ID   TXR7_MACRV              Reviewed;          78 AA.
AC   P0DL75;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2017, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=RTX-VII {ECO:0000303|PubMed:25784299};
DE   AltName: Full=Alpha-hexatoxin-MrVII {ECO:0000303|PubMed:25784299};
DE   Flags: Precursor;
OS   Macrothele raveni (Funnel-web spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Macrothelidae; Macrothele.
OX   NCBI_TaxID=269627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY,
RP   AMIDATION AT ARG-76, SUBCELLULAR LOCATION, FUNCTION, AND BIOASSAY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=25784299; DOI=10.1038/srep09241;
RA   Tang C., Zhou X., Zhang Y., Xiao Z., Hu Z., Zhang C., Huang Y., Chen B.,
RA   Liu Z., Liang S.;
RT   "Synergetic action of domain II and IV underlies persistent current
RT   generation in Nav1.3 as revealed by a tarantula toxin.";
RL   Sci. Rep. 5:9241-9241(2015).
CC   -!- FUNCTION: Agonist of rat Nav1.3/SCN3A. This toxin increases the peak
CC       current amplitude, and potently inhibits the fast inactivation of the
CC       channel (EC(50)=120 nM). The inhibition of fast inactivation is
CC       voltage-independent (depolarizing voltages ranging from 220 mV to 130
CC       mV). The toxin might bind to the domain IV of the Nav1.3 channel, while
CC       domain II might not participate in interacting with the toxin but could
CC       determine the efficacy of RTX-VII. In vivo, when
CC       intracerebroventricularly injected into mice, the toxin causes
CC       involuntary body twitching (seizure-like symptoms).
CC       {ECO:0000269|PubMed:25784299}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25784299}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:25784299}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000305|PubMed:25784299}.
CC   -!- MASS SPECTROMETRY: Mass=4064.71; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:25784299};
CC   -!- SIMILARITY: Belongs to the rTX family.
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DR   AlphaFoldDB; P0DL75; -.
DR   SMR; P0DL75; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Secreted; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..40
FT                   /evidence="ECO:0000269|PubMed:25784299"
FT                   /id="PRO_0000441927"
FT   CHAIN           41..76
FT                   /note="RTX-VII"
FT                   /evidence="ECO:0000269|PubMed:25784299"
FT                   /id="PRO_0000441928"
FT   MOD_RES         76
FT                   /note="Arginine amide"
FT                   /evidence="ECO:0000305|PubMed:25784299"
FT   DISULFID        42..58
FT                   /evidence="ECO:0000305|PubMed:25784299"
FT   DISULFID        47..63
FT                   /evidence="ECO:0000305|PubMed:25784299"
FT   DISULFID        57..73
FT                   /evidence="ECO:0000305|PubMed:25784299"
FT   DISULFID        65..71
FT                   /evidence="ECO:0000305|PubMed:25784299"
SQ   SEQUENCE   78 AA;  8712 MW;  CD2E2273BC527B10 CRC64;
     MKTIVYLIVS ILLLSSTVLV LAEGNAASHE LQEYPIEEQR KCVDGSCDPY SSDAPPCCDN
     QICQCIFFVP CYCKYRGK