KBX1_ANDAU
ID KBX1_ANDAU Reviewed; 91 AA.
AC P69939;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Potassium channel toxin AaTXK-beta;
DE Short=Toxin AaTXKbeta;
DE AltName: Full=Potassium channel toxin AaTXK-beta(1-64);
DE AltName: Full=Potassium channel toxin beta-KTx 2;
DE Contains:
DE RecName: Full=Potassium channel toxin AaTXK-beta(2-64);
DE Flags: Precursor;
OS Androctonus australis (Sahara scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Androctonus.
OX NCBI_TaxID=6858;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=9714546; DOI=10.1016/s0014-5793(98)00780-7;
RA Legros C., Ceard B., Bougis P.E., Martin-Eauclaire M.-F.;
RT "Evidence for a new class of scorpion toxins active against K+ channels.";
RL FEBS Lett. 431:375-380(1998).
RN [2]
RP PROTEIN SEQUENCE (POTASSIUM CHANNEL TOXIN AATXK-BETA AND POTASSIUM CHANNEL
RP TOXIN AATXK-BETA(2-64)), IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=24019223; DOI=10.1124/mol.113.088971;
RA Landoulsi Z., Miceli F., Palmese A., Amoresano A., Marino G., El Ayeb M.,
RA Taglialatela M., Benkhalifa R.;
RT "Subtype-selective activation of Kv7 channels by AaTXKbeta(2-64), a novel
RT toxin variant from the Androctonus australis scorpion venom.";
RL Mol. Pharmacol. 84:763-773(2013).
CC -!- FUNCTION: [Potassium channel toxin AaTXK-beta]: Blocks voltage-gated
CC potassium channels (Kv) (By similarity). Does not activate Kv7
CC channels. {ECO:0000250, ECO:0000269|PubMed:24019223}.
CC -!- FUNCTION: [Potassium channel toxin AaTXK-beta(2-64)]: Peptide activator
CC of Kv7.4/KCNQ4 channels. Also acts as a subtype-selective activator of
CC channels formed by Kv7.3 (KCNQ3), Kv7.2/Kv7.3 (KCNQ2/KCNQ3),
CC Kv7.5/Kv7.3 (KCNQ3/KCNQ5) subunits. {ECO:0000269|PubMed:24019223}.
CC -!- SUBUNIT: Monomer (both chains). {ECO:0000269|PubMed:24019223}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24019223}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the long chain scorpion toxin family. Class 1
CC subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P69939; -.
DR SMR; P69939; -.
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; IPR029237; Long_scorpion_toxin.
DR Pfam; PF14866; Toxin_38; 1.
DR PROSITE; PS51862; BSPN_CSAB; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW Voltage-gated potassium channel impairing toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..27
FT /id="PRO_0000035340"
FT CHAIN 28..91
FT /note="Potassium channel toxin AaTXK-beta"
FT /id="PRO_0000035341"
FT CHAIN 29..91
FT /note="Potassium channel toxin AaTXK-beta(2-64)"
FT /id="PRO_0000424386"
FT DOMAIN 54..91
FT /note="BetaSPN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT DISULFID 57..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT DISULFID 64..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT DISULFID 68..85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
SQ SEQUENCE 91 AA; 10148 MW; C4A3D2D45E2BD917 CRC64;
MQRNLVVLLF LGMVALSSCG LREKHVQKLV KYAVPVGTLR TILQTVVHKV GKTQFGCPAY
QGYCDDHCQD IKKEEGFCHG FKCKCGIPMG F
