ID   NA122_ANTEL             Reviewed;          47 AA.
AC   P0C1F3;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Delta-actitoxin-Ael1d {ECO:0000303|PubMed:22683676};
DE            Short=Delta-AITX-Ael1d {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Toxin APE 2-2 {ECO:0000303|PubMed:11072049};
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, AND SUBCELLULAR LOCATION.
RX   PubMed=11072049; DOI=10.1016/s0041-0101(00)00199-9;
RA   Bruhn T., Schaller C., Schulze C., Sanchez-Rodriguez J., Dannmeier C.,
RA   Ravens U., Heubach J.F., Eckhardt K., Schmidtmayer J., Schmidt H.,
RA   Aneiros A., Wachter E., Beress L.;
RT   "Isolation and characterisation of five neurotoxic and cardiotoxic
RT   polypeptides from the sea anemone Anthopleura elegantissima.";
RL   Toxicon 39:693-702(2001).
RN   [2]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=22048953; DOI=10.1098/rspb.2011.1731;
RA   Moran Y., Genikhovich G., Gordon D., Wienkoop S., Zenkert C., Ozbek S.,
RA   Technau U., Gurevitz M.;
RT   "Neurotoxin localization to ectodermal gland cells uncovers an alternative
RT   mechanism of venom delivery in sea anemones.";
RL   Proc. R. Soc. B 279:1351-1358(2012).
RN   [3]
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: Modifies current passing through the fast sodium channel
CC       (Nav) in neuroblastoma cells, leading to delayed and incomplete
CC       inactivation. Produces a positive inotropic effect in mammalian heart
CC       muscle (By similarity). Paralyzes the shore crab (C.maenas) by tetanic
CC       contractions after intramuscular injection. {ECO:0000250,
CC       ECO:0000269|PubMed:11072049}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11072049}.
CC   -!- TISSUE SPECIFICITY: Expressed in ectodermal glands. Not expressed in
CC       nematocytes. {ECO:0000305|PubMed:22048953}.
CC   -!- SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin
CC       family. Type I subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C1F3; -.
DR   SMR; P0C1F3; -.
DR   GO; GO:0005576; C:extracellular region; 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   Cardiotoxin; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..47
FT                   /note="Delta-actitoxin-Ael1d"
FT                   /evidence="ECO:0000269|PubMed:11072049"
FT                   /id="PRO_0000236027"
FT   DISULFID        4..44
FT                   /evidence="ECO:0000250|UniProtKB:P10454"
FT   DISULFID        6..34
FT                   /evidence="ECO:0000250|UniProtKB:P10454"
FT   DISULFID        27..45
FT                   /evidence="ECO:0000250|UniProtKB:P10454"
SQ   SEQUENCE   47 AA;  4911 MW;  BA0AFF7A43AF29CB CRC64;
     GVPCLCDSDG PNVRGNTLSG ILWLAGCPSG WHNCKAHGPT IGWCCKQ