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KAX6A_OPICA
ID   KAX6A_OPICA             Reviewed;          60 AA.
AC   Q6XLL5;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Potassium channel toxin alpha-KTx 6.10 {ECO:0000303|PubMed:14696198};
DE   AltName: Full=OcKTx5 {ECO:0000303|PubMed:14696198};
DE   Flags: Precursor;
OS   Opistophthalmus carinatus (African yellow leg scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Scorpionoidea; Scorpionidae; Opistophthalminae;
OC   Opistophthalmus.
OX   NCBI_TaxID=190115;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=14696198; DOI=10.1002/prot.10588;
RA   Zhu S.-Y., Huys I., Dyason K., Verdonck F., Tytgat J.;
RT   "Evolutionary trace analysis of scorpion toxins specific for K-channels.";
RL   Proteins 54:361-370(2004).
RN   [2]
RP   FUNCTION, AND SYNTHESIS OF 24-59.
RX   PubMed=29483648; DOI=10.1038/s41594-018-0033-9;
RA   Correnti C.E., Gewe M.M., Mehlin C., Bandaranayake A.D., Johnsen W.A.,
RA   Rupert P.B., Brusniak M.Y., Clarke M., Burke S.E., De Van Der Schueren W.,
RA   Pilat K., Turnbaugh S.M., May D., Watson A., Chan M.K., Bahl C.D.,
RA   Olson J.M., Strong R.K.;
RT   "Screening, large-scale production and structure-based classification of
RT   cystine-dense peptides.";
RL   Nat. Struct. Mol. Biol. 25:270-278(2018).
CC   -!- FUNCTION: Inhibits Kv1.2/KCNA2 and Kv1.3/KCNA3 and weakly inhibit
CC       Kv1.1/KCNA1 voltage-gated potassium channels (PubMed:29483648).
CC       {ECO:0000269|PubMed:29483648}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:14696198}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:14696198}.
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   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 06 subfamily. {ECO:0000305}.
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DR   EMBL; AY225783; AAP73821.1; -; mRNA.
DR   AlphaFoldDB; Q6XLL5; -.
DR   SMR; Q6XLL5; -.
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.
DR   PROSITE; PS01138; SCORP_SHORT_TOXIN; 1.
PE   3: Inferred from homology;
KW   Amidation; Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..59
FT                   /note="Potassium channel toxin alpha-KTx 6.10"
FT                   /id="PRO_0000227035"
FT   SITE            48
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
FT   SITE            57
FT                   /note="Aromatic residue of the functional dyad"
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
FT   MOD_RES         59
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
FT   DISULFID        28..49
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
FT   DISULFID        34..54
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
FT   DISULFID        38..56
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
FT   DISULFID        44..59
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
SQ   SEQUENCE   60 AA;  6514 MW;  D672EAC08057143D CRC64;
     MNAKFILLLV LTTMMLLPDT KGAEVIRCSG SKQCYGPCKQ QTGCTNSKCM NKVCKCYGCG
 
 
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