ID   TX1_POEVT               Reviewed;          36 AA.
AC   C0HLN4;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   02-DEC-2020, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=Beta/delta/mu-theraphotoxin-Pv1 {ECO:0000303|PubMed:32218140};
DE   AltName: Full=Beta/delta/mu-TRTX-Pv1 {ECO:0000303|PubMed:32218140};
DE   AltName: Full=Poecilotheriatoxin-1 {ECO:0000303|PubMed:32218140};
DE            Short=PcaTX-1 {ECO:0000303|PubMed:32218140};
OS   Poecilotheria vittata (Ghost ornamental tarantula).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Theraphosidae; Poecilotheria.
OX   NCBI_TaxID=2053141;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY,
RP   ISOMERIZATION, AND AMIDATION AT PHE-36.
RX   PubMed=32218140; DOI=10.3390/toxins12040207;
RA   Johnson S.R., Rikli H.G.;
RT   "Aspartic Acid Isomerization Characterized by High Definition Mass
RT   Spectrometry Significantly Alters the Bioactivity of a Novel Toxin from
RT   Poecilotheria.";
RL   Toxins 12:0-0(2020).
CC   -!- FUNCTION: Gating-modifier toxin that targets voltage-gated sodium
CC       channels. Inhibits the inactivation of Nav1.7/SCN9A.
CC       {ECO:0000269|PubMed:32218140}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32218140}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:32218140}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P0DM12}.
CC   -!- MASS SPECTROMETRY: Mass=4024.71; Mass_error=0.005; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:32218140};
CC   -!- MISCELLANEOUS: Exists in two forms, due to cis-trans isomerization at
CC       33-Asp-Gly-34. The cis isomer also acts by shifting activation of the
CC       Nav1.7/SCN9A channel to more depolarized voltages.
CC       {ECO:0000269|PubMed:32218140}.
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DR   AlphaFoldDB; C0HLN4; -.
DR   SMR; C0HLN4; -.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR   InterPro; IPR011696; Huwentoxin-1.
DR   Pfam; PF07740; Toxin_12; 1.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   PEPTIDE         1..36
FT                   /note="Beta/delta/mu-theraphotoxin-Pv1"
FT                   /id="PRO_0000451742"
FT   MOD_RES         36
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:32218140"
FT   DISULFID        3..17
FT                   /evidence="ECO:0000250|UniProtKB:P0DM12"
FT   DISULFID        10..22
FT                   /evidence="ECO:0000250|UniProtKB:P0DM12"
FT   DISULFID        16..30
FT                   /evidence="ECO:0000250|UniProtKB:P0DM12"
SQ   SEQUENCE   36 AA;  4035 MW;  B71F000FD706557A CRC64;
     AGCKYLFGSC KEDSDCCKHL GCRRKAPQYC GWDGTF