ID   NDB4T_HETPE             Reviewed;          67 AA.
AC   P0DME6;
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 Hp1036 {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 PHE-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 antibacterial activities (By
CC       similarity). Shows antiviral activities against the herpes simplex
CC       virus type-1. It potently inhibits the initial infection by provoking
CC       the rupture of viral envelop and the dissociation of proteins from the
CC       virions (EC(50) is 0.43 uM). It also effectively inhibits viral
CC       attachment (EC(50) is 2.87 uM), viral entry (EC(50) is 4.29 uM) and
CC       viral proliferation after infection (EC(50) is 7.86). Morever, it
CC       enters mammalian tested cells (Vero) and reduces the intracellular
CC       infectivity. {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; P0DME6; -.
DR   SMR; P0DME6; -.
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:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Antibiotic; Antimicrobial; Antiviral protein;
KW   Cleavage on pair of basic residues; Membrane; Secreted; Signal;
KW   Target cell membrane; Target membrane.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         24..36
FT                   /note="Peptide Hp1036"
FT                   /evidence="ECO:0000305|PubMed:24315793"
FT                   /id="PRO_0000428684"
FT   PROPEP          40..67
FT                   /evidence="ECO:0000305|PubMed:24315793"
FT                   /id="PRO_0000428685"
FT   MOD_RES         36
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000305|PubMed:24315793"
SQ   SEQUENCE   67 AA;  7627 MW;  653EAD53B22FE2C8 CRC64;
     MKTQFAILLI TLVLFQMFSQ SDAILGKIWE GIKSIFGKRG LNDLSDLDEL FDGEISEADV
     DFLREIM