ID   NDBW_MESEU              Reviewed;          69 AA.
AC   E4VP50;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Venom antimicrobial peptide-9;
DE   AltName: Full=Meucin-18 {ECO:0000303|PubMed:19088182};
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).
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)=1.5-
CC       10.9 uM) than against Gram-negative bacteria (LC=6.2->50 uM), and fungi
CC       (LC=25.1-8.3 uM). Is lethal to the fungus Beauveria sp (LC=1.9 uM), a
CC       highly lethal pathogenic fungus to insects and resistant to many AMPs.
CC       Shows hemolytic activity against rabbit erythrocytes (37.7% of
CC       inhibition at 6.25 uM) and cytolysis against rat dorsal root ganglions.
CC       In vivo, intravenous injection into mice tail provokes uncomfortable
CC       symptoms with a death rate of 12.5%. {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. Medium-length antimicrobial peptide (group 3) family.
CC       {ECO:0000305}.
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DR   EMBL; EF445092; ABR21067.1; -; mRNA.
DR   AlphaFoldDB; E4VP50; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; 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.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         17..34
FT                   /note="Venom antimicrobial peptide-9"
FT                   /id="PRO_0000418793"
FT   PROPEP          38..69
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000418794"
SQ   SEQUENCE   69 AA;  8400 MW;  A8749AFBE9C3F582 CRC64;
     MVIFLAYFLV VNESEAFFGH LFKLATKIIP SLFQRKKERS VMNRDLENLF DPYQRNLEMD
     RLLKQLRNY