KA154_ANDAU
ID KA154_ANDAU Reviewed; 59 AA.
AC Q867F4;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Potassium channel toxin alpha-KTx 15.4 {ECO:0000305};
DE Short=AaTX1 {ECO:0000303|PubMed:12467669};
DE Short=Toxin Aa1 {ECO:0000303|PubMed:11018665};
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 [GENOMIC DNA / MRNA].
RC TISSUE=Muscle, and Venom gland;
RX PubMed=12467669; DOI=10.1016/s0041-0101(02)00212-x;
RA Legros C., Bougis P.E., Martin-Eauclaire M.-F.;
RT "Characterisation of the genes encoding Aa1 isoforms from the scorpion
RT Androctonus australis.";
RL Toxicon 41:115-119(2003).
RN [2]
RP PROTEIN SEQUENCE OF 23-59, MASS SPECTROMETRY, PYROGLUTAMATE FORMATION AT
RP GLN-23, FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Garzoni; TISSUE=Venom;
RX PubMed=11018665; DOI=10.1016/s0005-2736(00)00259-5;
RA Pisciotta M., Coronas F.I., Bloch C. Jr., Prestipino G., Possani L.D.;
RT "Fast K(+) currents from cerebellum granular cells are completely blocked
RT by a peptide purified from Androctonus australis Garzoni scorpion venom.";
RL Biochim. Biophys. Acta 1468:203-212(2000).
RN [3]
RP SYNTHESIS OF 23-59, AND FUNCTION.
RX PubMed=12473099; DOI=10.1046/j.1432-1033.2002.03294.x;
RA Vacher H., Alami M., Crest M., Possani L.D., Bougis P.E.,
RA Martin-Eauclaire M.-F.;
RT "Expanding the scorpion toxin alpha-KTX 15 family with AmmTX3 from
RT Androctonus mauretanicus.";
RL Eur. J. Biochem. 269:6037-6041(2002).
CC -!- FUNCTION: Blocker of A-type voltage-gated potassium channels of
CC cerebellar granular cells (PubMed:11018665). May also inhibit Kv4/KCND
CC when coexpressed with DPP6 or DPP10 (By similarity). The occlusion of
CC the outer entry of the K(+) conducting pore is partially reversible and
CC affects both open and closed channels (PubMed:11018665). It shares the
CC same target in rat brain than BmTX3 (AC Q8I0L5) and AmmTX3 (AC P60208).
CC {ECO:0000250|UniProtKB:P60208, ECO:0000269|PubMed:11018665,
CC ECO:0000269|PubMed:12473099}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11018665}.
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:P84777}.
CC -!- MASS SPECTROMETRY: Mass=3850.83; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11018665};
CC -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC channel inhibitor family. Alpha-KTx 15 subfamily. {ECO:0000305}.
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DR EMBL; AJ427745; CAD20744.1; -; Genomic_DNA.
DR EMBL; AJ427743; CAD20742.1; -; mRNA.
DR AlphaFoldDB; Q867F4; -.
DR SMR; Q867F4; -.
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 SUPFAM; SSF57095; SSF57095; 1.
DR PROSITE; PS01138; SCORP_SHORT_TOXIN; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Potassium channel impairing toxin; Pyrrolidone carboxylic acid;
KW Secreted; Signal; Toxin; Voltage-gated potassium channel impairing toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:11018665"
FT CHAIN 23..59
FT /note="Potassium channel toxin alpha-KTx 15.4"
FT /evidence="ECO:0000269|PubMed:11018665"
FT /id="PRO_0000035310"
FT SITE 28
FT /note="Hot spot basic residue in hERG blocking currents"
FT /evidence="ECO:0000250|UniProtKB:P60233"
FT SITE 40
FT /note="Hot spot basic residue in hERG blocking currents"
FT /evidence="ECO:0000250|UniProtKB:P60233"
FT SITE 41
FT /note="Hot spot basic residue in hERG blocking currents"
FT /evidence="ECO:0000250|UniProtKB:P60233"
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:0000269|PubMed:11018665"
FT DISULFID 30..50
FT /evidence="ECO:0000250|UniProtKB:Q86BX0"
FT DISULFID 35..55
FT /evidence="ECO:0000250|UniProtKB:Q86BX0"
FT DISULFID 39..57
FT /evidence="ECO:0000250|UniProtKB:Q86BX0"
FT CONFLICT 24
FT /note="I -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 59 AA; 6291 MW; E429B1B607A2F64E CRC64;
MKFSSIILLT LLICSMSIFG NCQIETNKKC QGGSCASVCR RVIGVAAGKC INGRCVCYP
