K1A_THAAS
ID K1A_THAAS Reviewed; 75 AA.
AC E2S066;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=Kappa-thalatoxin-Tas2a {ECO:0000305};
DE Short=Kappa-TATX-Tas2a {ECO:0000305};
DE AltName: Full=Kappa1.3-thalatoxin-Ta1a {ECO:0000303|PubMed:21339955};
DE Short=Kappa1.3-TATX-Ta1a {ECO:0000305|PubMed:21339955};
DE Short=Kappa1.3-TLTX-Ta1a {ECO:0000303|PubMed:21339955};
DE AltName: Full=Potassium channel peptide toxin ta-k {ECO:0000312|EMBL:BAJ23163.1};
DE Short=TaK {ECO:0000305};
DE Flags: Precursor;
OS Thalassianthus aster (Fuzzy-tipped anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Nynantheae; Thalassianthidae; Thalassianthus.
OX NCBI_TaxID=659516;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=21339955; DOI=10.3390/md8122893;
RA Yamaguchi Y., Hasegawa Y., Honma T., Nagashima Y., Shiomi K.;
RT "Screening and cDNA cloning of Kv1 potassium channel toxins in sea
RT anemones.";
RL Mar. Drugs 8:2893-2905(2010).
RN [2]
RP FUNCTION, AND RECOMBINANT EXPRESSION.
RX PubMed=30648553; DOI=10.1016/j.bbrc.2019.01.014;
RA Liu Y., Zhang J., Wang R., Wu Y., Wang W., Xin X., Du M., Cao Y., Zhang H.;
RT "Identification of novel Kv1.3 targeting venom peptides by a single round
RT of autocrine-based selection.";
RL Biochem. Biophys. Res. Commun. 509:954-959(2019).
CC -!- FUNCTION: Inhibits voltage-gated potassium channels (Kv) with higher
CC potency for Kv1.1/KCNA1 and Kv1.3/KCNA3 (IC(50)=3.4 nM).
CC {ECO:0000250|UniProtKB:P29187, ECO:0000269|PubMed:30648553}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC -!- MISCELLANEOUS: This protein is also called kappa-TLTX-Hh1a
CC (PubMed:21339955). The TATX abbreviation is given to this protein,
CC since the abbreviation TLTX was already given to a spider family.
CC {ECO:0000305|PubMed:21339955}.
CC -!- SIMILARITY: Belongs to the sea anemone type 1 potassium channel toxin
CC family. Type 1a subfamily. {ECO:0000305}.
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DR EMBL; AB595209; BAJ23163.1; -; mRNA.
DR AlphaFoldDB; E2S066; -.
DR SMR; E2S066; -.
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 PROSITE; PS51670; SHKT; 1.
PE 3: Inferred from homology;
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..22
FT /evidence="ECO:0000255"
FT PROPEP 23..40
FT /evidence="ECO:0000250"
FT /id="PRO_0000425844"
FT PEPTIDE 41..75
FT /note="Kappa-thalatoxin-Tas2a"
FT /evidence="ECO:0000250|UniProtKB:P29187"
FT /id="PRO_0000425843"
FT DOMAIN 43..75
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT SITE 47
FT /note="Important residue for binding Kv1.3/KCNA3"
FT /evidence="ECO:0000250|UniProtKB:P29187"
FT SITE 49
FT /note="Important residue for binding Kv1.3/KCNA3"
FT /evidence="ECO:0000250|UniProtKB:P29187"
FT SITE 51
FT /note="Important residue for binding Kv1.3/KCNA3"
FT /evidence="ECO:0000250|UniProtKB:P29187"
FT SITE 60
FT /note="Important residue for binding Kv1.3/KCNA3"
FT /evidence="ECO:0000250|UniProtKB:P29187"
FT SITE 61
FT /note="Important residue for binding Kv1.3/KCNA3"
FT /evidence="ECO:0000250|UniProtKB:P29187"
FT SITE 62
FT /note="Key residue for binding both Kv1.2/KCNA2 and
FT Kv1.3/KCNA3 (occludes the channel pore like a cork in a
FT bottle)"
FT /evidence="ECO:0000250|UniProtKB:P29187"
FT SITE 63
FT /note="Important residue for binding Kv1.3/KCNA3"
FT /evidence="ECO:0000250|UniProtKB:P29187"
FT SITE 67
FT /note="Important residue for binding Kv1.3/KCNA3"
FT /evidence="ECO:0000250|UniProtKB:P29187"
FT DISULFID 43..75
FT /evidence="ECO:0000250|UniProtKB:P29187"
FT DISULFID 52..68
FT /evidence="ECO:0000250|UniProtKB:P29187"
FT DISULFID 57..72
FT /evidence="ECO:0000250|UniProtKB:P29187"
SQ SEQUENCE 75 AA; 8649 MW; 9E163D99BADA1459 CRC64;
MKFQMIAAVL LIAFCLSVVV TARMELQDDE EMKNGSFQKR RTCIDTIPKS RCTAFQCKHS
MKYRLSFCRK TCGTC
