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