TK1A_HADMO
ID TK1A_HADMO Reviewed; 73 AA.
AC P0DMQ4;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 23-FEB-2022, entry version 8.
DE RecName: Full=Lambda-hexatoxin-Hmo1d {ECO:0000305};
DE Short=Lambda-HXTX-Hmo1d {ECO:0000305};
DE AltName: Full=Kappa-hexatoxin-Hmo1d {ECO:0000303|PubMed:24593665};
DE Flags: Precursor;
OS Hadronyche modesta (Victorian funnel-web spider).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Mygalomorphae; Hexathelidae; Hadronyche.
OX NCBI_TaxID=1337084;
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 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.
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_0000430927"
FT PEPTIDE 38..73
FT /note="Lambda-hexatoxin-Hmo1d"
FT /id="PRO_0000430928"
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 69
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..70
FT /evidence="ECO:0000250"
SQ SEQUENCE 73 AA; 7672 MW; 7A87FDFB396271E0 CRC64;
MNTATGFIVL LVXATVIGGI EAGESDMRKD VMGLFRRTIC TGADRPCAAC CPCCPGTSCQ
GPESNXISYC RND
