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K1BAA_ANEVI
ID   K1BAA_ANEVI             Reviewed;          86 AA.
AC   P0DN04;
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-Avd10a {ECO:0000303|PubMed:22683676};
DE            Short=U-AITX-Avd10a {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Potassium channel toxin avtx-10 {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; FK743341; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DN04; -.
DR   SMR; P0DN04; -.
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..42
FT                   /evidence="ECO:0000305|PubMed:21281459"
FT                   /id="PRO_0000433747"
FT   CHAIN           45..86
FT                   /note="U-actitoxin-Avd10a"
FT                   /evidence="ECO:0000305|PubMed:21281459"
FT                   /id="PRO_0000433748"
FT   DOMAIN          51..86
FT                   /note="ShKT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        51..86
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        60..79
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        69..83
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ   SEQUENCE   86 AA;  9273 MW;  625CF4AEF6F3117E CRC64;
     MSRIAILLFV AFLLVAGISA KSTAHFKKNV LADLFKERRF NAKRDPAGST CVNIDVDSFC
     DGMAERGACN IIPQMATNCA KACNSC
 
 
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