KA166_BUTOS
ID KA166_BUTOS Reviewed; 58 AA.
AC B8XH42;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Potassium channel toxin alpha-KTx 16.6;
DE AltName: Full=Toxin Tx608;
DE Flags: Precursor;
OS Buthus occitanus israelis (Common yellow scorpion) (Buthus israelis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Buthus.
OX NCBI_TaxID=539894;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Zilberberg N., Kozminsky-Atias A.;
RT "Buthus occitanus israelis scorpion toxin.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Inhibits potassium channel. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC beta-sheet by disulfide bonds (CSalpha/beta). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC channel inhibitor family. Alpha-KTx 16 subfamily. {ECO:0000305}.
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DR EMBL; FJ360831; ACJ23151.1; -; mRNA.
DR AlphaFoldDB; B8XH42; -.
DR SMR; B8XH42; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR InterPro; IPR001947; Scorpion_toxinS_K_inh.
DR Pfam; PF00451; Toxin_2; 1.
DR SUPFAM; SSF57095; SSF57095; 1.
DR PROSITE; PS01138; SCORP_SHORT_TOXIN; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW Potassium channel impairing toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..58
FT /note="Potassium channel toxin alpha-KTx 16.6"
FT /id="PRO_0000428824"
FT SITE 49
FT /note="Basic residue of the functional dyad"
FT /evidence="ECO:0000250"
FT SITE 58
FT /note="Aromatic residue of the functional dyad"
FT /evidence="ECO:0000250"
FT DISULFID 29..50
FT /evidence="ECO:0000250"
FT DISULFID 35..55
FT /evidence="ECO:0000250"
FT DISULFID 39..57
FT /evidence="ECO:0000250"
SQ SEQUENCE 58 AA; 6512 MW; 073AEE37C8D1D738 CRC64;
MKILSVLLIA LIICSINICS EAGLIDVRCY ASRECWEPCR RVTGSAQAKC QNNQCRCY