ID   TK1E_HADVE              Reviewed;          74 AA.
AC   S0F1M9;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Lambda-hexatoxin-Hv1e {ECO:0000305};
DE            Short=Lambda-HXTX-Hv1e {ECO:0000305};
DE   AltName: Full=Kappa-hexatoxin-Hv1e {ECO:0000303|PubMed:24593665};
DE   Flags: Precursor;
OS   Hadronyche versuta (Blue mountains funnel-web spider) (Atrax versutus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Hexathelidae; Hadronyche.
OX   NCBI_TaxID=6904;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=24593665; DOI=10.1186/1471-2164-15-177;
RA   Pineda S.S., Sollod B.L., Wilson D., Darling A., Sunagar K., Undheim E.A.,
RA   Kely L., Antunes A., Fry B.G., King G.F.;
RT   "Diversification of a single ancestral gene into a successful toxin
RT   superfamily in highly venomous Australian funnel-web spiders.";
RL   BMC Genomics 15:177-177(2014).
CC   -!- FUNCTION: This excitatory toxin inhibits insect calcium-activated
CC       potassium (KCa) channels (Slo-type). {ECO:0000250|UniProtKB:P82228}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P82228}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:24593665}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 11 (kappa toxin) family.
CC       {ECO:0000303|PubMed:24593665}.
CC   -!- CAUTION: This toxin has the prefix lambda in its name (instead of
CC       kappa), since lambda is the Greek letter attributed to calcium-
CC       activated potassium (KCa) channel impairing toxins (according to the
CC       nomenclature of King et al., 2008). {ECO:0000305}.
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DR   EMBL; HG001310; CDF44171.1; -; mRNA.
DR   AlphaFoldDB; S0F1M9; -.
DR   SMR; S0F1M9; -.
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; IPR012499; Toxin_16.
DR   Pfam; PF07945; Toxin_16; 1.
DR   PROSITE; PS60020; J_ACTX; 1.
PE   3: Inferred from homology;
KW   Calcium-activated potassium channel impairing toxin;
KW   Cleavage on pair of basic residues; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Neurotoxin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..35
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000430925"
FT   PEPTIDE         38..74
FT                   /note="Lambda-hexatoxin-Hv1e"
FT                   /id="PRO_0000430926"
FT   SITE            39
FT                   /note="Important for the neurotoxic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            45
FT                   /note="Critical for the neurotoxic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            46
FT                   /note="Critical for the neurotoxic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            50
FT                   /note="Critical for the neurotoxic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            51
FT                   /note="Critical for the neurotoxic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            66
FT                   /note="Important for the neurotoxic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            68
FT                   /note="Critical for the neurotoxic activity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        40..54
FT                   /evidence="ECO:0000250"
FT   DISULFID        47..59
FT                   /evidence="ECO:0000250"
FT   DISULFID        50..51
FT                   /evidence="ECO:0000250"
FT   DISULFID        53..69
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   74 AA;  7881 MW;  82E6725ACE541B1C CRC64;
     MNTATCFIVL LVVATVIGGI EAGEFDMRKD VMGLFRRAIC PGADRPCAAC CPCCPGTSCK
     AESNGVFYCR KDEP