TX3_THEBL
ID TX3_THEBL Reviewed; 35 AA.
AC P83747;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Kappa-theraphotoxin-Tb1c {ECO:0000305};
DE Short=Kappa-TRTX-Tb1c {ECO:0000305};
DE AltName: Full=Theraphotoxin-3 {ECO:0000305};
DE AltName: Full=TlTx3 {ECO:0000303|PubMed:15150824, ECO:0000303|PubMed:15208026};
OS Theraphosa blondi (Goliath birdeating spider).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Mygalomorphae; Theraphosidae; Theraphosa.
OX NCBI_TaxID=260533 {ECO:0000305};
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=15150824; DOI=10.1002/rcm.1442;
RA Legros C., Celerier M.-L., Henry M., Guette C.;
RT "Nanospray analysis of the venom of the tarantula Theraphosa leblondi: a
RT powerful method for direct venom mass fingerprinting and toxin
RT sequencing.";
RL Rapid Commun. Mass Spectrom. 18:1024-1032(2004).
RN [2]
RP MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=15208026; DOI=10.1016/j.toxicon.2003.12.012;
RA Ebbinghaus J., Legros C., Nolting A., Guette C., Celerier M.L., Pongs O.,
RA Bahring R.;
RT "Modulation of Kv4.2 channels by a peptide isolated from the venom of the
RT giant bird-eating tarantula Theraphosa leblondi.";
RL Toxicon 43:923-932(2004).
CC -!- FUNCTION: Blocks Kv4.2/KCND2 voltage-gated potassium channels probably
CC by shifting the voltage-dependence of channel activation to more
CC depolarized potentials and by binding to the S3-S4 linker region of the
CC voltage sensor domain. {ECO:0000269|PubMed:15150824}.
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15150824,
CC ECO:0000269|PubMed:15208026}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:15150824, ECO:0000305|PubMed:15208026}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000250|UniProtKB:P58426}.
CC -!- MASS SPECTROMETRY: Mass=4208.78; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15150824};
CC -!- MASS SPECTROMETRY: Mass=4205.88; Method=MALDI; Note=Monoisotopic mass.;
CC Evidence={ECO:0000269|PubMed:15208026};
CC -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 59 (Tltx)
CC subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P83747; -.
DR SMR; P83747; -.
DR ArachnoServer; AS000277; kappa-theraphotoxin-Tb1c.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR011696; Huwentoxin-1.
DR Pfam; PF07740; Toxin_12; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Knottin; Neurotoxin; Potassium channel impairing toxin; Secreted; Toxin;
KW Voltage-gated potassium channel impairing toxin.
FT PEPTIDE 1..35
FT /note="Kappa-theraphotoxin-Tb1c"
FT /evidence="ECO:0000269|PubMed:15150824"
FT /id="PRO_0000045028"
FT DISULFID 3..18
FT /evidence="ECO:0000250|UniProtKB:P58426"
FT DISULFID 10..23
FT /evidence="ECO:0000250|UniProtKB:P58426"
FT DISULFID 17..30
FT /evidence="ECO:0000250|UniProtKB:P58426"
SQ SEQUENCE 35 AA; 4200 MW; 2DDC9DD502A0BB16 CRC64;
DDCLGMFSSC DPNNDKCCPN RVCRVRDQWC KYKLW
