ID   ANDT_ANDAU              Reviewed;          25 AA.
AC   P56684; P81616;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Androctonin;
OS   Androctonus australis (Sahara scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Androctonus.
OX   NCBI_TaxID=6858;
RN   [1]
RP   PROTEIN SEQUENCE, CHARACTERIZATION, MASS SPECTROMETRY, AND SYNTHESIS.
RC   STRAIN=Hector; TISSUE=Hemolymph;
RX   PubMed=8939880; DOI=10.1074/jbc.271.47.29537;
RA   Ehret-Sabatier L., Loew D., Goyffon M., Fehlbaum P., Hoffmann J.A.,
RA   van Dorsselaer A., Bulet P.;
RT   "Characterization of novel cysteine-rich antimicrobial peptides from
RT   scorpion blood.";
RL   J. Biol. Chem. 271:29537-29544(1996).
RN   [2]
RP   SYNTHESIS OF D-AMINO ACID ENANTIOMER, AND CHARACTERIZATION.
RC   STRAIN=Hector;
RX   PubMed=10642525; DOI=10.1042/bj3450653;
RA   Hetru C., Letellier L., Oren Z., Hoffmann J.A., Shai Y.;
RT   "Androctonin, a hydrophilic disulphide-bridged non-haemolytic anti-
RT   microbial peptide: a plausible mode of action.";
RL   Biochem. J. 345:653-664(2000).
RN   [3]
RP   STRUCTURE BY NMR.
RC   STRAIN=Hector;
RX   PubMed=10563585; DOI=10.1080/07391102.1999.10508368;
RA   Mandard N., Sy D., Maufrais C., Bonmatin J.-M., Bulet P., Hetru C.,
RA   Vovelle F.;
RT   "Androctonin, a novel antimicrobial peptide from scorpion Androctonus
RT   australis: solution structure and molecular dynamics simulations in the
RT   presence of a lipid monolayer.";
RL   J. Biomol. Struct. Dyn. 17:367-380(1999).
CC   -!- FUNCTION: Active against both bacteria (Gram-positive and Gram-
CC       negative) and filamentous fungi. Acts on the membrane of the bacterial
CC       cells. It destabilize a membrane by modifying its properties.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MASS SPECTROMETRY: Mass=3076.7; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:8939880};
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DR   PDB; 1CZ6; NMR; -; A=1-25.
DR   PDBsum; 1CZ6; -.
DR   AlphaFoldDB; P56684; -.
DR   SMR; P56684; -.
DR   EvolutionaryTrace; P56684; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW   Disulfide bond; Fungicide; Secreted.
FT   PEPTIDE         1..25
FT                   /note="Androctonin"
FT                   /id="PRO_0000043596"
FT   DISULFID        4..20
FT   DISULFID        10..16
FT   STRAND          6..9
FT                   /evidence="ECO:0007829|PDB:1CZ6"
FT   STRAND          12..14
FT                   /evidence="ECO:0007829|PDB:1CZ6"
FT   STRAND          17..20
FT                   /evidence="ECO:0007829|PDB:1CZ6"
SQ   SEQUENCE   25 AA;  3081 MW;  D4183D6EA5AA50AA CRC64;
     RSVCRQIKIC RRRGGCYYKC TNRPY