ID   TOX1_OXYTA              Reviewed;         123 AA.
AC   P83288; W0LP48;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2018, sequence version 2.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Omega-oxotoxin-Ot1a;
DE            Short=Omega-OXTX-Ot1a;
DE   AltName: Full=Oxytoxin-1 {ECO:0000303|PubMed:24462682};
DE            Short=OxyTx1 {ECO:0000303|PubMed:24462682};
DE   AltName: Full=Tx-1 {ECO:0000312|EMBL:AHG24516.1};
DE   Flags: Precursor;
OS   Oxyopes takobius (Lynx spider) (Oxyopes foliiformis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Lycosoidea; Oxyopidae; Oxyopes.
OX   NCBI_TaxID=666126;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=24462682; DOI=10.1016/j.febslet.2014.01.018;
RA   Sachkova M.Y., Slavokhotova A.A., Grishin E.V., Vassilevski A.A.;
RT   "Genes and evolution of two-domain toxins from lynx spider venom.";
RL   FEBS Lett. 588:740-745(2014).
RN   [2]
RP   PROTEIN SEQUENCE OF 55-123, FUNCTION, SUBCELLULAR LOCATION, TOXIC DOSE,
RP   MASS SPECTROMETRY, AND CIRCULAR DICHROISM ANALYSIS.
RC   TISSUE=Venom;
RX   PubMed=11976325; DOI=10.1074/jbc.m200511200;
RA   Corzo G., Villegas E., Gomez-Lagunas F., Possani L.D., Belokoneva O.S.,
RA   Nakajima T.;
RT   "Oxyopinins, large amphipathic peptides isolated from the venom of the wolf
RT   spider Oxyopes kitabensis with cytolytic properties and positive
RT   insecticidal cooperativity with spider neurotoxins.";
RL   J. Biol. Chem. 277:23627-23637(2002).
CC   -!- FUNCTION: Weak blocker of vertebrate P/Q-, N- and L-type voltage-gated
CC       calcium channels (Cav1 and Cav2) (By similarity). Is both paralytic and
CC       lethal when injected into lepidopteran larvae. Is not toxic to mice.
CC       {ECO:0000250, ECO:0000269|PubMed:11976325}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11976325}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:11976325}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000305}.
CC   -!- PTM: Mass spectrometry data suggest a carboxylated free C-terminal
CC       residue.
CC   -!- MASS SPECTROMETRY: Mass=8059.25; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11976325};
CC   -!- TOXIC DOSE: LD(50) is 5.1 +- 0.5 nmol/g on lepidopteran larvae
CC       (Spodoptera litura). {ECO:0000269|PubMed:11976325}.
CC   -!- MISCELLANEOUS: The primary structure of the mature peptide is identical
CC       to that of omega-oxotoxin-Ol1a from Oxyopes lineatus (AC P0C8M0).
CC   -!- SIMILARITY: Belongs to the spiderine family. Spiderine subfamily.
CC       {ECO:0000305}.
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DR   EMBL; KF766562; AHG24516.1; -; mRNA.
DR   AlphaFoldDB; P83288; -.
DR   ArachnoServer; AS000779; omega-oxotoxin-Ot1a.
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.
DR   InterPro; IPR044061; OXYTX_ICK.
DR   PROSITE; PS51861; OXYTX_ICK; 1.
PE   1: Evidence at protein level;
KW   Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated calcium channel impairing toxin.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..54
FT                   /evidence="ECO:0000269|PubMed:11976325"
FT                   /id="PRO_0000444424"
FT   CHAIN           55..123
FT                   /note="Omega-oxotoxin-Ot1a"
FT                   /evidence="ECO:0000269|PubMed:11976325"
FT                   /id="PRO_0000087676"
FT   DOMAIN          55..122
FT                   /note="Oxytoxin-type inhibitor cystine knot (ICK)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01208"
FT   DISULFID        58..72
FT                   /evidence="ECO:0000250|UniProtKB:P86716"
FT   DISULFID        65..77
FT                   /evidence="ECO:0000250|UniProtKB:P86716"
FT   DISULFID        69..118
FT                   /evidence="ECO:0000250|UniProtKB:P86716"
FT   DISULFID        71..106
FT                   /evidence="ECO:0000250|UniProtKB:P86716"
FT   DISULFID        79..104
FT                   /evidence="ECO:0000250|UniProtKB:P86716"
SQ   SEQUENCE   123 AA;  14065 MW;  E6154B3568B180B4 CRC64;
     MKIVLVFVCT LYLAQATYLS EQDVNEVSEF LEALDQANEA ASEMVEAAET EEARDWECLP
     LHSSCDNDCV CCKNHHCHCP YSNVSKLEKW LPEWAKIPDA LKRCSCQRND KDGKINTCDK
     YKN