ID   BDS7_ANEVI              Reviewed;          76 AA.
AC   P0DMY1;
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-Avd4g {ECO:0000303|PubMed:22683676};
DE            Short=Kappa-AITX-Avd4g {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Antihypertensive protein BDS-7;
DE   AltName: Full=Blood depressing substance 7 {ECO:0000303|PubMed:21281459};
DE            Short=BDS-7 {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: Moderately expressed in the ectodermal tissue from
CC       the distal and proximal tentacles, body wall, and oral disk.
CC       {ECO:0000269|PubMed:24177670}.
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; FK736435; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FK729210; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FK729786; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DMY1; -.
DR   SMR; P0DMY1; -.
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_0000433658"
FT   CHAIN           34..76
FT                   /note="Kappa-actitoxin-Avd4g"
FT                   /id="PRO_0000433659"
FT   DISULFID        37..72
FT                   /evidence="ECO:0000250|UniProtKB:P11494"
FT   DISULFID        39..65
FT                   /evidence="ECO:0000250|UniProtKB:P11494"
FT   DISULFID        55..73
FT                   /evidence="ECO:0000250|UniProtKB:P11494"
SQ   SEQUENCE   76 AA;  8357 MW;  5636A6D45399AAF6 CRC64;
     MNKALFLCLV VLCAAVVFAA EDLQKAKHAP FKRAAPCFCS GKPGRGDLWI LRGDCPGGYG
     YTSNCYKWPN ICCYPH