ID   NDB4U_HETPE             Reviewed;          67 AA.
AC   P0DME7;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Peptide Hp1165 {ECO:0000303|PubMed:24315793};
DE   Flags: Precursor;
OS   Heterometrus petersii (Asian forest scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Scorpionoidea; Scorpionidae; Heterometrinae;
OC   Heterometrus.
OX   NCBI_TaxID=754296;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=20443192; DOI=10.1002/pmic.200900763;
RA   Ma Y., Zhao Y., Zhao R., Zhang W., He Y., Wu Y., Cao Z., Guo L., Li W.;
RT   "Molecular diversity of toxic components from the scorpion Heterometrus
RT   petersii venom revealed by proteomic and transcriptome analysis.";
RL   Proteomics 10:2471-2485(2010).
RN   [2]
RP   SYNTHESIS OF 24-36, FUNCTION, AND PROBABLE AMIDATION AT LEU-36.
RX   PubMed=24315793; DOI=10.1016/j.antiviral.2013.11.013;
RA   Hong W., Li T., Song Y., Zhang R., Zeng Z., Han S., Zhang X., Wu Y., Li W.,
RA   Cao Z.;
RT   "Inhibitory activity and mechanism of two scorpion venom peptides against
RT   herpes simplex virus type 1.";
RL   Antiviral Res. 102:1-10(2014).
CC   -!- FUNCTION: Amphipathic peptide with antimicrobial activity (By
CC       similarity). Does not show antiviral activity (PubMed:24315793).
CC       {ECO:0000250, ECO:0000269|PubMed:24315793}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Target cell membrane
CC       {ECO:0000250}. Note=Forms an alpha-helical membrane channel in the
CC       prey. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:20443192}.
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   AlphaFoldDB; P0DME7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Antimicrobial; Cleavage on pair of basic residues; Membrane;
KW   Secreted; Signal; Target cell membrane; Target membrane.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         24..36
FT                   /note="Peptide Hp1165"
FT                   /evidence="ECO:0000305|PubMed:24315793"
FT                   /id="PRO_0000428686"
FT   PROPEP          40..67
FT                   /evidence="ECO:0000305|PubMed:24315793"
FT                   /id="PRO_0000428687"
FT   MOD_RES         36
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000305|PubMed:24315793"
SQ   SEQUENCE   67 AA;  7634 MW;  32AD16DDA227405D CRC64;
     MKTQFAILLI TLVLFQMFSQ SDAILGEIWK GIKDILGKRG LNDLSDLDEL FDGEISKADL
     DFLREIM