ID   BDS2A_ANTMC             Reviewed;          80 AA.
AC   P69930; Q5R214;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Delta-actitoxin-Amc2a {ECO:0000303|PubMed:22683676};
DE            Short=Delta-AITX-Amc2a {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Peptide toxin Am II {ECO:0000303|PubMed:15581681};
DE   AltName: Full=Peptide toxin Am-2 {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-56, 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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=5238.1; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15581681};
CC   -!- TOXIC DOSE: PD(50) is 420 ug/kg into crabs.
CC       {ECO:0000269|PubMed:15581681}.
CC   -!- SIMILARITY: Belongs to the sea anemone type 3 (BDS) potassium channel
CC       toxin family. {ECO:0000305}.
CC   -!- CAUTION: There is no mention of the activity in PubMed:15581681. The
CC       Greek letter 'delta' in the name delta-AITX-Amc2a (which indicates an
CC       inhibition of sodium channels) has been deduced from the toxin
CC       paralytic activity to crabs. {ECO:0000305|PubMed:22683676}.
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DR   EMBL; AB180686; BAD74022.1; -; mRNA.
DR   AlphaFoldDB; P69930; -.
DR   SMR; P69930; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.20.20.10; -; 1.
DR   InterPro; IPR012414; BDS_K_chnl_tox.
DR   InterPro; IPR023355; Myo_ane_neurotoxin_sf.
DR   Pfam; PF07936; Defensin_4; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Disulfide bond; Hydroxylation;
KW   Nematocyst; Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..30
FT                   /evidence="ECO:0000269|PubMed:15581681"
FT                   /id="PRO_0000034861"
FT   CHAIN           33..78
FT                   /note="Delta-actitoxin-Amc2a"
FT                   /evidence="ECO:0000269|PubMed:15581681"
FT                   /id="PRO_0000034862"
FT   MOD_RES         56
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:15581681"
FT   DISULFID        37..73
FT                   /evidence="ECO:0000250|UniProtKB:P11494"
FT   DISULFID        39..65
FT                   /evidence="ECO:0000250|UniProtKB:P11494"
FT   DISULFID        55..74
FT                   /evidence="ECO:0000250|UniProtKB:P11494"
SQ   SEQUENCE   80 AA;  9028 MW;  78AC8B7FBA736865 CRC64;
     MNKVLFLCLV VLCATSAFAA EEEYVERAPV KRALLSCRCE GKTEYGDKWL FHGGCPNNYG
     YNYKCFMKPG AVCCYPQNGR