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TK1A_HADFO
ID   TK1A_HADFO              Reviewed;          37 AA.
AC   P0C2L8;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Lambda-hexatoxin-Hf1a {ECO:0000305};
DE            Short=Lambda-HXTX-Hf1a {ECO:0000305};
DE   AltName: Full=Janus-atracotoxin-Hf1a;
DE            Short=Janus-AcTx-Hf1a;
DE   AltName: Full=Kappa-atracotoxin-Hf1a;
DE            Short=Kappa-AcTx-Hf1a;
DE   AltName: Full=Kappa-hexatoxin-Hf1a {ECO:0000305};
DE            Short=Kappa-HXTX-Hf1a {ECO:0000305};
OS   Hadronyche formidabilis (Northern tree funnel-web spider) (Atrax
OS   formidabilis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Hexathelidae; Hadronyche.
OX   NCBI_TaxID=426499;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Atkinson R.K., Howden M.E.H., Tyler M.I., Vonarx E.J.;
RT   "Insecticidal toxins derived from funnel web (Atrax or Hadronyche)
RT   spiders.";
RL   Patent number US5763568, 09-JUN-1998.
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}.
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DR   AlphaFoldDB; P0C2L8; -.
DR   SMR; P0C2L8; -.
DR   ArachnoServer; AS000171; kappa-hexatoxin-Hf1a.
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   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..37
FT                   /note="Lambda-hexatoxin-Hf1a"
FT                   /id="PRO_0000280461"
FT   SITE            9
FT                   /note="Critical for the neurotoxic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            10
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            15
FT                   /note="Critical for the neurotoxic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            31
FT                   /note="Important for the neurotoxic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            33
FT                   /note="Critical for the neurotoxic activity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        4..18
FT                   /evidence="ECO:0000250"
FT   DISULFID        11..23
FT                   /evidence="ECO:0000250"
FT   DISULFID        14..15
FT                   /evidence="ECO:0000250"
FT   DISULFID        17..34
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   37 AA;  3722 MW;  D23A54CDB0B48347 CRC64;
     SPTCTGADRP CAACCPCCPG TSCKGPEPNG VSYCRND
 
 
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