ID   TXDF1_DAFVA             Reviewed;          34 AA.
AC   P0DPC2;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2017, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Mu-theraphotoxin-Df1a {ECO:0000303|PubMed:28542706};
DE            Short=Mu-TRTX-Df1a {ECO:0000303|PubMed:28542706};
OS   Davus fasciatus (Costa Rican tiger rump) (Cyclosternum fasciatus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Theraphosidae; Davus.
OX   NCBI_TaxID=2024242;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   AMIDATION AT PHE-34.
RX   PubMed=28542706; DOI=10.1111/bph.13865;
RA   Cardoso F.C., Dekan Z., Smith J.J., Deuis J.R., Vetter I., Herzig V.,
RA   Alewood P.F., King G.F., Lewis R.J.;
RT   "Modulatory features of the novel spider toxin mu-TRTX-Df1a isolated from
RT   the venom of the spider Davus fasciatus.";
RL   Br. J. Pharmacol. 174:2528-2544(2017).
CC   -!- FUNCTION: Inhibits sodium channel Nav1.7/SCN9A with high potency
CC       (IC(50)=117 nM) and Nav1.2/SCN2A, Nav1.3/SCN3A, Nav1.6/SCN8A and
CC       Nav1.5/SCN5 with weaker potency. Also inhibits voltage-gated calcium
CC       channel Cav3.1/CACNA1G, Cav3.2/CACNA1H and Cav3.3/CACNA1I.
CC       {ECO:0000269|PubMed:28542706}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28542706}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:28542706}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P83480}.
CC   -!- PTM: C-terminal amidation is important for the high potency of the
CC       toxin. {ECO:0000269|PubMed:28542706}.
CC   -!- MASS SPECTROMETRY: Mass=4075.8; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:28542706};
CC   -!- MISCELLANEOUS: Does not show activity on voltage-gated potassium
CC       channels (Kv). {ECO:0000269|PubMed:28542706}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 54 (ProTx-1)
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DPC2; -.
DR   SMR; P0DPC2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019855; F:calcium channel inhibitor activity; 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; Calcium channel impairing toxin; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Knottin; Secreted; Toxin;
KW   Voltage-gated calcium channel impairing toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..34
FT                   /note="Mu-theraphotoxin-Df1a"
FT                   /evidence="ECO:0000269|PubMed:28542706"
FT                   /id="PRO_0000442773"
FT   MOD_RES         34
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:28542706"
FT   DISULFID        2..16
FT                   /evidence="ECO:0000250|UniProtKB:P83476"
FT   DISULFID        9..21
FT                   /evidence="ECO:0000250|UniProtKB:P83476"
FT   DISULFID        15..28
FT                   /evidence="ECO:0000250|UniProtKB:P83476"
SQ   SEQUENCE   34 AA;  4086 MW;  EADD3BA74415BAA8 CRC64;
     ECRWFLGGCS GGQTCCEHLV CHRKHQWCVW DWSF