KAX1C_LEIHE
ID KAX1C_LEIHE Reviewed; 59 AA.
AC P59943;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Potassium channel toxin alpha-KTx 1.12;
DE AltName: Full=Charybdotoxin b {ECO:0000303|PubMed:9929387};
DE Short=ChTx-b {ECO:0000303|PubMed:9929387};
DE Flags: Precursor;
OS Leiurus hebraeus (Deathstalker scorpion) (Leiurus quinquestriatus
OS hebraeus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Leiurus.
OX NCBI_TaxID=6884;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Single abdominal segment;
RX PubMed=9929387; DOI=10.1007/pl00006457;
RA Froy O., Sagiv T., Poreh M., Urbach D., Zilberberg N., Gurevitz M.;
RT "Dynamic diversification from a putative common ancestor of scorpion toxins
RT affecting sodium, potassium, and chloride channels.";
RL J. Mol. Evol. 48:187-196(1999).
CC -!- FUNCTION: Potent selective inhibitor of high conductance (maxi-K),
CC different medium and small conductance calcium-activated potassium
CC channels (KCa1.1/KCNMA1 and others), as well as a voltage-dependent
CC potassium channel (Kv1.3/KCNA3>Kv1.2/KCNA2>Kv1.6/KCNA3>>Shaker/Sh). It
CC blocks channel activity by a simple bimolecular inhibition process.
CC {ECO:0000250|UniProtKB:P13487}.
CC -!- FUNCTION: Has a pH-specific antimicrobial activity against bacteria
CC (B.subtilis, E.coli and S.aureus) and the fungus C.albicans.
CC {ECO:0000250|UniProtKB:P13487}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P13487}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC beta-sheet by disulfide bonds (CSalpha/beta).
CC {ECO:0000250|UniProtKB:P13487}.
CC -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC channel inhibitor family. Alpha-KTx 01 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P59943; -.
DR SMR; P59943; -.
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 GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; 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 Antibiotic; Antimicrobial;
KW Calcium-activated potassium channel impairing toxin; Disulfide bond;
KW Fungicide; Ion channel impairing toxin; Neurotoxin;
KW Potassium channel impairing toxin; Pyrrolidone carboxylic acid; Secreted;
KW Signal; Toxin; Voltage-gated potassium channel impairing toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000250|UniProtKB:P13487"
FT CHAIN 23..59
FT /note="Potassium channel toxin alpha-KTx 1.12"
FT /id="PRO_0000035308"
FT REGION 48..55
FT /note="Interaction with Ca(2+)-activated K(+) channels"
FT /evidence="ECO:0000255"
FT SITE 49
FT /note="Basic residue of the functional dyad"
FT /evidence="ECO:0000250"
FT SITE 58
FT /note="Aromatic residue of the functional dyad"
FT /evidence="ECO:0000250"
FT MOD_RES 23
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P13487"
FT DISULFID 29..50
FT /evidence="ECO:0000250|UniProtKB:P13487"
FT DISULFID 35..55
FT /evidence="ECO:0000250|UniProtKB:P13487"
FT DISULFID 39..57
FT /evidence="ECO:0000250|UniProtKB:P13487"
SQ SEQUENCE 59 AA; 6632 MW; 379C290B41051947 CRC64;
MKILSVLLLA LIICSIVGWS EAQFTDVSCT TSKECWSVCQ RLHNTSIGKC MNKKCRCYS