ID   NA11_ANESU              Reviewed;          46 AA.
AC   P01533;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Delta-actitoxin-Avd1a {ECO:0000303|PubMed:22683676};
DE            Short=Delta-AITX-Avd1a {ECO:0000303|PubMed:22683676};
DE   AltName: Full=As1;
DE   AltName: Full=Delta-actitoxin-Avd1b {ECO:0000303|PubMed:22683676};
DE            Short=Delta-AITX-Avd1b {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Toxin ATX-I {ECO:0000303|PubMed:2892680};
DE            Short=ATX I {ECO:0000303|PubMed:2409523};
DE   AltName: Full=Toxin-1 {ECO:0000303|PubMed:29753};
OS   Anemonia sulcata (Mediterranean snakelocks sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Anemonia.
OX   NCBI_TaxID=6108;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Nematoblast;
RX   PubMed=29753; DOI=10.1111/j.1432-1033.1978.tb20890.x;
RA   Wunderer G., Eulitz M.;
RT   "Amino-acid sequence of toxin I from Anemonia sulcata.";
RL   Eur. J. Biochem. 89:11-17(1978).
RN   [2]
RP   FUNCTION.
RX   PubMed=2409523; DOI=10.1007/bf00585406;
RA   Hartung K., Rathmayer W.;
RT   "Anemonia sulcata toxins modify activation and inactivation of Na+ currents
RT   in a crayfish neurone.";
RL   Pflugers Arch. 404:119-125(1985).
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).
RN   [4]
RP   STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX   PubMed=2892680; DOI=10.1111/j.1432-1033.1988.tb13774.x;
RA   Widmer H., Wagner G., Schweitz H., Lazdunski M., Wuethrich K.;
RT   "The secondary structure of the toxin ATX Ia from Anemonia sulcata in
RT   aqueous solution determined on the basis of complete sequence-specific 1H-
RT   NMR assignments.";
RL   Eur. J. Biochem. 171:177-192(1988).
RN   [5]
RP   STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX   PubMed=2576133; DOI=10.1002/prot.340060403;
RA   Widmer H., Billeter M., Wuethrich K.;
RT   "Three-dimensional structure of the neurotoxin ATX Ia from Anemonia sulcata
RT   in aqueous solution determined by nuclear magnetic resonance
RT   spectroscopy.";
RL   Proteins 6:357-371(1989).
CC   -!- FUNCTION: Binds specifically to voltage-gated sodium channels (Nav) and
CC       delays their inactivation during signal transduction (when tested on
CC       the soma membrane of a crustacean neuron). Has also been observed to
CC       affect the activation of the sodium current.
CC       {ECO:0000269|PubMed:2409523}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC   -!- MISCELLANEOUS: Does not have effect on potassium or calcium currents
CC       with concentrations up to 5 uM (PubMed:2409523). Is inactive at
CC       excitable membranes of frog (Inferred fromPubMed:2409523).
CC       {ECO:0000269|PubMed:2409523}.
CC   -!- SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin
CC       family. Type I subfamily. {ECO:0000305}.
CC   -!- CAUTION: Opinions are divided on whether Anemonia viridis (Forsskal,
CC       1775) and Anemonia sulcata (Pennant, 1777) are separate species.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PIR; A01796; TZAZ1.
DR   PDB; 1ATX; NMR; -; A=1-46.
DR   PDBsum; 1ATX; -.
DR   AlphaFoldDB; P01533; -.
DR   BMRB; P01533; -.
DR   SMR; P01533; -.
DR   EvolutionaryTrace; P01533; -.
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   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Nematocyst; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..46
FT                   /note="Delta-actitoxin-Avd1a"
FT                   /evidence="ECO:0000269|PubMed:29753"
FT                   /id="PRO_0000221512"
FT   DISULFID        4..43
FT                   /evidence="ECO:0000269|PubMed:2892680"
FT   DISULFID        6..34
FT                   /evidence="ECO:0000269|PubMed:2892680"
FT   DISULFID        27..44
FT                   /evidence="ECO:0000269|PubMed:2892680"
FT   VARIANT         3
FT                   /note="A -> P (in about 20% of the molecules)"
FT   STRAND          3..5
FT                   /evidence="ECO:0007829|PDB:1ATX"
FT   STRAND          16..25
FT                   /evidence="ECO:0007829|PDB:1ATX"
FT   STRAND          32..34
FT                   /evidence="ECO:0007829|PDB:1ATX"
FT   STRAND          37..45
FT                   /evidence="ECO:0007829|PDB:1ATX"
SQ   SEQUENCE   46 AA;  4814 MW;  862C1E21FDA5432D CRC64;
     GAACLCKSDG PNTRGNSMSG TIWVFGCPSG WNNCEGRAII GYCCKQ