ID   AMP4_HETSP              Reviewed;          74 AA.
AC   P0DMJ0; A0A096VHN5;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   14-MAY-2014, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Antimicrobial peptide HsAp4 {ECO:0000303|PubMed:23000095};
DE   Flags: Precursor;
OS   Heterometrus spinifer (Asia giant forest scorpion) (Malaysian black
OS   scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Scorpionoidea; Scorpionidae; Heterometrinae;
OC   Heterometrus.
OX   NCBI_TaxID=118530;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=23000095; DOI=10.1016/j.peptides.2012.09.012;
RA   Nie Y., Zeng X.C., Yang Y., Luo F., Luo X., Wu S., Zhang L., Zhou J.;
RT   "A novel class of antimicrobial peptides from the scorpion Heterometrus
RT   spinifer.";
RL   Peptides 38:389-394(2012).
CC   -!- FUNCTION: Possesses antimicrobial activity against both Gram-negative
CC       and Gram-positive bacteria, as well as against the fungus C.tropicalis.
CC       Also possesses a relatively high hemolytic activity.
CC       {ECO:0000250|UniProtKB:P0DMI7}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Target cell membrane
CC       {ECO:0000250}. Note=Forms a helical membrane channel in the prey.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP)
CC       superfamily. Medium-length antimicrobial peptide (group 3) family.
CC       {ECO:0000305}.
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DR   EMBL; JX311704; AFR60587.1; -; mRNA.
DR   AlphaFoldDB; P0DMJ0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Amidation; Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW   Cytolysis; Fungicide; Membrane; Secreted; Signal; Target cell membrane;
KW   Target membrane.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..33
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000429200"
FT   PEPTIDE         37..65
FT                   /note="Antimicrobial peptide HsAp4"
FT                   /id="PRO_0000429201"
FT   PROPEP          69..74
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000429202"
FT   MOD_RES         65
FT                   /note="Arginine amide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   74 AA;  8555 MW;  696040CBC602FD98 CRC64;
     MSRRRILILV LVTMLVKTMA GMESKWVETT YEIKKRSGTS EKERESGRLL GVVKRLIVGF
     RSPFRGRRAI SEQT