ID   AMP1_HETSP              Reviewed;          74 AA.
AC   P0DMI7; A0A096VHN4;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   14-MAY-2014, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Antimicrobial peptide HsAp1 {ECO:0000303|PubMed:23000095, ECO:0000305};
DE            Short=HsAp {ECO:0000303|PubMed:23000095};
DE   AltName: Full=Non-disulfide-bridged peptide 3.3 {ECO:0000303|PubMed:24184590};
DE            Short=NDBP-3.3 {ECO:0000303|PubMed:24184590};
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], SYNTHESIS OF 37-65, AMIDATION AT
RP   PRO-65, AND FUNCTION.
RC   TISSUE=Venom gland;
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).
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: Possesses antimicrobial activity against both Gram-negative
CC       (MIC between 23.8 and 51.2 uM) and Gram-positive (MIC between 11.8 and
CC       46.5 uM) bacteria, as well as against the fungus C.tropicalis (MIC of
CC       48.6 uM). Also possesses a relatively high hemolytic activity.
CC       {ECO:0000269|PubMed:23000095}.
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.
CC       {ECO:0000305|PubMed:23000095}.
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; JX311701; AFR60584.1; -; mRNA.
DR   AlphaFoldDB; P0DMI7; -.
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   1: Evidence at protein level;
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_0000429191"
FT   PEPTIDE         37..65
FT                   /note="Antimicrobial peptide HsAp1"
FT                   /id="PRO_0000429192"
FT   PROPEP          69..74
FT                   /evidence="ECO:0000305|PubMed:23000095"
FT                   /id="PRO_0000429193"
FT   MOD_RES         65
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000305|PubMed:23000095"
SQ   SEQUENCE   74 AA;  8349 MW;  6233CF24F83963A9 CRC64;
     MSRRVILTLV LVTILVKTMA GMESKKVETT DEIKKRSGTS EKERESGRLL GVVKRLIVCF
     RSPFPGRRAI SEQT