ID   TK1A_HADVE              Reviewed;          36 AA.
AC   P82227;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   22-FEB-2023, entry version 61.
DE   RecName: Full=Lambda-hexatoxin-Hv1a {ECO:0000305};
DE            Short=Lambda-HXTX-Hv1a {ECO:0000305};
DE   AltName: Full=Janus-atracotoxin-Hv1a;
DE            Short=Janus-AcTx-Hv1a;
DE   AltName: Full=Kappa-atracotoxin-Hv1a;
DE            Short=Kappa-AcTx-Hv1a;
DE   AltName: Full=Kappa-hexatoxin-Hv1a {ECO:0000305};
DE            Short=Kappa-HXTX-Hv1a {ECO:0000305};
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   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=10881200; DOI=10.1038/75921;
RA   Wang X.-H., Connor M., Smith R., Maciejewski M.W., Howden M.E.H.,
RA   Nicholson G.M., Christie M.J., King G.F.;
RT   "Discovery and characterization of a family of insecticidal neurotoxins
RT   with a rare vicinal disulfide bridge.";
RL   Nat. Struct. Biol. 7:505-513(2000).
CC   -!- FUNCTION: This excitatory toxin inhibits insect calcium-activated
CC       potassium (KCa) channels (Slo-type). {ECO:0000250|UniProtKB:P82228}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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:0000305}.
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}.
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; P82227; -.
DR   SMR; P82227; -.
DR   ArachnoServer; AS000172; kappa-hexatoxin-Hv1a.
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   SUPFAM; SSF57059; omega toxin-like; 1.
DR   PROSITE; PS60020; J_ACTX; 1.
PE   1: Evidence at protein level;
KW   Calcium-activated potassium channel impairing toxin;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Knottin; Neurotoxin; Potassium channel impairing toxin; Secreted; Toxin.
FT   PEPTIDE         1..36
FT                   /note="Lambda-hexatoxin-Hv1a"
FT                   /id="PRO_0000044996"
FT   SITE            2
FT                   /note="Important for the neurotoxic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            8
FT                   /note="Critical for the neurotoxic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            9
FT                   /note="Critical for the neurotoxic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            13
FT                   /note="Critical for the neurotoxic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            14
FT                   /note="Critical for the neurotoxic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            30
FT                   /note="Important for the neurotoxic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            32
FT                   /note="Critical for the neurotoxic activity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        3..17
FT                   /evidence="ECO:0000250"
FT   DISULFID        10..22
FT                   /evidence="ECO:0000250"
FT   DISULFID        13..14
FT                   /evidence="ECO:0000250"
FT   DISULFID        16..33
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   36 AA;  3685 MW;  D1598B2560BFE997 CRC64;
     TICTGADRPC AACCPCCPGT SCQGPESNGV VYCRNF
//