ID   NA1_CONGI               Reviewed;          47 AA.
AC   P0C280; P0DMX1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Delta-actitoxin-Cgg1a {ECO:0000303|PubMed:22683676};
DE            Short=Delta-AITX-Cgg1a {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Toxin CgNa {ECO:0000303|PubMed:16814340};
DE   AltName: Full=Toxin Cp-2 {ECO:0000305};
DE            Short=CpII {ECO:0000305};
DE            Short=Toxin Cp II {ECO:0000303|Ref.1};
OS   Condylactis gigantea (Giant Caribbean anemone) (Condylactis passiflora).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Condylactis.
OX   NCBI_TaxID=47073;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND HYDROXYLATION AT PRO-3.
RA   Shiomi K., Lin X.Y., Nagashima Y., Ishida M.;
RT   "Isolation and amino acid sequences of polypeptide toxins in the Caribbean
RT   sea anemone Condylactis passiflora.";
RL   Fish. Sci. 61:1016-1021(1995).
RN   [2]
RP   PROTEIN SEQUENCE, FUNCTION, TOXIC DOSE, MASS SPECTROMETRY, AND
RP   HYDROXYLATION AT PRO-3.
RX   PubMed=16814340; DOI=10.1016/j.toxicon.2006.05.001;
RA   Standker L., Beress L., Garateix A., Christ T., Ravens U., Salceda E.,
RA   Soto E., John H., Forssmann W.-G., Aneiros A.;
RT   "A new toxin from the sea anemone Condylactis gigantea with effect on
RT   sodium channel inactivation.";
RL   Toxicon 48:211-220(2006).
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   TOXIC DOSE.
RX   PubMed=29109403; DOI=10.1038/s41598-017-14961-1;
RA   Babenko V.V., Mikov A.N., Manuvera V.A., Anikanov N.A., Kovalchuk S.I.,
RA   Andreev Y.A., Logashina Y.A., Kornilov D.A., Manolov A.I., Sanamyan N.P.,
RA   Sanamyan K.E., Kostryukova E.S., Kozlov S.A., Grishin E.V., Govorun V.M.,
RA   Lazarev V.N.;
RT   "Identification of unusual peptides with new Cys frameworks in the venom of
RT   the cold-water sea anemone Cnidopus japonicus.";
RL   Sci. Rep. 7:14534-14534(2017).
RN   [5]
RP   STRUCTURE BY NMR, DISULFIDE BONDS, AND HYDROXYLATION AT PRO-3.
RX   PubMed=17506725; DOI=10.1042/bj20070130;
RA   Salceda E., Perez-Castells J., Lopez-Mendez B., Garateix A., Salazar H.,
RA   Lopez O., Aneiros A., Standker L., Beress L., Forssmann W.-G., Soto E.,
RA   Jimenez-Barbero J., Gimenez-Gallego G.;
RT   "CgNa, a type I toxin from the giant Caribbean sea anemone Condylactis
RT   gigantea shows structural similarities to both type I and II toxins, as
RT   well as distinctive structural and functional properties.";
RL   Biochem. J. 406:67-76(2007).
CC   -!- FUNCTION: Slows down the inactivation process of TTX-sensitive voltage-
CC       gated sodium channels (Nav) (PubMed:16814340). Has a strong crab-
CC       paralyzing activity (PubMed:16814340). The minimum lethal dose against
CC       crabs is 7.9 mg/kg (Ref.1). {ECO:0000269|PubMed:16814340,
CC       ECO:0000269|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=5043; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16814340};
CC   -!- TOXIC DOSE: LD(50) is 1 ug/kg by injection at the junction between the
CC       body and the walking leg of crabs. {ECO:0000269|PubMed:16814340}.
CC   -!- TOXIC DOSE: LD(100) is 5 ug/g when injected into fly larvae
CC       (M.domestica). {ECO:0000269|PubMed:29109403}.
CC   -!- SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin
CC       family. Type I subfamily. {ECO:0000305}.
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DR   PDB; 2H9X; NMR; -; A=1-47.
DR   PDBsum; 2H9X; -.
DR   AlphaFoldDB; P0C280; -.
DR   BMRB; P0C280; -.
DR   SMR; P0C280; -.
DR   EvolutionaryTrace; P0C280; -.
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   3D-structure; Direct protein sequencing; Disulfide bond; Hydroxylation;
KW   Ion channel impairing toxin; Nematocyst; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   PEPTIDE         1..47
FT                   /note="Delta-actitoxin-Cgg1a"
FT                   /evidence="ECO:0000269|PubMed:16814340, ECO:0000269|Ref.1"
FT                   /id="PRO_0000269544"
FT   MOD_RES         3
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:16814340,
FT                   ECO:0000269|PubMed:17506725, ECO:0000269|Ref.1"
FT   DISULFID        4..44
FT                   /evidence="ECO:0000269|PubMed:17506725,
FT                   ECO:0000312|PDB:2H9X"
FT   DISULFID        6..34
FT                   /evidence="ECO:0000269|PubMed:17506725,
FT                   ECO:0000312|PDB:2H9X"
FT   DISULFID        27..45
FT                   /evidence="ECO:0000269|PubMed:17506725,
FT                   ECO:0000312|PDB:2H9X"
FT   STRAND          20..26
FT                   /evidence="ECO:0007829|PDB:2H9X"
FT   STRAND          34..36
FT                   /evidence="ECO:0007829|PDB:2H9X"
FT   STRAND          40..46
FT                   /evidence="ECO:0007829|PDB:2H9X"
SQ   SEQUENCE   47 AA;  5037 MW;  B0800D52466F2E00 CRC64;
     GVPCRCDSDG PSVHGNTLSG TVWVGSCASG WHKCNDEYNI AYECCKE