ID   KAX6V_HETLA             Reviewed;          34 AA.
AC   C0HJN0;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2019, sequence version 2.
DT   23-FEB-2022, entry version 12.
DE   RecName: Full=Potassium channel toxin alpha-KTx 6 hetlaxin {ECO:0000303|PubMed:23657660};
OS   Heterometrus laoticus (Thai giant scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Scorpionoidea; Scorpionidae; Heterometrinae;
OC   Heterometrus.
OX   NCBI_TaxID=217256;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BONDS, MASS
RP   SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY, AND AMIDATION AT CYS-34.
RC   TISSUE=Venom;
RX   PubMed=24189292; DOI=10.1016/j.toxicon.2013.10.027;
RA   Hoang A.N., Vo H.D., Vo N.P., Kudryashova K.S., Nekrasova O.V.,
RA   Feofanov A.V., Kirpichnikov M.P., Andreeva T.V., Serebryakova M.V.,
RA   Tsetlin V.I., Utkin Y.N.;
RT   "Vietnamese Heterometrus laoticus scorpion venom: evidence for analgesic
RT   and anti-inflammatory activity and isolation of new polypeptide toxin
RT   acting on Kv1.3 potassium channel.";
RL   Toxicon 77:40-48(2014).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BONDS, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=23657660; DOI=10.1134/s1607672913020142;
RA   Anh H.N., Hoang V.D.M., Kudryashova K.S., Nekrasova O.V., Feofanov A.V.,
RA   Andreeva T.V., Tsetlin V.I., Utkin Y.N.;
RT   "Hetlaxin, a new toxin from the Heterometrus laoticus scorpion venom,
RT   interacts with voltage-gated potassium channel Kv1.3.";
RL   Dokl. Biochem. Biophys. 449:109-111(2013).
CC   -!- FUNCTION: Binds to voltage-gated potassium channels Kv1.3/KCNA3
CC       (IC(50)=0.48 uM) and Kv1.1/KCNA1 (IC(50)=6.7 uM) and inhibits channel
CC       activity. {ECO:0000269|PubMed:23657660, ECO:0000269|PubMed:24189292}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23657660,
CC       ECO:0000269|PubMed:24189292}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:23657660, ECO:0000305|PubMed:24189292}.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC       antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC       {ECO:0000305}.
CC   -!- PTM: Contains 4 disulfide bonds. {ECO:0000269|PubMed:23657660,
CC       ECO:0000269|PubMed:24189292}.
CC   -!- MASS SPECTROMETRY: Mass=3670.8; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:24189292};
CC   -!- MASS SPECTROMETRY: Mass=3669.2; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:23657660};
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 06 subfamily. {ECO:0000255}.
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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   PRINTS; PR00286; CHARYBDTOXIN.
DR   SUPFAM; SSF57095; SSF57095; 1.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Potassium channel impairing toxin; Secreted;
KW   Toxin; Voltage-gated potassium channel impairing toxin.
FT   PEPTIDE         1..34
FT                   /note="Potassium channel toxin alpha-KTx 6 hetlaxin"
FT                   /evidence="ECO:0000269|PubMed:24189292"
FT                   /id="PRO_0000430775"
FT   MOD_RES         34
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:24189292"
FT   DISULFID        3..24
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
FT   DISULFID        9..29
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
FT   DISULFID        13..31
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
FT   DISULFID        19..34
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
FT   UNSURE          29
FT                   /note="Assigned by comparison with orthologs"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   34 AA;  3666 MW;  0B4848C3CE349A4E CRC64;
     ISCTGSKQCY DPCKKKTGCP NAKCMNKSCX CYGC