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KA11L_LYCMC
ID   KA11L_LYCMC             Reviewed;          65 AA.
AC   A9QLM3;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Toxin KTx8;
DE            Short=LmKTx8 {ECO:0000303|PubMed:18006119};
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=18006119; DOI=10.1016/j.peptides.2007.10.009;
RA   Wu W., Yin S., Ma Y., Wu Y.L., Zhao R., Gan G., Ding J., Cao Z., Li W.;
RT   "Molecular cloning and electrophysiological studies on the first K(+)
RT   channel toxin (LmKTx8) derived from scorpion Lychas mucronatus.";
RL   Peptides 28:2306-2312(2007).
CC   -!- FUNCTION: This recombinant toxin inhibits the mammalian voltage-gated
CC       potassium channels Kv1.3/KCNA3 in vitro with an IC(50) of 26.40 nM.
CC       {ECO:0000269|PubMed:18006119}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:18006119}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:18006119}.
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   -!- MISCELLANEOUS: This toxin does not have effect on BK currents
CC       (KCa1.1/KCNMA1 channels). {ECO:0000305|PubMed:18006119}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 11 subfamily. {ECO:0000305}.
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DR   EMBL; EU118812; ABW90713.1; -; mRNA.
DR   AlphaFoldDB; A9QLM3; -.
DR   SMR; A9QLM3; -.
DR   TCDB; 8.B.2.2.2; the short scorpion toxin (s-st) superfamily.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   SUPFAM; SSF57095; SSF57095; 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..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..65
FT                   /note="Toxin KTx8"
FT                   /evidence="ECO:0000305|PubMed:18006119"
FT                   /id="PRO_0000396528"
FT   DISULFID        31..53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        38..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        42..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
SQ   SEQUENCE   65 AA;  6912 MW;  7AB2AF07161EB2AB CRC64;
     MNKVCFVVVL VLFVALAAYV SPIEGVPTGG CPLSDSLCAK YCKSHKFGKT GRCTGPNKMK
     CKCLV
 
 
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