MELS_APICE
ID MELS_APICE Reviewed; 77 AA.
AC Q8LW54;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Melittin {ECO:0000303|Ref.2};
DE Short=MEL;
DE Short=MLT;
DE Flags: Precursor;
GN Name=MELT;
OS Apis cerana (Indian honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC Apis.
OX NCBI_TaxID=7461;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Le H.Q., Le B.T.;
RT "Gene encoding melittin in honeybee Apis cerana colleted in Hanoi
RT Vietnam.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 51-76, AMIDATION AT GLN-76, AND SUBCELLULAR LOCATION.
RA Kreil G.;
RT "Structure of melittin isolated from two species of honey bees.";
RL FEBS Lett. 33:241-244(1973).
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:0000269|Ref.2}. 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.2}.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC {ECO:0000250|UniProtKB:P01501}.
CC -!- SIMILARITY: Belongs to the melittin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Why Pooh luvvs hunny - Issue
CC 12 of July 2001;
CC URL="https://web.expasy.org/spotlight/back_issues/012";
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DR EMBL; AJ489619; CAD33921.1; -; Genomic_DNA.
DR PIR; A01762; MEHBCI.
DR AlphaFoldDB; Q8LW54; -.
DR BMRB; Q8LW54; -.
DR SMR; Q8LW54; -.
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 1: Evidence at protein level;
KW Allergen; Amidation; Antimicrobial; Cytolysis; Direct protein sequencing;
KW Formylation; Hemolysis; Ion transport; Membrane; Porin; Secreted; Signal;
KW Target cell membrane; Target membrane; Toxin; Transmembrane; Transport.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT PROPEP 31..50
FT /note="Removed by a dipeptidylpeptidase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000035146"
FT PEPTIDE 51..76
FT /note="Melittin"
FT /evidence="ECO:0000269|Ref.2"
FT /id="PRO_0000035147"
FT SITE 64
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 51
FT /note="N-formylglycine; partial"
FT /evidence="ECO:0000250|UniProtKB:P01501"
FT MOD_RES 76
FT /note="Glutamine amide"
FT /evidence="ECO:0000269|Ref.2"
SQ SEQUENCE 77 AA; 8515 MW; 091BEF7CE6019374 CRC64;
MKFLVNVALV FYGRVHFLHL CVHFLHLWAP EPEPAPEAEA EADAEADPEA GIGAVLKVLT
TGLPALISWI KRKRQQG