ID   BDS3_ANTEL              Reviewed;          42 AA.
AC   B3EWF9;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Delta-actitoxin-Ael2d {ECO:0000303|PubMed:22683676};
DE            Short=Delta-AITX-Ael2d {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Toxin APETx3 {ECO:0000303|PubMed:22972919};
OS   Anthopleura elegantissima (Green aggregating anemone) (Actinia
OS   elegantissima).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Anthopleura.
OX   NCBI_TaxID=6110;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=22972919; DOI=10.1096/fj.12-218479;
RA   Peigneur S., Beress L., Moeller C., Mari F., Forssmann W.G., Tytgat J.;
RT   "A natural point mutation changes both target selectivity and mechanism of
RT   action of sea anemone toxins.";
RL   FASEB J. 26:5141-5151(2012).
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: Binds to voltage-gated sodium channels (Nav), and slows down
CC       the inactivation of mammalian Nav1.2/SCN2A, Nav1.3/SCN3A Nav1.4/SCN4A,
CC       Nav1.6/SCN8A, insect DmNav1 and BgNav1 channels, and arachnid VdNav1
CC       channel (PubMed:22972919). This toxin acts by binding to site 3 of
CC       sodium channels. {ECO:0000269|PubMed:22972919}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22972919,
CC       ECO:0000305}. Nematocyst {ECO:0000269|PubMed:22972919, ECO:0000305}.
CC   -!- DOMAIN: Has the CSbeta/beta fold, which comprises anti-parallel beta-
CC       sheets stabilized by three or four disulfide bonds.
CC       {ECO:0000250|UniProtKB:P61541}.
CC   -!- MASS SPECTROMETRY: Mass=4544.7; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:22972919};
CC   -!- MISCELLANEOUS: Has no effect on Nav1.5, Nav1.7 and Nav1.8 sodium
CC       channels and on Kv1.1, Kv1.2, Kv1.3, Kv1.4, Kv1.5, Kv1.6, Kv2.1, Kv3.1,
CC       Kv4.2, Kv4.3, Kv7.2, Kv7.4, Kv11.1/KCNH2/ERG1, and Shaker potassium
CC       channels. {ECO:0000269|PubMed:22972919}.
CC   -!- SIMILARITY: Belongs to the sea anemone type 3 (BDS) potassium channel
CC       toxin family. {ECO:0000255}.
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DR   AlphaFoldDB; B3EWF9; -.
DR   SMR; B3EWF9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.20.20.10; -; 1.
DR   InterPro; IPR012414; BDS_K_chnl_tox.
DR   InterPro; IPR023355; Myo_ane_neurotoxin_sf.
DR   Pfam; PF07936; Defensin_4; 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   CHAIN           1..42
FT                   /note="Delta-actitoxin-Ael2d"
FT                   /evidence="ECO:0000269|PubMed:22972919"
FT                   /id="PRO_0000415949"
FT   DISULFID        4..37
FT                   /evidence="ECO:0000250|UniProtKB:P61541"
FT   DISULFID        6..30
FT                   /evidence="ECO:0000250|UniProtKB:P61541"
FT   DISULFID        20..38
FT                   /evidence="ECO:0000250|UniProtKB:P61541"
SQ   SEQUENCE   42 AA;  4554 MW;  B012C408814B3713 CRC64;
     GTPCYCGKTI GIYWFGTKTC PSNRGYTGSC GYFLGICCYP VD