KA167_MESGB
ID KA167_MESGB Reviewed; 59 AA.
AC B3EWY1; K7WHX1; K7WPN2;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 2.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Potassium channel toxin alpha-KTx 16.7;
DE AltName: Full=Alpha-KTx 16.5;
DE AltName: Full=MegKTx3 {ECO:0000303|PubMed:23142506};
DE Flags: Precursor;
OS Mesobuthus gibbosus (Mediterranean checkered scorpion) (Buthus gibbosus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX NCBI_TaxID=123226;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-59, FUNCTION, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom {ECO:0000269|PubMed:23142506}, and Venom gland;
RX PubMed=23142506; DOI=10.1016/j.toxicon.2012.10.010;
RA Diego-Garcia E., Peigneur S., Debaveye S., Gheldof E., Tytgat J.,
RA Caliskan F.;
RT "Novel potassium channel blocker venom peptides from Mesobuthus gibbosus
RT (Scorpiones: Buthidae).";
RL Toxicon 61:72-82(2013).
CC -!- FUNCTION: May play a role in blocking voltage-gated potassium channels
CC Kv1.2/KCNA2, and Kv1.3/KCNA3. Blocks the voltage-gated potassium
CC channel Kv1.3/KCNA3, with an IC(50) of 118.3 +-55.8 nM.
CC {ECO:0000269|PubMed:23142506}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23142506}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:23142506}.
CC -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=4066.6; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:23142506};
CC -!- MISCELLANEOUS: Has no effect on rat Kv1.2/KCNA2 channel.
CC {ECO:0000305|PubMed:23142506}.
CC -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC channel inhibitor family. Alpha-KTx 16 subfamily. {ECO:0000255}.
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DR EMBL; JX025013; AFX61609.1; -; mRNA.
DR EMBL; JX025014; AFX61610.1; -; mRNA.
DR AlphaFoldDB; B3EWY1; -.
DR SMR; B3EWY1; -.
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 Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW Voltage-gated potassium channel impairing toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:23142506"
FT PEPTIDE 23..59
FT /note="Potassium channel toxin alpha-KTx 16.7"
FT /id="PRO_0000421235"
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"
FT CONFLICT 21
FT /note="E -> K (in Ref. 1; AFX61610)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 59 AA; 6402 MW; 60CD0E046C277553 CRC64;
MKILSILLIA LVICSISICT EAFGLIDVKC SASRECWVAC KKVTGSGQGK CQNNQCRCY
