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Potassium channel toxin alpha-KTx 1.13 (Charybdotoxin c) (ChTx-c)

 KAX1D_LEIQH             Reviewed;          37 AA.
P59944;
31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
31-OCT-2003, sequence version 1.
22-NOV-2017, entry version 51.
RecName: Full=Potassium channel toxin alpha-KTx 1.13;
AltName: Full=Charybdotoxin c {ECO:0000303|PubMed:9929387};
Short=ChTx-c {ECO:0000303|PubMed:9929387};
Leiurus quinquestriatus hebraeus (Yellow scorpion).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
Scorpiones; Buthida; Buthoidea; Buthidae; Leiurus.
NCBI_TaxID=6884;
[1]
PROTEIN SEQUENCE.
TISSUE=Venom;
PubMed=9929387; DOI=10.1007/PL00006457;
Froy O., Sagiv T., Poreh M., Urbach D., Zilberberg N., Gurevitz M.;
"Dynamic diversification from a putative common ancestor of scorpion
toxins affecting sodium, potassium, and chloride channels.";
J. Mol. Evol. 48:187-196(1999).
-!- FUNCTION: Potent selective inhibitor of high conductance (maxi-K),
different medium and small conductance calcium-activated potassium
channels (KCa1.1/KCNMA1 and others), as well as a voltage-
dependent potassium channel
(Kv1.3/KCNA3>Kv1.2/KCNA2>Kv1.6/KCNA3>>Shaker/Sh). It blocks
channel activity by a simple bimolecular inhibition process.
{ECO:0000250|UniProtKB:P13487}.
-!- FUNCTION: Has a pH-specific antimicrobial activity against
bacteria (B.subtilis, E.coli and S.aureus) and the fungus
C.albicans. {ECO:0000250|UniProtKB:P13487}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P13487}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
-!- DOMAIN: Has the structural arrangement of an alpha-helix connected
to a beta-sheet by disulfide bonds (CSalpha/beta).
{ECO:0000250|UniProtKB:P13487}.
-!- SIMILARITY: Belongs to the short scorpion toxin superfamily.
Potassium channel inhibitor family. Alpha-KTx 01 subfamily.
{ECO:0000305}.
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ProteinModelPortal; P59944; -.
SMR; P59944; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
GO; GO:0031640; P:killing of cells of other organism; IEA:UniProtKB-KW.
Gene3D; 3.30.30.10; -; 1.
InterPro; IPR036574; Scorpion_toxin-like_sf.
InterPro; IPR001947; Scorpion_toxinS_K_inh.
Pfam; PF00451; Toxin_2; 1.
PRINTS; PR00286; CHARYBDTOXIN.
ProDom; PD003586; Scorpion_toxinS; 1.
SUPFAM; SSF57095; SSF57095; 1.
PROSITE; PS01138; SCORP_SHORT_TOXIN; 1.
1: Evidence at protein level;
Antibiotic; Antimicrobial;
Calcium-activated potassium channel impairing toxin;
Direct protein sequencing; Disulfide bond; Fungicide;
Ion channel impairing toxin; Neurotoxin;
Potassium channel impairing toxin; Pyrrolidone carboxylic acid;
Secreted; Toxin; Voltage-gated potassium channel impairing toxin.
CHAIN 1 37 Potassium channel toxin alpha-KTx 1.13.
/FTId=PRO_0000044892.
REGION 26 33 Interaction with Ca(2+)-activated K(+)
channels. {ECO:0000255}.
SITE 27 27 Basic residue of the functional dyad.
{ECO:0000250}.
SITE 36 36 Aromatic residue of the functional dyad.
{ECO:0000250}.
MOD_RES 1 1 Pyrrolidone carboxylic acid.
{ECO:0000250|UniProtKB:P13487}.
DISULFID 7 28 {ECO:0000250|UniProtKB:P13487}.
DISULFID 13 33 {ECO:0000250|UniProtKB:P13487}.
DISULFID 17 35 {ECO:0000250|UniProtKB:P13487}.
SEQUENCE 37 AA; 4318 MW; 29319BCB43994EE2 CRC64;
QFTNVSCTTS KECWSVCEKL YNTSRGKCMN KKCRCYS


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