ID   NDB4T_HOFGE             Reviewed;          68 AA.
AC   P0C8W2;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Non-disulfide-bridged peptide 5.6 {ECO:0000303|PubMed:17506894};
DE            Short=NDBP-5.6 {ECO:0000303|PubMed:17506894};
DE   Flags: Precursor;
OS   Hoffmannihadrurus gertschi (Scorpion) (Hadrurus gertschi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Iuroidea; Hadrurus.
OX   NCBI_TaxID=380989;
RN   [1] {ECO:0000312|EMBL:EL698902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND NOMENCLATURE.
RC   TISSUE=Venom gland;
RX   PubMed=17506894; DOI=10.1186/1471-2164-8-119;
RA   Schwartz E.F., Diego-Garcia E., Rodriguez de la Vega R.C., Possani L.D.;
RT   "Transcriptome analysis of the venom gland of the Mexican scorpion Hadrurus
RT   gertschi (Arachnida: Scorpiones).";
RL   BMC Genomics 8:119-119(2007).
RN   [2]
RP   FUNCTION, AND SYNTHESIS OF 24-33.
RX   PubMed=27917162; DOI=10.3389/fmicb.2016.01844;
RA   Guilhelmelli F., Vilela N., Smidt K.S., de Oliveira M.A.,
RA   da Cunha Morales Alvares A., Rigonatto M.C., da Silva Costa P.H.,
RA   Tavares A.H., de Freitas S.M., Nicola A.M., Franco O.L., Derengowski L.D.,
RA   Schwartz E.F., Mortari M.R., Bocca A.L., Albuquerque P., Silva-Pereira I.;
RT   "Activity of scorpion venom-derived antifungal peptides against planktonic
RT   cells of Candida spp. and Cryptococcus neoformans and Candida albicans
RT   biofilms.";
RL   Front. Microbiol. 7:1844-1844(2016).
CC   -!- FUNCTION: Antibacterial peptide with activity against both Gram-
CC       positive and Gram-negative bacteria probably by forming pores in the
CC       cell membrane (By similarity). Has also weak hemolytic activity (By
CC       similarity). Does not show antifungal activity (PubMed:27917162).
CC       {ECO:0000250|UniProtKB:I0DEB6, ECO:0000269|PubMed:27917162}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Target cell membrane
CC       {ECO:0000305}. Note=Forms an alpha-helical membrane channel in the
CC       prey. {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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   EMBL; EL698902; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0C8W2; -.
DR   SMR; P0C8W2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Cytolysis; Ion transport; Membrane;
KW   Secreted; Signal; Target cell membrane; Target membrane; Toxin;
KW   Transmembrane; Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         24..33
FT                   /note="Non-disulfide-bridged peptide 5.6"
FT                   /evidence="ECO:0000305|PubMed:27917162"
FT                   /id="PRO_0000366099"
FT   PROPEP          37..68
FT                   /evidence="ECO:0000305|PubMed:27917162"
FT                   /id="PRO_0000366100"
SQ   SEQUENCE   68 AA;  8009 MW;  87ECF05370E515F2 CRC64;
     MKTQVIIFIM AVVFLQLLSQ SEAFIFDLLK KLVGKRELRN IDLDQFDDMF DEPEISAADM
     RFLQELLK