ID   BDSE_ANEVI              Reviewed;          76 AA.
AC   P0DMY8;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Kappa-actitoxin-Avd4n {ECO:0000303|PubMed:22683676};
DE            Short=Kappa-AITX-Avd4n {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Antihypertensive protein BDS-14;
DE   AltName: Full=Blood depressing substance 14 {ECO:0000303|PubMed:21281459};
DE            Short=BDS-14 {ECO:0000303|PubMed:21281459};
DE   Flags: Precursor;
OS   Anemonia viridis (Snakelocks anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Anemonia.
OX   NCBI_TaxID=51769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=19627569; DOI=10.1186/1471-2164-10-333;
RA   Sabourault C., Ganot P., Deleury E., Allemand D., Furla P.;
RT   "Comprehensive EST analysis of the symbiotic sea anemone, Anemonia
RT   viridis.";
RL   BMC Genomics 10:333-333(2009).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=21281459; DOI=10.1186/1471-2164-12-88;
RA   Kozlov S., Grishin E.;
RT   "The mining of toxin-like polypeptides from EST database by single residue
RT   distribution analysis.";
RL   BMC Genomics 12:88-88(2011).
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   3D-STRUCTURE MODELING, AND TISSUE SPECIFICITY.
RX   PubMed=24177670; DOI=10.3390/md11114213;
RA   Nicosia A., Maggio T., Mazzola S., Cuttitta A.;
RT   "Evidence of accelerated evolution and ectodermal-specific expression of
RT   presumptive BDS toxin cDNAs from Anemonia viridis.";
RL   Mar. Drugs 11:4213-4231(2013).
CC   -!- FUNCTION: Blocks Kv3 voltage-gated potassium channels. Reduces blood
CC       pressure. {ECO:0000250|UniProtKB:P11494}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Experimental results show no expression in the
CC       ectodermal tissue from the distal and proximal tentacles, body wall,
CC       and oral disk. Since paralogs are expressed in this tissue, an
CC       expression of this toxin in this tissue is probable. The negative
CC       results could be explained by the very low abundance of EST sequences.
CC       {ECO:0000305|PubMed:24177670}.
CC   -!- PTM: Lacks the conventional Cys residue at position 55. Thus, only 2
CC       disulfide are possible present. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the sea anemone type 3 (BDS) potassium channel
CC       toxin family. {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}.
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DR   EMBL; FK745823; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DMY8; -.
DR   SMR; P0DMY8; -.
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:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0008217; P:regulation of blood pressure; 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   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Disulfide bond; Hypotensive agent;
KW   Ion channel impairing toxin; Nematocyst; Neurotoxin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..31
FT                   /evidence="ECO:0000250|UniProtKB:P11494"
FT                   /id="PRO_0000433672"
FT   CHAIN           34..76
FT                   /note="Kappa-actitoxin-Avd4n"
FT                   /id="PRO_0000433673"
FT   DISULFID        37..72
FT                   /evidence="ECO:0000250|UniProtKB:P11494"
FT   DISULFID        39..65
FT                   /evidence="ECO:0000250|UniProtKB:P11494"
SQ   SEQUENCE   76 AA;  8273 MW;  7E14BF7F5A9D2722 CRC64;
     MNKAFFLCLV VLCAAVVFAA EDLQKGKHAP FKRAAPCFCS GNPGRGDLWI LRGPSPGGYG
     YTSNCYKWPN ICCFPP