ID   TX9AN_BUNCN             Reviewed;          28 AA.
AC   P86467;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=Toxin Bcg III 23.41 {ECO:0000303|PubMed:20483220};
DE            Short=Bcg 23.41 {ECO:0000303|PubMed:20483220};
DE   AltName: Full=AnmTX BC 9a-1 {ECO:0000303|PubMed:23801332};
DE   Flags: Fragment;
OS   Bunodosoma cangicum (Sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Bunodosoma.
OX   NCBI_TaxID=138296;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RX   PubMed=20483220; DOI=10.1016/j.cbd.2008.04.002;
RA   Zaharenko A.J., Ferreira W.A. Jr., Oliveira J.S., Richardson M.,
RA   Pimenta D.C., Konno K., Portaro F.C., de Freitas J.C.;
RT   "Proteomics of the neurotoxic fraction from the sea anemone Bunodosoma
RT   cangicum venom: novel peptides belonging to new classes of toxins.";
RL   Comp. Biochem. Physiol. 3D:219-225(2008).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=23801332; DOI=10.1074/jbc.m113.485516;
RA   Osmakov D.I., Kozlov S.A., Andreev Y.A., Koshelev S.G., Sanamyan N.P.,
RA   Sanamyan K.E., Dyachenko I.A., Bondarenko D.A., Murashev A.N., Mineev K.S.,
RA   Arseniev A.S., Grishin E.V.;
RT   "Sea anemone peptide with uncommon beta-hairpin structure inhibits acid-
RT   sensing ion channel 3 (ASIC3) and reveals analgesic activity.";
RL   J. Biol. Chem. 288:23116-23127(2013).
CC   -!- FUNCTION: Possible voltage-gated potassium channel (Kv) blocker.
CC       Increases amplitude and duration of crab leg nerve compound action
CC       potential. {ECO:0000269|PubMed:20483220}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=3176.36; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20483220};
CC   -!- SIMILARITY: Belongs to the sea anemone structural class 9a family.
CC       {ECO:0000305|PubMed:23801332}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P86467; -.
DR   SMR; P86467; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Nematocyst; Potassium channel impairing toxin; Secreted; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   CHAIN           1..>28
FT                   /note="Toxin Bcg III 23.41"
FT                   /id="PRO_0000392955"
FT   DISULFID        7..19
FT                   /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT   DISULFID        10..26
FT                   /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT   NON_TER         28
FT                   /evidence="ECO:0000303|PubMed:20483220"
SQ   SEQUENCE   28 AA;  3082 MW;  1ED49F3404A86B3C CRC64;
     NIIDVPCRPC YYRDSSGNCV YDQLGCGA