}.
-!- SUBUNIT: Monomer and homotetramer.
-!- SUBCELLULAR LOCATION: Secreted. Target cell membrane. Note=Forms a
transmembrane alpha-helix in the target cell membrane. Forms a
membrane channel in the prey.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- ALLERGEN: Causes an allergic reaction in human.
-!- TOXIC DOSE: LC(50) is 2.7 ug/ml against killifish.
-!- MISCELLANEOUS: N-formyl-melittin major has 80% of the activity of
melittin.
-!- MISCELLANEOUS: 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.
-!- MISCELLANEOUS: Melittin-S: The secretion of this protein into
venom follows a seasonal pattern, the maximum secretion occurring
during the (southern) winter months.
-!- SIMILARITY: Belongs to the melittin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Why Pooh luvvs hunny
- Issue 12 of July 2001;
URL="https://web.expasy.org/spotlight/back_issues/012";
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EMBL; X02007; CAA26038.1; -; mRNA.
PIR; A91133; MPHB1.
RefSeq; NP_001011607.1; NM_001011607.1.
UniGene; Ame.1212; -.
PDB; 1BH1; NMR; -; A=44-69.
PDB; 2MLT; X-ray; 2.00 A; A/B=44-69.
PDB; 2MW6; NMR; -; A=44-69.
PDB; 3QRX; X-ray; 2.20 A; B=44-69.
PDBsum; 1BH1; -.
PDBsum; 2MLT; -.
PDBsum; 2MW6; -.
PDBsum; 3QRX; -.
ProteinModelPortal; P01501; -.
SMR; P01501; -.
BioGrid; 1455502; 1.
DIP; DIP-48928N; -.
STRING; 7460.GB10355-PA; -.
ChEMBL; CHEMBL3351188; -.
Allergome; 3091; Api m 4.0101.
Allergome; 48; Api m 4.
TCDB; 1.C.18.1.1; the melittin (melittin) family.
PaxDb; P01501; -.
EnsemblMetazoa; GB44112-RA; GB44112-PA; GB44112.
GeneID; 406130; -.
KEGG; ame:406130; -.
CTD; 38785; -.
EvolutionaryTrace; P01501; -.
PMAP-CutDB; P01501; -.
Proteomes; UP000005203; Linkage group 4.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0044218; C:other organism cell membrane; IEA:UniProtKB-SubCell.
GO; GO:0004860; F:protein kinase inhibitor activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0044179; P:hemolysis in other organism; IEA:UniProtKB-KW.
GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
InterPro; IPR002116; Melittin/Api_allergen.
Pfam; PF01372; Melittin; 1.
ProDom; PD014636; Melittin/Api_allergen; 1.
1: Evidence at protein level;
3D-structure; Allergen; Amidation; Complete proteome; Cytolysis;
Direct protein sequencing; Formylation; Hemolysis; Ion transport;
Membrane; Reference proteome; Secreted; Signal; Target cell membrane;
Target membrane; Toxin; Transmembrane; Transport.
SIGNAL 1 21
PROPEP 22 43 Removed by a dipeptidylpeptidase.
{ECO:0000269|PubMed:20403370,
ECO:0000269|PubMed:20472009,
ECO:0000269|PubMed:5592400}.
/FTId=PRO_0000035148.
PEPTIDE 44 69 Melittin.
/FTId=PRO_0000035149.
MOD_RES 44 44 N-formylglycine; partial.
{ECO:0000269|PubMed:5139483}.
MOD_RES 69 69 Glutamine amide.
{ECO:0000269|PubMed:5592400}.
VARIANT 53 53 T -> S (in melittin-S).
VARIANT 64 64 K -> S (in melittin-2; possibly an
artifact).
VARIANT 67 70 RQQG -> KRQQ (in melittin-2; possibly an
artifact).
HELIX 45 53 {ECO:0000244|PDB:2MLT}.
HELIX 55 68 {ECO:0000244|PDB:2MLT}.
SEQUENCE 70 AA; 7585 MW; 607F52C091C23BB6 CRC64;
MKFLVNVALV FMVVYISYIY AAPEPEPAPE PEAEADAEAD PEAGIGAVLK VLTTGLPALI
SWIKRKRQQG


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