KAX83_LEIHE
ID KAX83_LEIHE Reviewed; 29 AA.
AC P80670;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Potassium channel toxin alpha-KTx 8.3 {ECO:0000305};
DE AltName: Full=Gating modifier of anion channels 2 {ECO:0000303|PubMed:19574231};
DE Short=Toxin GaTx2 {ECO:0000303|PubMed:19574231};
DE AltName: Full=Leiuropeptide II {ECO:0000303|PubMed:9266482};
DE Short=LpII;
DE AltName: Full=Leiuropeptide-2 {ECO:0000305};
OS Leiurus hebraeus (Deathstalker scorpion) (Leiurus quinquestriatus
OS hebraeus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Leiurus.
OX NCBI_TaxID=6884;
RN [1]
RP PROTEIN SEQUENCE, STRUCTURE BY NMR, DISULFIDE BONDS, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Venom;
RX PubMed=9266482; DOI=10.1111/j.1399-3011.1997.tb01162.x;
RA Buisine E., Wieruszeski J.-M., Lippens G., Wouters D., Tartar A.,
RA Sautiere P.;
RT "Characterization of a new family of toxin-like peptides from the venom of
RT the scorpion Leiurus quinquestriatus hebraeus. 1H-NMR structure of
RT leiuropeptide II.";
RL J. Pept. Res. 49:545-555(1997).
RN [2]
RP PROTEIN SEQUENCE, SYNTHESIS, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=19574231; DOI=10.1074/jbc.m109.031724;
RA Thompson C.H., Olivetti P.R., Fuller M.D., Freeman C.S., McMaster D.,
RA French R.J., Pohl J., Kubanek J., McCarty N.A.;
RT "Isolation and characterization of a high affinity peptide inhibitor of
RT ClC-2 chloride channels.";
RL J. Biol. Chem. 284:26051-26062(2009).
RN [3]
RP FUNCTION.
RX PubMed=16596447; DOI=10.1007/s00232-005-0818-8;
RA Thompson C.H., Fields D.M., Olivetti P.R., Fuller M.D., Zhang Z.R.,
RA Kubanek J., McCarty N.A.;
RT "Inhibition of ClC-2 chloride channels by a peptide component or components
RT of scorpion venom.";
RL J. Membr. Biol. 208:65-76(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16551474; DOI=10.1016/j.toxicon.2006.01.015;
RA Nascimento D.G., Rates B., Santos D.M., Verano-Braga T., Barbosa-Silva A.,
RA Dutra A.A.A., Biondi I., Martin-Eauclaire M.-F., De Lima M.E.,
RA Pimenta A.M.C.;
RT "Moving pieces in a taxonomic puzzle: venom 2D-LC/MS and data clustering
RT analyses to infer phylogenetic relationships in some scorpions from the
RT Buthidae family (Scorpiones).";
RL Toxicon 47:628-639(2006).
CC -!- FUNCTION: Specific and potent inhibitor of ClC-2/CLCN2 chloride
CC channel. It slows ClC-2/CLCN2 activation by increasing the latency to
CC first opening by nearly 8-fold but is unable to inhibit open channels,
CC suggesting that this toxin inhibits channel activation gating.
CC {ECO:0000269|PubMed:16596447, ECO:0000269|PubMed:19574231}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9266482}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:9266482}.
CC -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC beta-sheet by disulfide bonds (CSalpha/beta).
CC {ECO:0000269|PubMed:9266482}.
CC -!- MASS SPECTROMETRY: Mass=3191.29; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:19574231};
CC -!- MISCELLANEOUS: Does not inhibit ClC-0, ClC-1/CLCN1, ClC-3/CLCN3, ClC-
CC 4/CLCN4, CFTR chloride channel, GABRR, calcium-activated chloride
CC channel regulator (Cl(Ca)), Shaker, and Kv1.2/KCNA2.
CC {ECO:0000269|PubMed:19574231}.
CC -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC channel inhibitor family. Alpha-KTx 08 subfamily.
CC {ECO:0000269|PubMed:9266482}.
CC -!- CAUTION: Has sequence similarities with potassium channel inhibitors,
CC but inhibits chloride channels. It is why the systematic name
CC 'Potassium channel toxin alpha-KTx 8.3' has been moved as alternative
CC name. {ECO:0000305}.
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DR AlphaFoldDB; P80670; -.
DR SMR; P80670; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0017081; F:chloride channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR InterPro; IPR008911; Toxin_alpha-KTx_8/9.
DR Pfam; PF05453; Toxin_6; 1.
DR SUPFAM; SSF57095; SSF57095; 1.
PE 1: Evidence at protein level;
KW Chloride channel impairing toxin; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin; Secreted; Toxin;
KW Voltage-gated chloride channel impairing toxin.
FT PEPTIDE 1..29
FT /note="Potassium channel toxin alpha-KTx 8.3"
FT /evidence="ECO:0000269|PubMed:19574231,
FT ECO:0000269|PubMed:9266482"
FT /id="PRO_0000044542"
FT DISULFID 3..19
FT /evidence="ECO:0000269|PubMed:9266482"
FT DISULFID 6..24
FT /evidence="ECO:0000269|PubMed:9266482"
FT DISULFID 10..26
FT /evidence="ECO:0000269|PubMed:9266482"
SQ SEQUENCE 29 AA; 3199 MW; BC5F650C196C15B8 CRC64;
VSCEDCPDHC STQKARAKCD NDKCVCEPI
