KA142_MESMA
ID KA142_MESMA Reviewed; 54 AA.
AC Q95NK7; Q549F2;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Potassium channel toxin alpha-KTx 14.2;
DE AltName: Full=BmKK2;
DE AltName: Full=BmTXKS3;
DE AltName: Full=KK1;
DE AltName: Full=Neurotoxin BmP07;
DE AltName: Full=Potassium ion channel blocker P07;
DE AltName: Full=Toxin Kk2;
DE Contains:
DE RecName: Full=BmKK2-b;
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 [GENOMIC DNA / MRNA].
RC TISSUE=Venom gland;
RX PubMed=11698110; DOI=10.1016/s0300-9084(01)01326-8;
RA Zeng X.-C., Peng F., Luo F., Zhu S.-Y., Liu H., Li W.-X.;
RT "Molecular cloning and characterization of four scorpion K(+)-toxin-like
RT peptides: a new subfamily of venom peptides (alpha-KTx14) and genomic
RT analysis of a member.";
RL Biochimie 83:883-889(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=11923087; DOI=10.1016/s1096-4959(02)00020-9;
RA Zhu S.-Y., Li W.-X.;
RT "Precursors of three unique cysteine-rich peptides from the scorpion Buthus
RT martensii Karsch.";
RL Comp. Biochem. Physiol. 131B:749-756(2002).
RN [3]
RP PROTEIN SEQUENCE OF 24-54, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=15208022; DOI=10.1016/j.toxicon.2003.11.028;
RA Li M.H., Zhang N.X., Chen X.Q., Wu G., Wu H., Hu G.Y.;
RT "Purification and pharmacological characterization of BmKK2 (alpha-KTx
RT 14.2), a novel potassium channel-blocking peptide, from the venom of Asian
RT scorpion Buthus martensi Karsch.";
RL Toxicon 43:895-900(2004).
RN [4]
RP PROTEIN SEQUENCE OF 26-29, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=22887697; DOI=10.1002/pmic.201200224;
RA Xu J., Zhang X., Guo Z., Yan J., Yu L., Li X., Xue X., Liang X.;
RT "Short-chain peptides identification of scorpion Buthus martensi Karsch
RT venom by employing high orthogonal 2D-HPLC system and tandem mass
RT spectrometry.";
RL Proteomics 12:3076-3084(2012).
RN [5]
RP STRUCTURE BY NMR OF 24-54, FUNCTION, AND DISULFIDE BONDS.
RX PubMed=15146482; DOI=10.1002/prot.20117;
RA Zhang N., Li M., Chen X., Wang Y., Wu G., Hu G., Wu H.;
RT "Solution structure of BmKK2, a new potassium channel blocker from the
RT venom of Chinese scorpion Buthus martensi Karsch.";
RL Proteins 55:835-845(2004).
CC -!- FUNCTION: Inhibits potassium channels. May be active towards small
CC conductance calcium-activated potassium channels (KCNN, SK), and less
CC active towards voltage-gated potassium channels (Kv/KCN).
CC {ECO:0000269|PubMed:15146482, ECO:0000269|PubMed:15208022}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22887697}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:22887697}.
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:15146482}.
CC -!- MASS SPECTROMETRY: [Potassium channel toxin alpha-KTx 14.2]:
CC Mass=3240.5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15208022};
CC -!- MASS SPECTROMETRY: [BmKK2-b]: Mass=3042.79; Method=Electrospray;
CC Note=Monoisotopic mass.; Evidence={ECO:0000269|PubMed:22887697};
CC -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC channel inhibitor family. Alpha-KTx 14 subfamily. {ECO:0000305}.
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DR EMBL; AJ277727; CAC38036.1; -; mRNA.
DR EMBL; AJ277730; CAC38039.1; -; Genomic_DNA.
DR EMBL; AF159975; AAK61822.1; -; mRNA.
DR EMBL; AF135817; AAQ13566.1; -; mRNA.
DR PDB; 1PVZ; NMR; -; A=24-54.
DR PDBsum; 1PVZ; -.
DR AlphaFoldDB; Q95NK7; -.
DR SMR; Q95NK7; -.
DR EvolutionaryTrace; Q95NK7; -.
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; IPR036574; Scorpion_toxin-like_sf.
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;
KW Voltage-gated potassium channel impairing toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:15208022"
FT CHAIN 24..54
FT /note="Potassium channel toxin alpha-KTx 14.2"
FT /evidence="ECO:0000269|PubMed:15208022"
FT /id="PRO_0000035334"
FT PEPTIDE 26..54
FT /note="BmKK2-b"
FT /id="PRO_0000431602"
FT DISULFID 30..46
FT /evidence="ECO:0000269|PubMed:15146482"
FT DISULFID 36..51
FT /evidence="ECO:0000269|PubMed:15146482"
FT DISULFID 40..53
FT /evidence="ECO:0000269|PubMed:15146482"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:1PVZ"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:1PVZ"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:1PVZ"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1PVZ"
SQ SEQUENCE 54 AA; 5786 MW; AF59694FDDDDC5C1 CRC64;
MKIFFAILLI LAVCSMAIWT VNGTPFAIKC ATDADCSRKC PGNPPCRNGF CACT
