K1A_STIME
ID K1A_STIME Reviewed; 74 AA.
AC E2S063;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 25-MAY-2022, entry version 23.
DE RecName: Full=Kappa-stichotoxin-Smt1a {ECO:0000305};
DE Short=Kappa-SHTX-Smt1a {ECO:0000305};
DE AltName: Full=Kappa-stichotoxin-Sm1a {ECO:0000303|PubMed:21339955};
DE Short=Kappa-SHTX-Sm1a {ECO:0000303|PubMed:21339955};
DE AltName: Full=Potassium channel peptide toxin sm-k {ECO:0000312|EMBL:BAJ23160.1};
DE Short=SmK {ECO:0000305};
DE Flags: Precursor;
OS Stichodactyla mertensii (Merten's carpet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Stichodactylidae; Stichodactyla.
OX NCBI_TaxID=645706;
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).
CC -!- FUNCTION: Inhibits voltage-gated potassium channels (Kv) with higher
CC potency for Kv1.1/KCNA1 and Kv1.3/KCNA3.
CC {ECO:0000250|UniProtKB:P29187}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
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; AB595206; BAJ23160.1; -; mRNA.
DR AlphaFoldDB; E2S063; -.
DR BMRB; E2S063; -.
DR SMR; E2S063; -.
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..39
FT /evidence="ECO:0000250"
FT /id="PRO_0000425834"
FT PEPTIDE 40..74
FT /note="Kappa-stichotoxin-Smt1a"
FT /evidence="ECO:0000250|UniProtKB:P29187"
FT /id="PRO_0000425833"
FT DOMAIN 42..74
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT SITE 46
FT /note="Important residue for binding Kv1.3/KCNA3"
FT /evidence="ECO:0000250|UniProtKB:P29187"
FT SITE 48
FT /note="Important residue for binding Kv1.3/KCNA3"
FT /evidence="ECO:0000250|UniProtKB:P29187"
FT SITE 50
FT /note="Important residue for binding Kv1.3/KCNA3"
FT /evidence="ECO:0000250|UniProtKB:P29187"
FT SITE 59
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="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 62
FT /note="Important residue for binding Kv1.3/KCNA3"
FT /evidence="ECO:0000250|UniProtKB:P29187"
FT SITE 66
FT /note="Important residue for binding Kv1.3/KCNA3"
FT /evidence="ECO:0000250|UniProtKB:P29187"
FT DISULFID 42..74
FT /evidence="ECO:0000250|UniProtKB:P29187"
FT DISULFID 51..67
FT /evidence="ECO:0000250|UniProtKB:P29187"
FT DISULFID 56..71
FT /evidence="ECO:0000250|UniProtKB:P29187"
SQ SEQUENCE 74 AA; 8443 MW; 11E055982DDF1D04 CRC64;
MKSQVIAAVL LIAFCLCVVV TARMELQDVE DMENGFQKRR SCIDTIPKSR CTAFQCKHSM
KYRLSFCRKT CGTC
