NA13_ANTMC
ID NA13_ANTMC Reviewed; 74 AA.
AC P69928; Q5R213;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Delta-actitoxin-Amc3a {ECO:0000303|PubMed:22683676};
DE Short=Delta-AITX-Amc3a {ECO:0000303|PubMed:22683676};
DE AltName: Full=Peptide toxin Am III {ECO:0000303|PubMed:15581681};
DE AltName: Full=Peptide toxin Am-3 {ECO:0000305};
DE Flags: Precursor;
OS Antheopsis maculata (Sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Antheopsis.
OX NCBI_TaxID=280228;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], MASS SPECTROMETRY, HYDROXYLATION AT PRO-29, AND
RP TOXIC DOSE.
RX PubMed=15581681; DOI=10.1016/j.toxicon.2004.09.013;
RA Honma T., Hasegawa Y., Ishida M., Nagai H., Nagashima Y., Shiomi K.;
RT "Isolation and molecular cloning of novel peptide toxins from the sea
RT anemone Antheopsis maculata.";
RL Toxicon 45:33-41(2005).
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: Inhibits voltage-gated sodium channels (Nav).
CC {ECO:0000250|UniProtKB:P0C280}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=5147.6; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15581681};
CC -!- TOXIC DOSE: LD(50) is 70 ug/kg into crabs.
CC {ECO:0000269|PubMed:15581681}.
CC -!- SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin
CC family. Type I subfamily. {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 EMBL; AB180687; BAD74023.1; -; mRNA.
DR AlphaFoldDB; P69928; -.
DR SMR; P69928; -.
DR TCDB; 8.B.17.1.2; the sea anemone peptide toxin class iii (shi) family.
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 Amidation; Cleavage on pair of basic residues; Disulfide bond;
KW Hydroxylation; 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..24
FT /evidence="ECO:0000269|PubMed:15581681"
FT /id="PRO_0000034823"
FT PEPTIDE 27..73
FT /note="Delta-actitoxin-Amc3a"
FT /evidence="ECO:0000269|PubMed:15581681"
FT /id="PRO_0000034824"
FT MOD_RES 29
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:15581681"
FT MOD_RES 73
FT /note="Glutamine amide"
FT /evidence="ECO:0000255"
FT DISULFID 30..70
FT /evidence="ECO:0000250|UniProtKB:P0C280"
FT DISULFID 32..60
FT /evidence="ECO:0000250|UniProtKB:P0C280"
FT DISULFID 53..71
FT /evidence="ECO:0000250|UniProtKB:P0C280"
SQ SEQUENCE 74 AA; 8038 MW; 83DDDC375CD909F6 CRC64;
MNRLIILVVA AVFLGMASAE EDVLKRGFPC RCDSDGPSVH GNPLSGTIWV TSCATGWHKC
NSENELFHEC CKQG
