ID   NDB46_MESEU             Reviewed;          70 AA.
AC   E4VP07; E4VP35;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Venom antimicrobial peptide-6;
DE   AltName: Full=MeAMP-like toxin;
DE   AltName: Full=Meucin-13;
DE   AltName: Full=Non-disulfide bridged protein family 5;
DE            Short=NDBP-5;
DE   AltName: Full=Non-disulfide-bridged peptide 4.6 {ECO:0000303|PubMed:24184590};
DE            Short=NDBP-4.6 {ECO:0000303|PubMed:24184590};
DE   AltName: Full=VAMP-2;
DE   Flags: Precursor;
OS   Mesobuthus eupeus (Lesser Asian scorpion) (Buthus eupeus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX   NCBI_TaxID=34648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CIRCULAR DICHROISM ANALYSIS, AND
RP   STRUCTURE BY NMR.
RC   TISSUE=Venom gland;
RX   PubMed=19088182; DOI=10.1096/fj.08-122317;
RA   Gao B., Sherman P., Luo L., Bowie J., Zhu S.;
RT   "Structural and functional characterization of two genetically related
RT   meucin peptides highlights evolutionary divergence and convergence in
RT   antimicrobial peptides.";
RL   FASEB J. 23:1230-1245(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=23486842; DOI=10.5812/ircmj.4024;
RA   Farajzadeh-Sheikh A., Jolodar A., Ghaemmaghami S.;
RT   "Sequence characterization of cDNA sequence of encoding of an antimicrobial
RT   peptide with no disulfide bridge from the Iranian Mesobuthus eupeus
RT   venomous glands.";
RL   Iran. Red Crescent Med. J. 15:36-41(2013).
RN   [3]
RP   NOMENCLATURE.
RX   PubMed=24184590; DOI=10.1016/j.peptides.2013.10.021;
RA   Almaaytah A., Albalas Q.;
RT   "Scorpion venom peptides with no disulfide bridges: a review.";
RL   Peptides 51:35-45(2014).
CC   -!- FUNCTION: Amphipathic peptide that exhibits extensive cytolytic
CC       activities against both prokaryotic and eukaryotic cells. Is more
CC       potent against Gram-positive bacteria (lethal concentration (LC)=0.25-
CC       2.9 uM) than against Gram-negative bacteria (LC=6.2->50 uM), and fungi
CC       ((LC)=14.1->50 uM). Shows hemolytic activity against rabbit
CC       erythrocytes (37.7% of inhibition at 6.25 uM) and cytolysis against rat
CC       dorsal root ganglions. In vivo, intravenous injection into mice tail
CC       provokes uncomfortable symptoms with a death rate of 12.5%.
CC       {ECO:0000269|PubMed:19088182}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Target cell membrane
CC       {ECO:0000250}. Note=Forms a helical membrane channel in the prey.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP)
CC       superfamily. Short antimicrobial peptide (group 4) family.
CC       {ECO:0000305}.
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DR   EMBL; EF442055; ABR20120.1; -; mRNA.
DR   EMBL; EF445077; ABR21052.1; -; mRNA.
DR   AlphaFoldDB; E4VP07; -.
DR   SMR; E4VP07; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW   Cytolysis; Fungicide; Hemolysis; Membrane; Secreted; Signal;
KW   Target cell membrane; Target membrane; Toxin; Transmembrane.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   PEPTIDE         24..36
FT                   /note="Venom antimicrobial peptide-6"
FT                   /id="PRO_0000418791"
FT   PROPEP          40..70
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000418792"
FT   MOD_RES         36
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        24..25
FT                   /note="IF -> FI (in Ref. 2; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        28
FT                   /note="I -> V (in Ref. 2; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        52
FT                   /note="D -> I (in Ref. 2; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   70 AA;  7985 MW;  6E36D329F19384E0 CRC64;
     MKSQTFFLLF LVVFLLAITQ SEAIFGAIAG LLKNIFGKRS LRDMDTMKYL YDPSLSAADL
     KTLQKLMENY