ID   NA1C_ANTEL              Reviewed;          47 AA.
AC   P01532; P0C1F2;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Delta-actitoxin-Ael1a {ECO:0000303|PubMed:22683676};
DE            Short=Delta-AITX-Ael1a {ECO:0000303|PubMed:22683676};
DE   AltName: Full=APE 2-1 {ECO:0000303|PubMed:11072049};
DE   AltName: Full=Anthopleurin-C {ECO:0000303|PubMed:6108877};
DE            Short=AP-C {ECO:0000303|PubMed:6108877};
DE            Short=ApC {ECO:0000305};
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, AND SUBCELLULAR LOCATION.
RX   PubMed=6108877;
RA   Norton T.R.;
RT   "Cardiotonic polypeptides from Anthopleura xanthogrammica (Brandt) and A.
RT   elegantissima (Brandt).";
RL   Fed. Proc. 40:21-25(1981).
RN   [2]
RP   PROTEIN SEQUENCE, FUNCTION, TOXIC DOSE, 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   [3]
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   [4]
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 specifically to voltage-gated sodium channels (Nav),
CC       thereby delaying their inactivation during signal transduction. It
CC       strongly stimulates mammalian cardiac muscle contraction. Paralyzes the
CC       shore crab (C.maenas) by tetanic contractions after intramuscular
CC       injection. {ECO:0000269|PubMed:11072049}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11072049,
CC       ECO:0000269|PubMed:6108877}.
CC   -!- TISSUE SPECIFICITY: Expressed in ectodermal glands. Not expressed in
CC       nematocytes. {ECO:0000305|PubMed:22048953}.
CC   -!- TOXIC DOSE: LD(50) is 1 ug/kg by intramuscular injection into crabs
CC       (C.maenas). {ECO:0000269|PubMed:11072049}.
CC   -!- SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin
CC       family. Type I subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia;
CC       URL="https://en.wikipedia.org/wiki/Anthopleurin";
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DR   PIR; A01793; NAXACE.
DR   AlphaFoldDB; P01532; -.
DR   SMR; P01532; -.
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-Ael1a"
FT                   /evidence="ECO:0000269|PubMed:11072049,
FT                   ECO:0000269|PubMed:6108877"
FT                   /id="PRO_0000221517"
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;  4884 MW;  BA0AFF6AADA1D9CB CRC64;
     GVPCLCDSDG PSVRGNTLSG ILWLAGCPSG WHNCKAHGPT IGWCCKQ