KAX91_MESMA
ID KAX91_MESMA Reviewed; 56 AA.
AC Q9NJP7; P58491;
DT 19-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Potassium channel toxin alpha-KTx 9.1 {ECO:0000305};
DE AltName: Full=BmKK6 {ECO:0000312|EMBL:AAP43906.1};
DE Short=Toxin Kk6 {ECO:0000312|EMBL:AAP43906.1};
DE AltName: Full=Neurotoxin BmP02 {ECO:0000303|PubMed:10471839, ECO:0000303|PubMed:11076505, ECO:0000303|PubMed:22511981, ECO:0000303|PubMed:9151979};
DE Flags: Precursor;
OS Mesobuthus martensii (Manchurian scorpion) (Buthus martensii).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX NCBI_TaxID=34649;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=10471839; DOI=10.1016/s0014-5793(99)01101-1;
RA Zhu S.-Y., Li W.-X., Zeng X.-C., Jiang D.-H., Mao X., Liu H.;
RT "Molecular cloning and sequencing of two 'short chain' and two 'long chain'
RT K(+) channel-blocking peptides from the Chinese scorpion Buthus martensii
RT Karsch.";
RL FEBS Lett. 457:509-514(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Li W.-X., Zeng X.-C., Zhu S.-Y.;
RT "Precursor of a potassium-channel inhibitor [named BmKK6] from scorpion
RT Buthus martensii Karsch which is highly homologous with Leiuropeptide I.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 29-56, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RX PubMed=9151979; DOI=10.1111/j.1432-1033.1997.00457.x;
RA Romi-Lebrun R., Martin-Eauclaire M.-F., Escoubas P., Wu F.Q., Lebrun B.,
RA Hisada M., Nakajima T.;
RT "Characterization of four toxins from Buthus martensi scorpion venom, which
RT act on apamin-sensitive Ca2+-activated K+ channels.";
RL Eur. J. Biochem. 245:457-464(1997).
RN [4]
RP FUNCTION ON KV7.1/KCNQ1 CHANNELS.
RC TISSUE=Venom gland;
RX PubMed=22511981; DOI=10.1371/journal.pone.0035154;
RA Chen Z.Y., Zeng D.Y., Hu Y.T., He Y.W., Pan N., Ding J.P., Cao Z.J.,
RA Liu M.L., Li W.X., Yi H., Jiang L., Wu Y.L.;
RT "Structural and functional diversity of acidic scorpion potassium channel
RT toxins.";
RL PLoS ONE 7:E35154-E35154(2012).
RN [5]
RP STRUCTURE BY NMR OF 29-56, AND DISULFIDE BONDS.
RX PubMed=11076505; DOI=10.1021/bi000860s;
RA Xu Y.-Q., Wu J.-H., Pei J.-M., Shi Y.-Y., Ji Y.-H., Tong Q.-C.;
RT "Solution structure of BmP02, a new potassium channel blocker from the
RT venom of the Chinese scorpion Buthus martensi Karsch.";
RL Biochemistry 39:13669-13675(2000).
CC -!- FUNCTION: Blocks small conductance calcium-activated potassium channels
CC (KCNN, SK). Weakly inhibits the Kv7.1/KCNQ1 channel (10 uM of the toxin
CC inhibits currents by 23.3%). Low toxicity by intracerebroventricular
CC injection into mice. {ECO:0000269|PubMed:22511981}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9151979}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:9151979}.
CC -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC beta-sheet by disulfide bonds (CSalpha/beta).
CC {ECO:0000269|PubMed:11076505}.
CC -!- MASS SPECTROMETRY: Mass=2950.72; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9151979};
CC -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC channel inhibitor family. Alpha-KTx 09 subfamily. {ECO:0000305}.
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DR EMBL; AF132975; AAF31296.1; -; mRNA.
DR EMBL; AF154633; AAP43906.1; -; mRNA.
DR PDB; 1DU9; NMR; -; A=29-56.
DR PDBsum; 1DU9; -.
DR AlphaFoldDB; Q9NJP7; -.
DR BMRB; Q9NJP7; -.
DR SMR; Q9NJP7; -.
DR EvolutionaryTrace; Q9NJP7; -.
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 InterPro; IPR036574; Scorpion_toxin-like_sf.
DR InterPro; IPR008911; Toxin_alpha-KTx_8/9.
DR Pfam; PF05453; Toxin_6; 1.
DR SUPFAM; SSF57095; SSF57095; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium-activated potassium channel impairing toxin;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Potassium channel impairing toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:9151979"
FT PEPTIDE 29..56
FT /note="Potassium channel toxin alpha-KTx 9.1"
FT /evidence="ECO:0000269|PubMed:9151979"
FT /id="PRO_0000035349"
FT DISULFID 31..47
FT /evidence="ECO:0000269|PubMed:11076505,
FT ECO:0000312|PDB:1DU9"
FT DISULFID 34..52
FT /evidence="ECO:0000269|PubMed:11076505,
FT ECO:0000312|PDB:1DU9"
FT DISULFID 38..54
FT /evidence="ECO:0000269|PubMed:11076505,
FT ECO:0000312|PDB:1DU9"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:1DU9"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:1DU9"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:1DU9"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1DU9"
SQ SEQUENCE 56 AA; 6015 MW; 70953032042F8672 CRC64;
MSRLFTLVLI VLAMNVMMAI ISDPVVEAVG CEECPMHCKG KNAKPTCDDG VCNCNV
