MEL_APICC
ID MEL_APICC Reviewed; 70 AA.
AC P68407; A0A2A3EE60; P59260;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2019, sequence version 3.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Melittin {ECO:0000303|Ref.1};
DE Short=MEL;
DE Short=MLT;
DE Flags: Precursor;
GN Name=MELT;
OS Apis cerana cerana (Oriental honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC Apis.
OX NCBI_TaxID=94128;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Venom gland;
RA Li J.-H., Zhang C.-X.;
RT "Transcription and expression of melittin gene in the venom gland of the
RT Chinese honeybee, Apis cerana.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Diao Q., Sun L., Zheng H., Zheng H., Xu S., Wang S., Zeng Z., Hu F., Su S.,
RA Wu J.;
RT "Genomic and transcriptomic analysis on Apis cerana provide comprehensive
RT insights into honey bee biology.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Main toxin of bee venom with strong hemolytic activity and
CC antimicrobial activity. It has enhancing effects on bee venom
CC phospholipase A2 activity. This amphipathic toxin binds to negatively
CC charged membrane surface and forms pore by inserting into lipid
CC bilayers inducing the leakage of ions and molecules and the enhancement
CC of permeability that ultimately leads to cell lysis. It acts as a
CC voltage-gated pore with higher selectivity for anions over cations. The
CC ion conductance has been shown to be voltage-dependent. Self-
CC association of melittin in membranes is promoted by high ionic
CC strength, but not by the presence of negatively charged lipids. In
CC vivo, intradermal injection into healthy human volunteers produce sharp
CC pain sensation and an inflammatory response. It produces pain by
CC activating primary nociceptor cells directly and indirectly due to its
CC ability to activate plasma membrane phospholipase A2 and its pore-
CC forming activity. {ECO:0000250|UniProtKB:P01501}.
CC -!- SUBUNIT: Monomer (in solution and for integration into membranes),
CC homotetramer (in solution and potentially as a toroidal pore in
CC membranes), and potenially homomultimer (as a toroidal pore in
CC membranes). {ECO:0000250|UniProtKB:P01501}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|Ref.1}. Target cell
CC membrane {ECO:0000250|UniProtKB:P01501}. Note=Alpha-helical peptides
CC form toroidal pores in the prey. {ECO:0000250|UniProtKB:P01501}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.1}.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC {ECO:0000250|UniProtKB:P01501}.
CC -!- SIMILARITY: Belongs to the melittin family. {ECO:0000305}.
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DR EMBL; AF487907; AAO12201.2; -; mRNA.
DR EMBL; AJ786346; CAH05131.1; -; Genomic_DNA.
DR EMBL; KZ288269; PBC29998.1; -; Genomic_DNA.
DR AlphaFoldDB; P68407; -.
DR Proteomes; UP000242457; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR002116; Melittin/Api_allergen.
DR Pfam; PF01372; Melittin; 1.
PE 3: Inferred from homology;
KW Allergen; Amidation; Antimicrobial; Cytolysis; Formylation; Hemolysis;
KW Ion transport; Membrane; Porin; Reference proteome; Secreted; Signal;
KW Target cell membrane; Target membrane; Toxin; Transmembrane; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT PROPEP 22..43
FT /note="Removed by a dipeptidylpeptidase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000035144"
FT PEPTIDE 44..69
FT /note="Melittin"
FT /evidence="ECO:0000250|UniProtKB:P01501"
FT /id="PRO_0000035145"
FT SITE 57
FT /note="Important for the flexibility at the center of the
FT helix, flexibility that is important for the stability of
FT the voltage-gated pore"
FT /evidence="ECO:0000250|UniProtKB:P01501"
FT MOD_RES 44
FT /note="N-formylglycine; partial"
FT /evidence="ECO:0000250|UniProtKB:P01501"
FT MOD_RES 69
FT /note="Glutamine amide"
FT /evidence="ECO:0000250|UniProtKB:P01501"
FT CONFLICT 61
FT /note="S -> G (in Ref. 1; AAO12201)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 70 AA; 7543 MW; DA6B17C086C9560C CRC64;
MKFLVNVALV FMVVYISFIY AAPEPEPAPE AEAEADAEAD PEAGIGAVLK VLTTGLPALI
SWIKRKRQQG
