ID   BDS2_ANESU              Reviewed;          43 AA.
AC   P59084;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2002, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=DeltaKappa-actitoxin-Avd4b {ECO:0000303|PubMed:22683676};
DE            Short=DeltaKappa-AITX-Avd4b {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Antihypertensive protein BDS-2;
DE   AltName: Full=Blood depressing substance II {ECO:0000303|PubMed:9506974};
DE            Short=BDS-II {ECO:0000303|PubMed:9506974};
OS   Anemonia sulcata (Mediterranean snakelocks sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Anemonia.
OX   NCBI_TaxID=6108;
RN   [1]
RP   PROTEIN SEQUENCE, AND FUNCTION.
RA   Beress L., Doppelfeld I.-S., Etschenberg E., Graf E., Henschen-Edman A.,
RA   Zwick J.;
RT   "Polypeptides, process for their preparation, and their use as hypotensive
RT   active compounds.";
RL   Patent number DE3324689, 17-JAN-1985.
RN   [2]
RP   PROTEIN SEQUENCE, AND FUNCTION.
RX   PubMed=9506974; DOI=10.1074/jbc.273.12.6744;
RA   Diochot S., Schweitz H., Beress L., Lazdunski M.;
RT   "Sea anemone peptides with a specific blocking activity against the fast
RT   inactivating potassium channel Kv3.4.";
RL   J. Biol. Chem. 273:6744-6749(1998).
RN   [3]
RP   FUNCTION.
RX   PubMed=16177043; DOI=10.1523/jneurosci.2119-05.2005;
RA   Yeung S.Y., Thompson D., Wang Z., Fedida D., Robertson B.;
RT   "Modulation of Kv3 subfamily potassium currents by the sea anemone toxin
RT   BDS: significance for CNS and biophysical studies.";
RL   J. Neurosci. 25:8735-8745(2005).
RN   [4]
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: Acts as a gating modifier on both Kv and Nav ion channels.
CC       Voltage-dependently inhibits voltage-gated potassium channels Kv3
CC       (Kv3.1/KCNC1, Kv3.2/KCNC2 and Kv3.4/KCNC4) (PubMed:9506974,
CC       PubMed:16177043). Slows inactivation of the voltage-gated sodium
CC       channel Nav1.7/SCN9A (By similarity). Inhibits all Kv3.1, Kv3.2 and
CC       Kv3.4 by about 50% when tested at a voltage of +40 mV
CC       (PubMed:16177043). May act by binding residues in voltage-sensing
CC       domains S3b and S4 of Kv3 (PubMed:16177043). Tests have been done on
CC       human Nav1.7/SCN9A and rat SCG neurons that mostly carry Nav1.7
CC       channels (EC(50)=300 nM) (By similarity). This toxin also reduces blood
CC       pressure (Ref.1). {ECO:0000250|UniProtKB:P11494,
CC       ECO:0000269|PubMed:16177043, ECO:0000269|PubMed:9506974,
CC       ECO:0000269|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {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   AlphaFoldDB; P59084; -.
DR   SMR; P59084; -.
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   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   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Nematocyst; Neurotoxin; Potassium channel impairing toxin; Secreted; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   CHAIN           1..43
FT                   /note="DeltaKappa-actitoxin-Avd4b"
FT                   /evidence="ECO:0000269|PubMed:9506974, ECO:0000269|Ref.1"
FT                   /id="PRO_0000221542"
FT   DISULFID        4..39
FT                   /evidence="ECO:0000250|UniProtKB:P11494"
FT   DISULFID        6..32
FT                   /evidence="ECO:0000250|UniProtKB:P11494"
FT   DISULFID        22..40
FT                   /evidence="ECO:0000250|UniProtKB:P11494"
SQ   SEQUENCE   43 AA;  4782 MW;  7EEAABBE8A1FDE08 CRC64;
     AAPCFCPGKP DRGDLWILRG TCPGGYGYTS NCYKWPNICC YPH