ID   KA104_CENTE             Reviewed;          33 AA.
AC   C0HJW2;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   06-JUL-2016, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Potassium channel toxin alpha-KTx 10.4 {ECO:0000303|PubMed:26921461};
DE   AltName: Full=Toxin II.10.4 {ECO:0000303|PubMed:26921461};
OS   Centruroides tecomanus (Scorpion) (Centruroides limpidus tecomanus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX   NCBI_TaxID=1028682;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=26921461; DOI=10.1016/j.toxicon.2016.02.017;
RA   Olamendi-Portugal T., Bartok A., Zamudio-Zuniga F., Balajthy A.,
RA   Becerril B., Panyi G., Possani L.D.;
RT   "Isolation, chemical and functional characterization of several new K(+)-
RT   channel blocking peptides from the venom of the scorpion Centruroides
RT   tecomanus.";
RL   Toxicon 115:1-12(2016).
CC   -!- FUNCTION: Blocks human voltage-gated potassium channel Kv1.2/KCNA2
CC       (IC(50)=3.6 nM) and Kv1.3/KCNA3 (IC(50)=72 nM).
CC       {ECO:0000269|PubMed:26921461}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26921461}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:26921461}.
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   -!- MASS SPECTROMETRY: Mass=3804.2; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:26921461};
CC   -!- MISCELLANEOUS: Does not block voltage-gated potassium channel
CC       Kv1.1/KCNA1, intermediate conductance calcium-activated potassium
CC       channel KCa3.1/KCNN4 or the Shaker IR (with inactivation domain
CC       removed). {ECO:0000269|PubMed:26921461}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 10 subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; C0HJW2; -.
DR   SMR; C0HJW2; -.
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.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Potassium channel impairing toxin; Secreted; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   PEPTIDE         1..33
FT                   /note="Potassium channel toxin alpha-KTx 10.4"
FT                   /evidence="ECO:0000269|PubMed:26921461"
FT                   /id="PRO_0000436539"
FT   SITE            21
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000250|UniProtKB:O46028"
FT   SITE            30
FT                   /note="Aromatic residue of the functional dyad"
FT                   /evidence="ECO:0000250|UniProtKB:O46028"
FT   DISULFID        3..22
FT                   /evidence="ECO:0000250|UniProtKB:O46028"
FT   DISULFID        8..27
FT                   /evidence="ECO:0000250|UniProtKB:O46028"
FT   DISULFID        12..29
FT                   /evidence="ECO:0000250|UniProtKB:O46028"
SQ   SEQUENCE   33 AA;  3809 MW;  B884D830A309D82F CRC64;
     AVCVYRTCDK DCKRRGYRSG KCINNACKCY PYA