ID   TO1B_ATRRO              Reviewed;          73 AA.
AC   A5A3H1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Omega-hexatoxin-Ar1b;
DE            Short=Omega-HXTX-Ar1b;
DE   AltName: Full=Omega-atracotoxin-Ar1b;
DE            Short=Omega-ACTX-Ar1b;
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=XenFW208; TISSUE=Venom gland;
RX   PubMed=17610847; DOI=10.1016/j.bcp.2007.05.017;
RA   Chong Y., Hayes J.L., Sollod B., Wen S., Wilson D.T., Hains P.G.,
RA   Hodgson W.C., Broady K.W., King G.F., Nicholson G.M.;
RT   "The omega-atracotoxins: selective blockers of insect M-LVA and HVA calcium
RT   channels.";
RL   Biochem. Pharmacol. 74:623-638(2007).
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 female specimen. It is observed
CC       that propeptide sequences coming from female specimen have only limited
CC       homology with the male paralogs, but the reason is unknown.
CC   -!- SIMILARITY: Belongs to the neurotoxin 08 (Shiva) family. 01 (omega
CC       toxin) subfamily. {ECO:0000305}.
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DR   EMBL; EF523495; ABP63654.1; -; mRNA.
DR   AlphaFoldDB; A5A3H1; -.
DR   SMR; A5A3H1; -.
DR   ArachnoServer; AS000021; omega-hexatoxin-Ar1b.
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   Pfam; PF06357; Omega-toxin; 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..37
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000379908"
FT   PEPTIDE         38..73
FT                   /note="Omega-hexatoxin-Ar1b"
FT                   /id="PRO_0000379909"
FT   SITE            46
FT                   /note="Critical for insecticidal activity"
FT                   /evidence="ECO:0000250"
FT   SITE            63
FT                   /note="Critical for insecticidal activity"
FT                   /evidence="ECO:0000250"
FT   SITE            71
FT                   /note="Critical for insecticidal activity"
FT                   /evidence="ECO:0000250"
FT   DISULFID        40..54
FT                   /evidence="ECO:0000250"
FT   DISULFID        47..58
FT                   /evidence="ECO:0000250"
FT   DISULFID        53..72
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   73 AA;  7743 MW;  F0C75FC1535E3543 CRC64;
     MNTATGFIVL LVLATVLGCI EAGESHVRED AMGRARRGAC TPTGQPCPYN ESCCSGSCQE
     QLNENGHTVK RCV