ID   KAX6C_ANUPH             Reviewed;          35 AA.
AC   P0C166;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Potassium channel toxin alpha-KTx 6.12 {ECO:0000303|PubMed:15615696};
DE   AltName: Full=Anuroctoxin {ECO:0000303|PubMed:15615696};
OS   Anuroctonus phaiodactylus (Mafia scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Chactoidea; Chactidae; Uroctoninae; Anuroctonus.
OX   NCBI_TaxID=246982;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, DISULFIDE BONDS, PYROGLUTAMATE
RP   FORMATION AT GLN-1, AMIDATION AT LYS-35, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=15615696; DOI=10.1124/mol.104.007187;
RA   Bagdany M., Batista C.V.F., Valdez-Cruz N.A., Somodi S.,
RA   Rodriguez de la Vega R.C., Licea A.F., Varga Z., Gaspar R., Possani L.D.,
RA   Panyi G.;
RT   "Anuroctoxin, a new scorpion toxin of the Alpha-KTx 06 subfamily, is highly
RT   selective for Kv1.3 over IKCa1 ion channels of human T lymphocytes.";
RL   Mol. Pharmacol. 67:1034-1044(2005).
CC   -!- FUNCTION: High affinity blocker of Kv1.3/KCNA3 channels of human T
CC       cells. Blocks Kv1.2/KCNA2 with an order of magnitude smaller than for
CC       Kv1.3/KCNA3. {ECO:0000269|PubMed:15615696}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15615696}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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=4082.8; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15615696};
CC   -!- MISCELLANEOUS: This toxin does not block the calcium-activated
CC       KCa3.1/KCNN4 potassium channels, Shaker IR, Kv1.1/KCNA1, and
CC       Kv2.1/KCNB1 potassium channels. {ECO:0000305|PubMed:15615696}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 06 subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C166; -.
DR   SMR; P0C166; -.
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   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS01138; SCORP_SHORT_TOXIN; 1.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW   Pyrrolidone carboxylic acid; Secreted; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   CHAIN           1..35
FT                   /note="Potassium channel toxin alpha-KTx 6.12"
FT                   /id="PRO_0000226963"
FT   SITE            23
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
FT   SITE            32
FT                   /note="Aromatic residue of the functional dyad"
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:15615696"
FT   MOD_RES         35
FT                   /note="Lysine amide"
FT                   /evidence="ECO:0000269|PubMed:15615696"
FT   DISULFID        4..24
FT                   /evidence="ECO:0000269|PubMed:15615696"
FT   DISULFID        10..29
FT                   /evidence="ECO:0000269|PubMed:15615696"
FT   DISULFID        14..31
FT                   /evidence="ECO:0000269|PubMed:15615696"
FT   DISULFID        19..34
FT                   /evidence="ECO:0000269|PubMed:15615696"
SQ   SEQUENCE   35 AA;  4109 MW;  B9B8E9CD7E4DA845 CRC64;
     QKECTGPQHC TNFCRKNKCT HGKCMNRKCK CFNCK