ID   HTX2_CYRLI              Reviewed;          33 AA.
AC   B3EWN3;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Beta/kappa-theraphotoxin-Hlv1a;
DE            Short=Beta/kappa-TRTX-Hlv1a;
DE   AltName: Full=Beta/kappa-theraphotoxin-Hl2a {ECO:0000303|Ref.1};
DE            Short=Beta/kappa-TRTX-Hl2a {ECO:0000303|Ref.1};
DE   AltName: Full=Haplotoxin-2 {ECO:0000303|Ref.1};
OS   Cyriopagopus lividus (Cobalt blue tarantula) (Haplopelma lividum).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Theraphosidae; Haplopelma.
OX   NCBI_TaxID=1184493;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, AND AMIDATION AT ILE-33.
RC   TISSUE=Venom;
RA   Meir A., Cherki R.S., Kolb E., Langut Y., Bajayo N.;
RT   "Novel peptides isolated from spider venom, and uses thereof.";
RL   Submitted (MAY-2012) to UniProtKB.
CC   -!- FUNCTION: Spider venom neurotoxin that blocks voltage-gated sodium
CC       channel Nav1.3/SCN3A in human (IC(50)=80 nM) and rat (IC(50)=160 nM).
CC       Partially inhibits human Kv11.1/KCNH2/ERG (25% at 175 uM).
CC       {ECO:0000269|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:D2Y1X6}.
CC   -!- MASS SPECTROMETRY: Mass=3705.6; Method=MALDI;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- MISCELLANEOUS: Has no effect on human and rat Nav1.8/SCN10A (Ref.1).
CC   -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 11
CC       (haplotoxin-2) subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; B3EWN3; -.
DR   SMR; B3EWN3; -.
DR   ArachnoServer; AS001561; beta/kappa-theraphotoxin-Hlv1a.
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:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011696; Huwentoxin-1.
DR   InterPro; IPR013140; Huwentoxin_CS1.
DR   Pfam; PF07740; Toxin_12; 1.
DR   PROSITE; PS60021; HWTX_1; 1.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Neurotoxin;
KW   Potassium channel impairing toxin; Secreted; Toxin;
KW   Voltage-gated potassium channel impairing toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..33
FT                   /note="Beta/kappa-theraphotoxin-Hlv1a"
FT                   /id="PRO_0000419140"
FT   MOD_RES         33
FT                   /note="Isoleucine amide"
FT                   /evidence="ECO:0000269|Ref.1"
FT   DISULFID        2..17
FT                   /evidence="ECO:0000250|UniProtKB:D2Y1X6"
FT   DISULFID        9..22
FT                   /evidence="ECO:0000250|UniProtKB:D2Y1X6"
FT   DISULFID        16..29
FT                   /evidence="ECO:0000250|UniProtKB:D2Y1X6"
SQ   SEQUENCE   33 AA;  3715 MW;  1BB8E0D6920E5711 CRC64;
     ACKGLFVTCT PGKDECCPNH VCSSKHKWCK YKI