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KAX88_ORTSC
ID   KAX88_ORTSC             Reviewed;          57 AA.
AC   A0A1L2FZD4; C0HK17;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Potassium channel toxin alpha-KTx 8.8 {ECO:0000303|PubMed:28179135};
DE   AltName: Full=OSK3 {ECO:0000303|PubMed:28179135};
DE   Flags: Precursor;
OS   Orthochirus scrobiculosus (Central Asian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Orthochirus.
OX   NCBI_TaxID=6892;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-57, FUNCTION,
RP   SUBCELLULAR LOCATION, PRESENCE OF DISULFIDE BONDS, AND MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=28179135; DOI=10.1016/j.bbapap.2017.02.001;
RA   Kuzmenkov A.I., Peigneur S., Chugunov A.O., Tabakmakher V.M., Efremov R.G.,
RA   Tytgat J., Grishin E.V., Vassilevski A.A.;
RT   "C-Terminal residues in small potassium channel blockers OdK1 and OSK3 from
RT   scorpion venom fine-tune the selectivity.";
RL   Biochim. Biophys. Acta 1865:465-472(2017).
CC   -!- FUNCTION: Selectively inhibits voltage-gated potassium channels
CC       rKv1.2/KCNA2 (IC(50)=331 nM) and hKv1.3/KCNA3 (IC(50)=503 nM).
CC       Partially inihibts rKv1.6/KCNA6 (IC(50)=9983 nM).
CC       {ECO:0000269|PubMed:28179135}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28179135}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:28179135}.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC       beta-sheet by disulfide bonds (CSalpha/beta).
CC       {ECO:0000250|UniProtKB:P56215}.
CC   -!- PTM: Contains 3 disulfide bonds. {ECO:0000269|PubMed:28179135}.
CC   -!- MASS SPECTROMETRY: Mass=3206.3; Mass_error=0.2; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:28179135};
CC   -!- MISCELLANEOUS: This toxin does not affect the following channels:
CC       rKv1.1/KCNA1, rKv1.4/KCNA4, rKv1.5/KCNA5, Shaker IR (with inactivation
CC       domain removed), rKv2.1/KCNB1, hKv3.1/KCNC1, rKv4.2/KCND2 and
CC       hKv11.1/KCNH2/ERG1. {ECO:0000269|PubMed:28179135}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 08 subfamily. {ECO:0000305}.
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DR   EMBL; KX355614; AOG62199.1; -; mRNA.
DR   AlphaFoldDB; A0A1L2FZD4; -.
DR   SMR; A0A1L2FZD4; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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   GO; GO:0044361; P:negative regulation of voltage-gated potassium channel activity in another organism; IDA:UniProtKB.
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   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..28
FT                   /evidence="ECO:0000305|PubMed:28179135"
FT                   /id="PRO_0000439599"
FT   PEPTIDE         29..57
FT                   /note="Potassium channel toxin alpha-KTx 8.8"
FT                   /evidence="ECO:0000269|PubMed:28179135"
FT                   /id="PRO_0000439600"
FT   DISULFID        31..47
FT                   /evidence="ECO:0000250|UniProtKB:P56215"
FT   DISULFID        34..52
FT                   /evidence="ECO:0000250|UniProtKB:P56215"
FT   DISULFID        38..54
FT                   /evidence="ECO:0000250|UniProtKB:P56215"
SQ   SEQUENCE   57 AA;  6386 MW;  A84D78A2DD492917 CRC64;
     MCRLYAIILI VLVMNVIMTI IPDSKVEVVS CEDCPEHCST QKARAKCDND KCVCEPI
 
 
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