NA11_ACTEQ
ID NA11_ACTEQ Reviewed; 82 AA.
AC Q9NJQ2; B1NWU1; Q9TXD2;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Delta-actitoxin-Aeq2a {ECO:0000303|PubMed:22683676};
DE Short=Delta-AITX-Aeq2a {ECO:0000303|PubMed:22683676};
DE AltName: Full=Ae1 {ECO:0000303|PubMed:18222944};
DE AltName: Full=Ae1-1 {ECO:0000303|PubMed:18222944};
DE AltName: Full=AeNa {ECO:0000303|PubMed:10669802};
DE AltName: Full=Neurotoxin 1 {ECO:0000312|EMBL:ABW97357.1};
DE AltName: Full=Neurotoxin Ae I {ECO:0000303|PubMed:8835334};
DE Flags: Precursor;
OS Actinia equina (Beadlet anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Actinia.
OX NCBI_TaxID=6106;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10669802; DOI=10.1016/s0167-4838(99)00237-x;
RA Anderluh G., Podlesek Z., Macek P.;
RT "A common motif in proparts of Cnidarian toxins and nematocyst collagens
RT and its putative role.";
RL Biochim. Biophys. Acta 1476:372-376(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=18222944; DOI=10.1093/molbev/msn021;
RA Moran Y., Weinberger H., Sullivan J.C., Reitzel A.M., Finnerty J.R.,
RA Gurevitz M.;
RT "Concerted evolution of sea anemone neurotoxin genes is revealed through
RT analysis of the Nematostella vectensis genome.";
RL Mol. Biol. Evol. 25:737-747(2008).
RN [3]
RP PROTEIN SEQUENCE OF 29-82, AND FUNCTION.
RX PubMed=8835334; DOI=10.1016/0041-0101(95)00121-2;
RA Lin X.-Y., Ishida M., Nagashima Y., Shiomi K.;
RT "A polypeptide toxin in the sea anemone Actinia equina homologous with
RT other sea anemone sodium channel toxins: isolation and amino acid
RT sequence.";
RL Toxicon 34:57-65(1996).
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 (By
CC similarity). Causes death to crabs (minimum lethal dose of 25 ug/kg)
CC and mice (PubMed:8835334). {ECO:0000250, ECO:0000269|PubMed:8835334}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin
CC family. Type I subfamily. {ECO:0000305}.
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DR EMBL; AF130344; AAF27538.1; -; mRNA.
DR EMBL; EU124478; ABW97357.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9NJQ2; -.
DR SMR; Q9NJQ2; -.
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 Gene3D; 2.20.20.10; -; 1.
DR InterPro; IPR023355; Myo_ane_neurotoxin_sf.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin; Nematocyst; Neurotoxin;
KW Secreted; Signal; Toxin; Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..26
FT /evidence="ECO:0000269|PubMed:8835334"
FT /id="PRO_0000034821"
FT CHAIN 29..82
FT /note="Delta-actitoxin-Aeq2a"
FT /evidence="ECO:0000269|PubMed:8835334"
FT /id="PRO_0000034822"
FT DISULFID 32..79
FT /evidence="ECO:0000250|UniProtKB:P01530"
FT DISULFID 34..69
FT /evidence="ECO:0000250|UniProtKB:P01530"
FT DISULFID 62..80
FT /evidence="ECO:0000250|UniProtKB:P01530"
SQ SEQUENCE 82 AA; 8696 MW; D255A329AB86DF3D CRC64;
MNRLMILVFA AVFLALASAD EDVDIAKRGI PCLCVSDGPS TRGNKLSGTI WMKTGGYGGN
GCPKGWHFCG KSRGLLSDCC KQ
