TX15_PARSR
ID TX15_PARSR Reviewed; 34 AA.
AC P0DL73;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2017, sequence version 1.
DT 25-MAY-2022, entry version 11.
DE RecName: Full=Toxin GTx1-15 {ECO:0000303|PubMed:24211312};
DE AltName: Full=Beta/omega-theraphotoxin-Gr2a {ECO:0000305};
DE Short=Beta/omega-TRTX-Gr2a {ECO:0000305};
DE AltName: Full=Toxin GpTx-1 {ECO:0000250|UniProtKB:P0DL72};
OS Paraphysa scrofa (Chilean copper tarantula) (Phrixotrichus auratus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Mygalomorphae; Theraphosidae; Paraphysa.
OX NCBI_TaxID=269635;
RN [1]
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, SYNTHESIS, AMIDATION AT PHE-34, AND
RP MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=24211312; DOI=10.1016/j.toxicon.2013.10.029;
RA Cherki R.S., Kolb E., Langut Y., Tsveyer L., Bajayo N., Meir A.;
RT "Two tarantula venom peptides as potent and differential Na(V) channels
RT blockers.";
RL Toxicon 77:58-67(2014).
CC -!- FUNCTION: Potent voltage-gated sodium channel blocker
CC (PubMed:24211312). Potently inhibits the voltage-gated sodium channels
CC Nav1.7/SCN9A (IC(50)=0.58-10 nM) (PubMed:24211312) (By similarity).
CC Shows a moderate activity on Nav1.1/SCN1A (IC(50)=6 nM), Nav1.2/SCN2A
CC (IC(50)=5-128 nM), Nav1.3/SCN3A (IC(50)=20.3-170 nM), and Nav1.6/SCN8A
CC (IC(50)=17-20.1 nM) (PubMed:24211312) (By similarity). Shows an unclear
CC inhibition of Nav1.4/SCN4A (IC(50)=200 nM to >10 uM), Nav1.5/SCN5A
CC (IC(50)=140 nM to >10 uM) and Nav1.8/SCN10A (IC(50)=68-12200 nM)
CC (PubMed:24211312) (By similarity). Weakly blocks the low voltage-gated
CC calcium channels Cav3.1/CACNA1G (30% inhibition of the peak current by
CC 9.8 nM of the toxin) (By similarity). It shows moderate affinity for
CC lipid bilayers (By similarity). {ECO:0000250|UniProtKB:P0DJA9,
CC ECO:0000250|UniProtKB:P0DL72, ECO:0000269|PubMed:24211312}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24211312}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:24211312}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000250|UniProtKB:P0DL72}.
CC -!- DOMAIN: This toxin is amphipathic in nature with a hydrophobic face on
CC one side of the molecule (composed of residues 5-Phe-Met-6 and 27-His--
CC Phe-34) and a hydrophilic (mostly cationic) face on the opposite side
CC (composed of residues 10-Ile--Lys-15 and 18-Arg--Pro-19).
CC {ECO:0000250|UniProtKB:P0DL72}.
CC -!- MASS SPECTROMETRY: Mass=4070.8; Method=Electrospray; Note=Monoisotopic
CC mass.; Evidence={ECO:0000269|PubMed:24211312};
CC -!- MISCELLANEOUS: The primary structure of the mature peptide is identical
CC to that of Gtx1-15 from Grammostola rosea (AC P0DJA9) and GpTx-1 from
CC Grammostola porteri (AC P0DL72). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 08 (Gtx1-15)
CC subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DL73; -.
DR SMR; P0DL73; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
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.
PE 1: Evidence at protein level;
KW Amidation; Calcium channel impairing toxin; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin; Secreted; Toxin;
KW Voltage-gated calcium channel impairing toxin;
KW Voltage-gated sodium channel impairing toxin.
FT CHAIN 1..34
FT /note="Toxin GTx1-15"
FT /evidence="ECO:0000269|PubMed:24211312"
FT /id="PRO_0000441930"
FT MOD_RES 34
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:24211312"
FT DISULFID 2..17
FT /evidence="ECO:0000250|UniProtKB:P0DL72"
FT DISULFID 9..23
FT /evidence="ECO:0000250|UniProtKB:P0DL72"
FT DISULFID 16..30
FT /evidence="ECO:0000250|UniProtKB:P0DL72"
SQ SEQUENCE 34 AA; 4081 MW; DDEF29032F4A84E2 CRC64;
DCLGFMRKCI PDNDKCCRPN LVCSRTHKWC KYVF
