K1B9C_ANEVI
ID K1B9C_ANEVI Reviewed; 80 AA.
AC P0DN02;
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=U-actitoxin-Avd9c {ECO:0000303|PubMed:22683676};
DE Short=U-AITX-Avd9c {ECO:0000303|PubMed:22683676};
DE AltName: Full=Potassium channel toxin avtx-8 {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).
CC -!- FUNCTION: Inhibits voltage-gated potassium channels (Kv1/KCNA).
CC {ECO:0000250|UniProtKB:P29186}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sea anemone type 1 potassium channel toxin
CC family. Type 1b subfamily.
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; FK755121; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; FK749797; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0DN02; -.
DR SMR; P0DN02; -.
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.
DR InterPro; IPR003582; ShKT_dom.
DR Pfam; PF01549; ShK; 1.
DR PROSITE; PS51670; SHKT; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Ion channel impairing toxin; Nematocyst; Neurotoxin;
KW Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW Voltage-gated potassium channel impairing toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..38
FT /evidence="ECO:0000305|PubMed:21281459"
FT /id="PRO_0000433743"
FT CHAIN 42..80
FT /note="U-actitoxin-Avd9c"
FT /id="PRO_0000433744"
FT DOMAIN 45..80
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT REGION 68..69
FT /note="Crucial for binding to potassium channels"
FT /evidence="ECO:0000250|UniProtKB:P29186"
FT DISULFID 45..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 54..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 63..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT CONFLICT 19
FT /note="M -> T (in Ref. 1; FK755121)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="G -> R (in Ref. 1; FK755121)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 80 AA; 8929 MW; D61D09141B59282D CRC64;
MSPKVLAVFV LCAILVVVMA GRTGTETGGN KKDTLQDLKK RTRNCFDRFE KGTCKMAKRN
GACEWSDKYE MNCKKTCGLC
