ID   K1B9A_ANEVI             Reviewed;          80 AA.
AC   P0DN00;
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-Avd9a {ECO:0000303|PubMed:22683676};
DE            Short=U-AITX-Avd9a {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Potassium channel toxin avtx-6 {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; FK724096; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FK738108; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DN00; -.
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..39
FT                   /evidence="ECO:0000305|PubMed:21281459"
FT                   /id="PRO_0000433730"
FT   CHAIN           42..80
FT                   /note="U-actitoxin-Avd9a"
FT                   /id="PRO_0000433731"
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="T -> M (in Ref. 1; FK738108)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   80 AA;  8990 MW;  45287395676E1079 CRC64;
     MNLKVLAVFV LCAILVVVTA ERRGTETGVY KKDTLQDLIK RTRNCIDRFP TGTCKQVKKG
     GSCKNSDKYR MNCRKTCGLC