KA125_LYCMC
ID KA125_LYCMC Reviewed; 60 AA.
AC P0CH12; D9U2A9;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=Potassium channel toxin alpha-KTx 12.5;
DE AltName: Full=Toxin alpha-KTx10;
DE Short=LmKTx10;
DE Flags: Precursor;
OS Lychas mucronatus (Chinese swimming scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Lychas.
OX NCBI_TaxID=172552;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND RECOMBINANT EXPRESSION.
RC TISSUE=Venom gland;
RX PubMed=19103241; DOI=10.1016/j.peptides.2008.11.015;
RA Liu J., Ma Y., Yin S., Zhao R., Fan S., Hu Y., Wu Y., Cao Z., Li W.;
RT "Molecular cloning and functional identification of a new K(+) channel
RT blocker, LmKTx10, from the scorpion Lychas mucronatus.";
RL Peptides 30:675-680(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hainan; TISSUE=Venom gland;
RX PubMed=20663230; DOI=10.1186/1471-2164-11-452;
RA Zhao R., Ma Y., He Y., Di Z., Wu Y.-L., Cao Z.-J., Li W.-X.;
RT "Comparative venom gland transcriptome analysis of the scorpion Lychas
RT mucronatus reveals intraspecific toxic gene diversity and new venomous
RT components.";
RL BMC Genomics 11:452-452(2010).
CC -!- FUNCTION: This recombinant toxin inhibits the mammalian voltage-gated
CC potassium channels Kv1.3/KCNA3 (IC(50)=28 nM). Kv1.1/KCNA1 and
CC Kv1.2/KCNA2 potassium channels are also weakly inhibited (IC(50)=1.73
CC uM and IC(50)=12.63 uM, respectively). {ECO:0000269|PubMed:19103241}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:19103241,
CC ECO:0000305|PubMed:20663230}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:19103241, ECO:0000305|PubMed:20663230}.
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 12 subfamily. {ECO:0000305}.
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DR EMBL; EU163856; ABY26665.1; -; mRNA.
DR AlphaFoldDB; P0CH12; -.
DR SMR; P0CH12; -.
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 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..60
FT /note="Potassium channel toxin alpha-KTx 12.5"
FT /evidence="ECO:0000305|PubMed:19103241"
FT /id="PRO_0000396529"
FT SITE 50
FT /note="Basic residue of the functional dyad"
FT /evidence="ECO:0000250"
FT SITE 59
FT /note="Aromatic residue of the functional dyad"
FT /evidence="ECO:0000250"
FT DISULFID 30..51
FT /evidence="ECO:0000250"
FT DISULFID 36..56
FT /evidence="ECO:0000250"
FT DISULFID 40..58
FT /evidence="ECO:0000250"
SQ SEQUENCE 60 AA; 6720 MW; AFD82216067F291B CRC64;
MNKLPILIFM LLVCSMFISS DCQKHTDIKC SSSSSCYEPC RGVTGRAHGK CMNGRCTCYY
