ID   TO1C_ATRRO              Reviewed;          78 AA.
AC   A5A3H2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Omega-hexatoxin-Ar1c;
DE            Short=Omega-HXTX-Ar1c;
DE   AltName: Full=Omega-atracotoxin-Ar1c;
DE            Short=Omega-ACTX-Ar1c;
DE   Flags: Precursor;
OS   Atrax robustus (Sydney funnel-web spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Hexathelidae; Atrax.
OX   NCBI_TaxID=6903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=XenFW137; TISSUE=Venom gland;
RA   Sollod B.L., Wilson D.T., Drinkwater R.D., King G.F.;
RT   "The omega-atracotoxins: selective blockers of insect M-LVA and HVA calcium
RT   channels.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Insecticidal toxin that reversibly and voltage-independently
CC       blocks both mid-low- (M-LVA) and high-voltage-activated (HVA) calcium
CC       channels (Cav) in cockroach DUM neurons. Also causes a modest block of
CC       insect sodium channel currents (Nav). Induces potent excitatory
CC       symptoms, followed by flaccid paralysis leading to death in house
CC       crickets (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- MISCELLANEOUS: This toxin comes from a male specimen. It is observed
CC       that propeptide sequences coming from male specimen are identical but
CC       have only limited homology with the female paralogs, but the reason is
CC       unknown.
CC   -!- SIMILARITY: Belongs to the neurotoxin 08 (Shiva) family. 01 (omega
CC       toxin) subfamily. {ECO:0000305}.
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DR   EMBL; EF523496; ABP63655.1; -; mRNA.
DR   AlphaFoldDB; A5A3H2; -.
DR   SMR; A5A3H2; -.
DR   ArachnoServer; AS000022; omega-hexatoxin-Ar1c.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019855; F:calcium 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   GO; GO:0006952; P:defense response; IEA:InterPro.
DR   InterPro; IPR009415; Omega-atracotox.
DR   InterPro; IPR018071; Omega-atracotox_CS.
DR   Pfam; PF06357; Omega-toxin; 1.
DR   PROSITE; PS60016; OMEGA_ACTX_1; 1.
PE   2: Evidence at transcript level;
KW   Calcium channel impairing toxin; Cleavage on pair of basic residues;
KW   Disulfide bond; Ion channel impairing toxin; Knottin; Neurotoxin; Secreted;
KW   Signal; Toxin; Voltage-gated calcium channel impairing toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..41
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000379910"
FT   PEPTIDE         42..78
FT                   /note="Omega-hexatoxin-Ar1c"
FT                   /id="PRO_0000379911"
FT   SITE            51
FT                   /note="Critical for insecticidal activity"
FT                   /evidence="ECO:0000250"
FT   SITE            68
FT                   /note="Critical for insecticidal activity"
FT                   /evidence="ECO:0000250"
FT   SITE            76
FT                   /note="Critical for insecticidal activity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        45..59
FT                   /evidence="ECO:0000250"
FT   DISULFID        52..63
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   78 AA;  8415 MW;  1D423E10B18C7C5B CRC64;
     MNTATGVIAL LVLATVIGCI EAEDTRADLQ GGEAAEKVFR RSPTCIPSGQ PCPYNENYCS
     QSCTFKENEN ANTVKRCD