ID   KA17C_MESMA             Reviewed;          31 AA.
AC   P0DMR8;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   04-FEB-2015, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Toxin BmKK12;
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   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, MASS SPECTROMETRY, PYROGLUTAMATE
RP   FORMATION AT GLN-1, AND AMIDATION AT PRO-31.
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).
CC   -!- FUNCTION: Blocker of potassium channels (Kv).
CC       {ECO:0000250|UniProtKB:Q95NJ8}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22887697}.
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:Q95NJ8}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:22887697}.
CC   -!- MASS SPECTROMETRY: Mass=3657.23; Method=Electrospray; Note=Monoisotopic
CC       mass.; Evidence={ECO:0000269|PubMed:22887697};
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 17 subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P0DMR8; -.
DR   SMR; P0DMR8; -.
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.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Potassium channel impairing toxin;
KW   Pyrrolidone carboxylic acid; Secreted; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   CHAIN           1..31
FT                   /note="Toxin BmKK12"
FT                   /id="PRO_0000431729"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:22887697"
FT   MOD_RES         31
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000269|PubMed:22887697"
FT   DISULFID        4..20
FT                   /evidence="ECO:0000250|UniProtKB:Q95NJ8"
FT   DISULFID        10..25
FT                   /evidence="ECO:0000250|UniProtKB:Q95NJ8"
FT   DISULFID        14..27
FT                   /evidence="ECO:0000250|UniProtKB:Q95NJ8"
SQ   SEQUENCE   31 AA;  3683 MW;  692BEC55166AB1B6 CRC64;
     QRQCQNVQNC YKYCMSPKKC EYGTCYCEPS P