ID   NDB4C_ANDAM             Reviewed;          74 AA.
AC   G8YYA6;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Antimicrobial peptide 2 {ECO:0000303|PubMed:22484288};
DE            Short=AamAP2 {ECO:0000303|PubMed:22484288};
DE   AltName: Full=Non-disulfide-bridged peptide 4.12 {ECO:0000303|PubMed:24184590};
DE            Short=NDBP-4.12 {ECO:0000303|PubMed:24184590};
DE   Flags: Precursor;
OS   Androctonus amoreuxi (African fattail scorpion) (Scorpio amoreuxi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Androctonus.
OX   NCBI_TaxID=112024;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-40, FUNCTION, AMIDATION
RP   AT LYS-40, AND MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=22484288; DOI=10.1016/j.peptides.2012.03.016;
RA   Almaaytah A., Zhou M., Wang L., Chen T., Walker B., Shaw C.;
RT   "Antimicrobial/cytolytic peptides from the venom of the North African
RT   scorpion, Androctonus amoreuxi: biochemical and functional characterization
RT   of natural peptides and a single site-substituted analog.";
RL   Peptides 35:291-299(2012).
RN   [2]
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: Has antibacterial activity against the Gram-positive bacteria
CC       S.aureus (MIC=48 uM), the Gram-negative bacteria E.coli (MIC=120 uM),
CC       and the yeast C.albicans (MIC=64 uM). Causes hemolysis on horse
CC       erythrocytes. {ECO:0000269|PubMed:22484288}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Target cell membrane. Note=Forms a
CC       helical membrane channel in the prey.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=1880.93; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:22484288};
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; FR821614; CBZ41127.1; -; mRNA.
DR   AlphaFoldDB; G8YYA6; -.
DR   PRIDE; G8YYA6; -.
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:0042742; P:defense response to bacterium; 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; Direct protein sequencing; Hemolysis; Membrane; Secreted;
KW   Signal; Target cell membrane; Target membrane; Transmembrane.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:22484288"
FT   PEPTIDE         23..40
FT                   /note="Antimicrobial peptide 2"
FT                   /id="PRO_5000827074"
FT   PROPEP          46..74
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_5000827073"
FT   MOD_RES         40
FT                   /note="Lysine amide"
FT                   /evidence="ECO:0000269|PubMed:22484288"
SQ   SEQUENCE   74 AA;  8539 MW;  C869F8B134A48725 CRC64;
     MEIKYLLTVF LVLLIVSDHC QAFPFSLIPH AIGGLISAIK GRRKRDLDGQ IDRSRNFRKR
     DAELEELLSK LPIY