ID   TOX2_OXYLI              Reviewed;          55 AA.
AC   P84756;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Omega-oxotoxin-Ol1b;
DE            Short=Omega-OXTX-Ol1b;
DE   AltName: Full=Oxytoxin-2;
DE            Short=OxyTx2;
OS   Oxyopes lineatus (Lynx spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Lycosoidea; Oxyopidae; Oxyopes.
OX   NCBI_TaxID=366495;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, AND AMIDATION AT SER-55.
RC   TISSUE=Venom;
RX   PubMed=18606178; DOI=10.1016/j.toxicon.2008.05.019;
RA   Villegas E., Adachi-Akahane S., Bosmans F., Tytgat J., Nakajima T.,
RA   Corzo G.;
RT   "Biochemical characterization of cysteine-rich peptides from Oxyopes sp.
RT   venom that block calcium ion channels.";
RL   Toxicon 52:228-236(2008).
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:18606178}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18606178}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:18606178}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=6175.2; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:18606178};
CC   -!- SIMILARITY: Belongs to the spiderine family. Spiderine subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P84756; -.
DR   SMR; P84756; -.
DR   PRIDE; P84756; -.
DR   ArachnoServer; AS000208; omega-oxotoxin-Ol1b.
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   Amidation; Calcium channel impairing toxin; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Knottin; Neurotoxin; Secreted;
KW   Toxin; Voltage-gated calcium channel impairing toxin.
FT   CHAIN           1..55
FT                   /note="Omega-oxotoxin-Ol1b"
FT                   /id="PRO_0000087683"
FT   DOMAIN          1..53
FT                   /note="Oxytoxin-type inhibitor cystine knot (ICK)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01208"
FT   MOD_RES         55
FT                   /note="Serine amide"
FT                   /evidence="ECO:0000269|PubMed:18606178"
FT   DISULFID        4..18
FT                   /evidence="ECO:0000250|UniProtKB:P86716"
FT   DISULFID        11..23
FT                   /evidence="ECO:0000250|UniProtKB:P86716"
FT   DISULFID        15..49
FT                   /evidence="ECO:0000250|UniProtKB:P86716"
FT   DISULFID        17..39
FT                   /evidence="ECO:0000250|UniProtKB:P86716"
FT   DISULFID        25..37
FT                   /evidence="ECO:0000250|UniProtKB:P86716"
SQ   SEQUENCE   55 AA;  6186 MW;  50EB2063188CA8F4 CRC64;
     AWKCLPKDST CGDDCDCCEG LHCHCPLRNM LPAILRCSCQ SKDDHINTCP KYKKS