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Melittin

 MEL_VESMC               Reviewed;          70 AA.
P59262;
01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
01-FEB-2003, sequence version 1.
16-JAN-2019, entry version 61.
RecName: Full=Melittin {ECO:0000303|PubMed:12939801};
Short=MEL;
Short=MLT;
Flags: Precursor;
Name=MELT;
Vespula maculifrons (Eastern yellow jacket) (Wasp).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata;
Vespoidea; Vespidae; Vespinae; Vespula.
NCBI_TaxID=7453;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
PubMed=12939801;
Shi W.J., Zhang S.F., Zhang C.-X., Cheng J.A.;
"Cloning and comparative analysis of the venom prepromelittin genes
from four wasp species.";
Yi Chuan Xue Bao 30:555-559(2003).
-!- FUNCTION: Main toxin of bee venom with strong hemolytic activity
and antimicrobial activity. It has enhancing effects on bee venom
phospholipase A2 activity. This amphipathic toxin binds to
negatively charged membrane surface and forms pore by inserting
into lipid bilayers inducing the leakage of ions and molecules and
the enhancement of permeability that ultimately leads to cell
lysis. It acts as a voltage-gated pore with higher selectivity for
anions over cations. The ion conductance has been shown to be
voltage-dependent. Self-association of melittin in membranes is
promoted by high ionic strength, but not by the presence of
negatively charged lipids. In vivo, intradermal injection into
healthy human volunteers produce sharp pain sensation and an
inflammatory response. It produces pain by activating primary
nociceptor cells directly and indirectly due to its ability to
activate plasma membrane phospholipase A2 and its pore-forming
activity. {ECO:0000250|UniProtKB:P01501}.
-!- SUBUNIT: Monomer (in solution and for integration into membranes),
homotetramer (in solution and potentially as a toroidal pore in
membranes), and potenially homomultimer (as a toroidal pore in
membranes). {ECO:0000250|UniProtKB:P01501}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:12939801}.
Target cell membrane {ECO:0000250|UniProtKB:P01501}. Note=Alpha-
helical peptides form toroidal pores in the prey.
{ECO:0000250|UniProtKB:P01501}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
{ECO:0000305|PubMed:12939801}.
-!- ALLERGEN: Causes an allergic reaction in human.
{ECO:0000250|UniProtKB:P01501}.
-!- SIMILARITY: Belongs to the melittin family. {ECO:0000305}.
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EMBL; AF487911; AAO12205.1; -; mRNA.
ProteinModelPortal; P59262; -.
SMR; P59262; -.
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.
3: Inferred from homology;
Allergen; Amidation; Antimicrobial; Cytolysis; Formylation; Hemolysis;
Ion transport; Membrane; Porin; Secreted; Signal;
Target cell membrane; Target membrane; Toxin; Transmembrane;
Transport.
SIGNAL 1 21 {ECO:0000250}.
PROPEP 22 43 Removed by a dipeptidylpeptidase.
{ECO:0000250}.
/FTId=PRO_0000035152.
PEPTIDE 44 69 Melittin. {ECO:0000250|UniProtKB:P01501}.
/FTId=PRO_0000035153.
SITE 57 57 Important for the flexibility at the
center of the helix, flexibility that is
important for the stability of the
voltage-gated pore.
{ECO:0000250|UniProtKB:P01501}.
MOD_RES 44 44 N-formylglycine; partial.
{ECO:0000250|UniProtKB:P01501}.
MOD_RES 69 69 Glutamine amide.
{ECO:0000250|UniProtKB:P01501}.
SEQUENCE 70 AA; 7585 MW; 607F52C091C23BB6 CRC64;
MKFLVNVALV FMVVYISYIY AAPEPEPAPE PEAEADAEAD PEAGIGAVLK VLTTGLPALI
SWIKRKRQQG


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