ID   NDB_HETSP               Reviewed;          73 AA.
AC   A0A0C4G5K0;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2015, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=Heterin-2 {ECO:0000303|PubMed:24389272};
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], FUNCTION, SYNTHESIS OF 23-46, AND
RP   MUTAGENESIS OF 44-LYS--ASP-46.
RX   PubMed=24389272; DOI=10.1016/j.peptides.2013.12.012;
RA   Wu S., Nie Y., Zeng X.C., Cao H., Zhang L., Zhou L., Yang Y., Luo X.,
RA   Liu Y.;
RT   "Genomic and functional characterization of three new venom peptides from
RT   the scorpion Heterometrus spinifer.";
RL   Peptides 53:30-41(2014).
CC   -!- FUNCTION: Amphipathic peptide with potent activities against Gram-
CC       positive bacteria (MIC=5.6-30.0 uM) and weaker activities against the
CC       tested Gram-negative bacteria (MIC=15 uM to >45 uM). It has high
CC       hemolytic activity against human erythrocytes.
CC       {ECO:0000269|PubMed:24389272}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:24389272}. Target
CC       cell membrane {ECO:0000305|PubMed:24389272}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:24389272}.
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; KC538869; AGK88595.1; -; mRNA.
DR   EMBL; KC538870; AGK88596.1; -; Genomic_DNA.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0098542; P:defense response to other organism; IEA:InterPro.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR012523; Antimicrobial_4.
DR   Pfam; PF08024; Antimicrobial_4; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Cytolysis; Hemolysis; Membrane;
KW   Secreted; Signal; Target cell membrane; Target membrane.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         23..46
FT                   /note="Heterin-2"
FT                   /evidence="ECO:0000250|UniProtKB:P83240"
FT                   /id="PRO_5007393682"
FT   PROPEP          47..73
FT                   /evidence="ECO:0000305|PubMed:24389272"
FT                   /id="PRO_0000454584"
FT   MUTAGEN         44..46
FT                   /note="Missing: Change in activity and specificity against
FT                   bacteria and decrease in hemolytic activity."
FT                   /evidence="ECO:0000269|PubMed:24389272"
SQ   SEQUENCE   73 AA;  8406 MW;  C4C59731E5852816 CRC64;
     MQYKTFLVIF LAYLLVTEEA LAFWGALAKG ALKLIPSLVS SFTKKDKRAL KNIFDPYQKN
     LDLELERLLS QLQ