BDS1_ANEVI
ID BDS1_ANEVI Reviewed; 76 AA.
AC P0DMX6;
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-Avd4a {ECO:0000303|PubMed:22683676};
DE Short=Kappa-AITX-Avd4a {ECO:0000303|PubMed:22683676};
DE AltName: Full=Antihypertensive protein BDS-1 {ECO:0000305};
DE AltName: Full=Blood depressing substance 1 {ECO:0000303|PubMed:21281459};
DE Short=BDS-1 {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 PROTEIN SEQUENCE OF 34-76, AND MASS SPECTROMETRY.
RX PubMed=29671760; DOI=10.3390/md16040134;
RA Loret E.P., Luis J., Nuccio C., Villard C., Mansuelle P., Lebrun R.,
RA Villard P.H.;
RT "A low molecular weight protein from the sea anemone anemonia viridis with
RT an anti-angiogenic activity.";
RL Mar. Drugs 16:0-0(2018).
RN [3]
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 [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).
RN [5]
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: Acts as a gating modifier on both Kv and Nav ion channels,
CC and also acts on blood pressure (By similarity). Voltage-dependently
CC inhibits voltage-gated potassium channels Kv3 (Kv3.1/KCNC1, Kv3.2/KCNC2
CC and Kv3.4/KCNC4) and 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 (45%, 48% and
CC 56%, respectively) (By similarity). May act by binding residues in
CC voltage-sensing domains S3b and S4 of Kv3 (By similarity). On sodium
CC channels, tests have been done on human Nav1.7/SCN9A (expressed in
CC HEK293 cells) (EC(50)=3 nM) and rat SCG neurons that mostly carry
CC Nav1.7 channels (EC(50)=300 nM) (By similarity). This toxin also
CC reduces blood pressure (By similarity). {ECO:0000250|UniProtKB:P11494}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the ectodermal tissue from the
CC distal and proximal tentacles, body wall, and oral disk.
CC {ECO:0000269|PubMed:24177670}.
CC -!- MASS SPECTROMETRY: Mass=4708; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:29671760};
CC -!- MISCELLANEOUS: Is the most represented component of the BDS family in
CC A.viridis. {ECO:0000305|PubMed:21281459}.
CC -!- MISCELLANEOUS: This protein sequence is identical to BDS-1 from
CC A.sulcata (AC P11494). {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; FK728690; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; FK727245; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; FK731753; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; FK734674; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; FK756071; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; FK756154; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; FK737141; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; FK733420; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; FK754388; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; FK721790; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; FK755366; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; FK745427; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; FK727043; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; FK752129; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0DMX6; -.
DR SMR; P0DMX6; -.
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 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Hypotensive agent; Ion channel impairing toxin; Nematocyst;
KW Neurotoxin; 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:0000305|PubMed:29671760"
FT /id="PRO_0000433648"
FT CHAIN 34..76
FT /note="Kappa-actitoxin-Avd4a"
FT /evidence="ECO:0000269|PubMed:29671760"
FT /id="PRO_0000433649"
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; 8343 MW; 5636A6D45399B741 CRC64;
MNKALFLCLV VLCAAVVFAA EDLQKAKHAP FKRAAPCFCS GKPGRGDLWI LRGTCPGGYG
YTSNCYKWPN ICCYPH
