ID   NA2H_HALCG              Reviewed;          47 AA.
AC   P0C5G6;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Delta-halcutoxin-Hcg1a {ECO:0000303|PubMed:22683676};
DE            Short=Delta-HCTX-Hcg1a {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Halcurin {ECO:0000303|PubMed:9133708};
OS   Halcurias carlgreni (Sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Endocoelantheae; Halcuriidae; Halcurias.
OX   NCBI_TaxID=462315;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TOXIC DOSE, AND MASS
RP   SPECTROMETRY.
RX   PubMed=9133708; DOI=10.1016/s0041-0101(96)00143-2;
RA   Ishida M., Yokoyama A., Shimakura K., Nagashima Y., Shiomi K.;
RT   "Halcurin, a polypeptide toxin from the sea anemone Halcurias sp., with a
RT   structural resemblance to type 1 and 2 toxins.";
RL   Toxicon 35:537-544(1997).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=22683676; DOI=10.1016/j.toxicon.2012.05.020;
RA   Oliveira J.S., Fuentes-Silva D., King G.F.;
RT   "Development of a rational nomenclature for naming peptide and protein
RT   toxins from sea anemones.";
RL   Toxicon 60:539-550(2012).
CC   -!- FUNCTION: Is potently lethal to crabs, although it showed neither
CC       lethal activity in mice nor hemolytic activity. May bind to voltage-
CC       gated sodium channels (Nav), thereby delaying their inactivation during
CC       signal transduction. {ECO:0000269|PubMed:9133708}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9133708}. Nematocyst
CC       {ECO:0000305|PubMed:9133708}.
CC   -!- MASS SPECTROMETRY: Mass=5074; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:9133708};
CC   -!- TOXIC DOSE: LD(50) is 5.8 ug/kg against crabs.
CC       {ECO:0000269|PubMed:9133708}.
CC   -!- SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin
CC       family. Type II subfamily. {ECO:0000305}.
CC   -!- CAUTION: This toxin probably comes from Halcurias carlgreni, although
CC       the identification is not definitive. {ECO:0000305}.
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DR   AlphaFoldDB; P0C5G6; -.
DR   SMR; P0C5G6; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR   Gene3D; 2.20.20.10; -; 1.
DR   InterPro; IPR000693; Anenome_toxin.
DR   InterPro; IPR023355; Myo_ane_neurotoxin_sf.
DR   PIRSF; PIRSF001905; Anenome_toxin; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Nematocyst; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   PEPTIDE         1..47
FT                   /note="Delta-halcutoxin-Hcg1a"
FT                   /evidence="ECO:0000269|PubMed:9133708"
FT                   /id="PRO_0000305120"
FT   DISULFID        3..43
FT                   /evidence="ECO:0000250|UniProtKB:P19651"
FT   DISULFID        5..33
FT                   /evidence="ECO:0000250|UniProtKB:P19651"
FT   DISULFID        26..44
FT                   /evidence="ECO:0000250|UniProtKB:P19651"
SQ   SEQUENCE   47 AA;  5086 MW;  B8B008C5C89716F7 CRC64;
     VACRCESDGP DVRSATFTGT VDLWNCNTGW HKCIATYTAV ASCCKKD