KA164_MESEU
ID KA164_MESEU Reviewed; 59 AA.
AC D3JXM1; F5CJW1;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 2.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=Potassium channel toxin alpha-KTx 16.4;
DE AltName: Full=Alpha-KTx MeuTx3B;
DE AltName: Full=MeuKTx-4;
DE Flags: Precursor;
OS Mesobuthus eupeus (Lesser Asian scorpion) (Buthus eupeus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX NCBI_TaxID=34648;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-59, FUNCTION, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=21466856; DOI=10.1016/j.cbpa.2011.03.027;
RA Gao B., Peigneur S., Dalziel J., Tytgat J., Zhu S.;
RT "Molecular divergence of two orthologous scorpion toxins affecting
RT potassium channels.";
RL Comp. Biochem. Physiol. 159:313-321(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-59.
RA Zhu S., Gao B.;
RT "Molecular characterization of a scorpion toxin specifically targeting
RT Kv1.3 potassium channel from the Mesobuthus eupeus venom.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 23-59, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Venom;
RA Zhu S., Gao B.;
RT "Molecular characterization of a new scorpion potassium channel toxin: 3.-
RT UTR divergence between two orthologous toxins.";
RL Submitted (APR-2010) to UniProtKB.
CC -!- FUNCTION: Weak inhibitor of voltage-gated potassium channel
CC hKv1.3/KCNA3. {ECO:0000269|PubMed:21466856}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.3}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000269|Ref.3}.
CC -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC beta-sheet by disulfide bonds (CSalpha/beta).
CC -!- MASS SPECTROMETRY: Mass=4066.8; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21466856};
CC -!- MISCELLANEOUS: Does not inhibit large conductance calcium-activated
CC potassium channels (KCa1.1/KCNMA1). {ECO:0000305|PubMed:21466856}.
CC -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC channel inhibitor family. Alpha-KTx 16 subfamily. {ECO:0000305}.
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DR EMBL; JF719812; AEC22868.1; -; mRNA.
DR EMBL; GU327370; ADB82798.1; -; mRNA.
DR AlphaFoldDB; D3JXM1; -.
DR SMR; D3JXM1; -.
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 PRINTS; PR00286; CHARYBDTOXIN.
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; Secreted; Signal; Toxin;
KW Voltage-gated potassium channel impairing toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:21466856, ECO:0000269|Ref.3"
FT PEPTIDE 23..59
FT /note="Potassium channel toxin alpha-KTx 16.4"
FT /evidence="ECO:0000269|PubMed:21466856, ECO:0000269|Ref.3"
FT /id="PRO_0000394730"
FT SITE 50
FT /note="Basic residue of the functional dyad"
FT /evidence="ECO:0000250"
FT SITE 59
FT /note="Aromatic residue of the functional dyad"
FT /evidence="ECO:0000250"
FT DISULFID 30..51
FT /evidence="ECO:0000250"
FT DISULFID 36..56
FT /evidence="ECO:0000250"
FT DISULFID 40..58
FT /evidence="ECO:0000250"
SQ SEQUENCE 59 AA; 6402 MW; 01A0AFD47DF1AE36 CRC64;
MKILSIVLIA LIICSISICT EAFGLIDVKC SASRECWVAC KKVTGSGQGK CQNNQCRCY
