ID   NDB4S_HETPE             Reviewed;          70 AA.
AC   P0DJ03;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Peptide Hp1035 {ECO:0000303|PubMed:20950663};
DE   AltName: Full=Non-disulfide-bridged peptide 5.10 {ECO:0000303|PubMed:22342498};
DE            Short=NDBP-5.10 {ECO:0000303|PubMed:22342498};
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   NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 24-36, AND CIRCULAR DICHROISM.
RC   TISSUE=Venom gland;
RX   PubMed=20950663; DOI=10.1016/j.peptides.2010.10.008;
RA   Yan R., Zhao Z., He Y., Wu L., Cai D., Hong W., Wu Y., Cao Z., Zheng C.,
RA   Li W.;
RT   "A new natural alpha-helical peptide from the venom of the scorpion
RT   Heterometrus petersii kills HCV.";
RL   Peptides 32:11-19(2011).
RN   [3]
RP   SYNTHESIS OF 24-36, AND FUNCTION.
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).
RN   [4]
RP   NOMENCLATURE.
RX   PubMed=22342498; DOI=10.1016/j.peptides.2012.02.002;
RA   Ramirez-Carreto S., Quintero-Hernandez V., Jimenez-Vargas J.M., Corzo G.,
RA   Possani L.D., Becerril B., Ortiz E.;
RT   "Gene cloning and functional characterization of four novel antimicrobial-
RT   like peptides from scorpions of the family Vaejovidae.";
RL   Peptides 34:290-295(2012).
CC   -!- FUNCTION: Amphipathic peptide with antimicrobial activity.
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   -!- MISCELLANEOUS: Does not show antiviral activity.
CC       {ECO:0000305|PubMed:24315793}.
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; P0DJ03; -.
DR   SMR; P0DJ03; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript 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 Hp1035"
FT                   /id="PRO_0000412877"
FT   PROPEP          40..70
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000412878"
FT   MOD_RES         36
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   70 AA;  7917 MW;  301A51F0B7E5DC06 CRC64;
     MKTQFVILLV ALVLFQMFAQ SEAIFSAIGG FLKSIFGKRG LQDLDMDDLD QLFDGEISQA
     DINFLNQLMR