BDS2C_ANTEL
ID BDS2C_ANTEL Reviewed; 70 AA.
AC P0DMX5;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 1.
DT 25-MAY-2022, entry version 10.
DE RecName: Full=U-actitoxin-Ael2c {ECO:0000303|PubMed:22683676};
DE Short=U-AITX-Ael2c {ECO:0000303|PubMed:22683676};
DE AltName: Full=U-AITX-Ael1a {ECO:0000303|PubMed:22015268};
DE Flags: Precursor; Fragment;
OS Anthopleura elegantissima (Green aggregating anemone) (Actinia
OS elegantissima).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Anthopleura.
OX NCBI_TaxID=6110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=20494848; DOI=10.1016/j.cbd.2008.08.001;
RA Richier S., Rodriguez-Lanetty M., Schnitzler C.E., Weis V.M.;
RT "Response of the symbiotic cnidarian Anthopleura elegantissima
RT transcriptome to temperature and UV increase.";
RL Comp. Biochem. Physiol. 3D:283-289(2008).
RN [2]
RP NOMENCLATURE.
RX PubMed=22015268; DOI=10.1016/j.peptides.2011.10.011;
RA Rodriguez A.A., Cassoli J.S., Sa F., Dong Z.Q., de Freitas J.C.,
RA Pimenta A.M., de Lima M.E., Konno K., Lee S.M., Garateix A.,
RA Zaharenko A.J.;
RT "Peptide fingerprinting of the neurotoxic fractions isolated from the
RT secretions of sea anemones Stichodactyla helianthus and Bunodosoma
RT granulifera. New members of the APETx-like family identified by a 454
RT pyrosequencing approach.";
RL Peptides 34:26-38(2012).
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).
CC -!- FUNCTION: Potently and selectively inhibits voltage-gated potassium
CC channels Kv11/KCNH/ERG. Acts as a gating-modifier toxin that shifts the
CC voltage-dependence of ERG activation in the positive direction and
CC suppresses its current amplitudes elicited by strong depolarizing
CC pulses that maximally activate the channels.
CC {ECO:0000250|UniProtKB:P61541}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC -!- MISCELLANEOUS: Shows significant expression differences between
CC stressed and unstressed A.elegantissima. {ECO:0000269|PubMed:20494848}.
CC -!- SIMILARITY: Belongs to the sea anemone type 3 (BDS) potassium channel
CC toxin family. {ECO:0000305}.
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DR EMBL; FG392547; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0DMX5; -.
DR SMR; P0DMX5; -.
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 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Disulfide bond;
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..21
FT /evidence="ECO:0000305"
FT PROPEP 22..26
FT /evidence="ECO:0000305"
FT /id="PRO_0000433584"
FT CHAIN 29..70
FT /note="U-actitoxin-Ael2c"
FT /id="PRO_0000433585"
FT DISULFID 32..65
FT /evidence="ECO:0000250|UniProtKB:P61541"
FT DISULFID 34..58
FT /evidence="ECO:0000250|UniProtKB:P61541"
FT DISULFID 48..66
FT /evidence="ECO:0000250|UniProtKB:P61541"
FT NON_TER 1
SQ SEQUENCE 70 AA; 7689 MW; E728A513BA3B6F02 CRC64;
SYQRFLFLVV VASLIATSLA IPKDLEKRGT TCYCGNTIGI YWFAKKTCPS GRGYTGSCGY
FLGICCYPVD
