ID   TBO1_TIBOB              Reviewed;          79 AA.
AC   A0A0G3F8Z3;
DT   28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=Omega-phylotoxin-To1a {ECO:0000303|PubMed:26611444};
DE            Short=Omega-PHTX-To1a {ECO:0000305};
DE   AltName: Full=Omega-Tbo-IT1 {ECO:0000303|PubMed:26611444};
DE   Flags: Precursor;
OS   Tibellus oblongus (Oblong running crab spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Dionycha; Philodromidae; Tibellus.
OX   NCBI_TaxID=336685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 39-50, MASS SPECTROMETRY,
RP   STRUCTURE BY NMR OF 39-79, DISULFIDE BONDS, SUBCELLULAR LOCATION, AND
RP   RECOMBINANT EXPRESSION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=26611444; DOI=10.1038/srep17232;
RA   Mikov A.N., Fedorova I.M., Potapieva N.N., Maleeva E.E., Andreev Y.A.,
RA   Zaitsev A.V., Kim K.K., Bocharov E.V., Bozin T.N., Altukhov D.A.,
RA   Lipkin A.V., Kozlov S.A., Tikhonov D.B., Grishin E.V.;
RT   "Omega-Tbo-IT1-new inhibitor of insect calcium channels isolated from
RT   spider venom.";
RL   Sci. Rep. 5:17232-17232(2015).
RN   [2]
RP   TOXIC DOSE.
RX   PubMed=33406803; DOI=10.3390/toxins13010029;
RA   Korolkova Y., Maleeva E., Mikov A., Lobas A., Solovyeva E., Gorshkov M.,
RA   Andreev Y., Peigneur S., Tytgat J., Kornilov F., Lushpa V., Mineev K.,
RA   Kozlov S.;
RT   "New Insectotoxin from Tibellus Oblongus Spider Venom Presents Novel
RT   Adaptation of ICK Fold.";
RL   Toxins 13:0-0(2021).
CC   -!- FUNCTION: Insect-specific toxin that probably acts as an inhibitor of
CC       presynaptic insect calcium channels, presumably Cav2 subtype. In vivo,
CC       induces immediate paralysis on insects, followed by death when high
CC       doses are injected. {ECO:0000269|PubMed:26611444}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26611444}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:26611444}.
CC   -!- DOMAIN: Adopts an inhibitor cystine knot (ICK) fold. Is defined as a
CC       knottin (one disulfide bond crosses the macrocycle formed by two other
CC       disulfide bonds). {ECO:0000269|PubMed:26611444}.
CC   -!- MASS SPECTROMETRY: Mass=4332.8; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:26611444};
CC   -!- TOXIC DOSE: LD(50) is 19 ug/g on fly larvae (M.domestica) (4.4 nmol/g
CC       of body weight). {ECO:0000269|PubMed:26611444}.
CC   -!- TOXIC DOSE: LD(50) is 20 ug/g on juvenile cockroaches (G.portentosa).
CC       {ECO:0000269|PubMed:26611444}.
CC   -!- TOXIC DOSE: LD(100) is 100 ug/g when tested on larvae of the housefly
CC       Musca domestica. {ECO:0000269|PubMed:33406803}.
CC   -!- MISCELLANEOUS: The toxin does not affect frog neuromuscular junctions
CC       and glutamatergic and GABAergic transmission in rat brains.
CC       {ECO:0000269|PubMed:26611444}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KP308197; AKJ77984.1; -; mRNA.
DR   PDB; 2MYH; NMR; -; A=39-79.
DR   PDBsum; 2MYH; -.
DR   AlphaFoldDB; A0A0G3F8Z3; -.
DR   SMR; A0A0G3F8Z3; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium channel impairing toxin; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Knottin; Neurotoxin;
KW   Presynaptic neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated calcium channel impairing toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..38
FT                   /evidence="ECO:0000305|PubMed:26611444"
FT                   /id="PRO_0000443393"
FT   CHAIN           39..79
FT                   /note="Omega-phylotoxin-To1a"
FT                   /evidence="ECO:0000305|PubMed:26611444"
FT                   /id="PRO_5005184403"
FT   DISULFID        39..59
FT                   /evidence="ECO:0000269|PubMed:26611444,
FT                   ECO:0007744|PDB:2MYH"
FT   DISULFID        46..63
FT                   /evidence="ECO:0000269|PubMed:26611444,
FT                   ECO:0007744|PDB:2MYH"
FT   DISULFID        58..78
FT                   /evidence="ECO:0000269|PubMed:26611444,
FT                   ECO:0007744|PDB:2MYH"
FT   DISULFID        65..76
FT                   /evidence="ECO:0000269|PubMed:26611444,
FT                   ECO:0007744|PDB:2MYH"
FT   HELIX           49..51
FT                   /evidence="ECO:0007829|PDB:2MYH"
FT   STRAND          58..68
FT                   /evidence="ECO:0007829|PDB:2MYH"
FT   TURN            69..71
FT                   /evidence="ECO:0007829|PDB:2MYH"
FT   STRAND          72..79
FT                   /evidence="ECO:0007829|PDB:2MYH"
SQ   SEQUENCE   79 AA;  8733 MW;  5C32EF258266C596 CRC64;
     MKKTFCFILI LVCIVLKSVN AEEEDNFEES SLEMETARCA SKNERCGNAL YGTKGPGCCN
     GKCICRTVPR KGVNSCRCM