TOX1_OXYLI
ID TOX1_OXYLI Reviewed; 69 AA.
AC P0C8M0;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Omega-oxotoxin-Ol1a;
DE Short=Omega-OXTX-Ol1a;
DE AltName: Full=Oxytoxin-1;
DE Short=OxyTx1;
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, AMIDATION AT ASN-69, AND TOXIC DOSE.
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). Is both paralytic and lethal when
CC injected into lepidopteran larvae. Is not toxic to mice.
CC {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:0000305}.
CC -!- MASS SPECTROMETRY: Mass=8058.2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18606178};
CC -!- TOXIC DOSE: PD(50) is 5.0 +- 0.3 nmol/g on lepidopteran larvae
CC (Spodoptera litura). {ECO:0000269|PubMed:18606178}.
CC -!- MISCELLANEOUS: The primary structure of the mature peptide is identical
CC to that of omega-oxotoxin-Ot1a from Oxyopes takobius (AC P83288).
CC -!- SIMILARITY: Belongs to the spiderine family. Spiderine subfamily.
CC {ECO:0000305}.
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DR AlphaFoldDB; P0C8M0; -.
DR SMR; P0C8M0; -.
DR ArachnoServer; AS000207; omega-oxotoxin-Ol1a.
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..69
FT /note="Omega-oxotoxin-Ol1a"
FT /id="PRO_0000359431"
FT DOMAIN 1..68
FT /note="Oxytoxin-type inhibitor cystine knot (ICK)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01208"
FT MOD_RES 69
FT /note="Asparagine 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..64
FT /evidence="ECO:0000250|UniProtKB:P86716"
FT DISULFID 17..52
FT /evidence="ECO:0000250|UniProtKB:P86716"
FT DISULFID 25..50
FT /evidence="ECO:0000250|UniProtKB:P86716"
SQ SEQUENCE 69 AA; 8069 MW; 2C3FCF05BA330159 CRC64;
DWECLPLHSS CDNDCVCCKN HHCHCPYSNV SKLEKWLPEW AKIPDALKRC SCQRNDKDGK
INTCDKYKN
