ID   TU139_LOPOL             Reviewed;          82 AA.
AC   P0DKN8;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Turripeptide OL139;
OS   Lophiotoma olangoensis (Sea snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Turridae; Iotyrris.
OX   NCBI_TaxID=2420066;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=16477526; DOI=10.1007/s00239-005-0010-x;
RA   Watkins M., Hillyard D.R., Olivera B.M.;
RT   "Genes expressed in a turrid venom duct: divergence and similarity to
RT   conotoxins.";
RL   J. Mol. Evol. 62:247-256(2006).
CC   -!- FUNCTION: Acts as a neurotoxin by inhibiting an ion channel.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The cysteine framework is C-C-C-C-C-C-C-C-C-C-C-C.
CC   -!- PTM: Contains 6 disulfide bonds. {ECO:0000250}.
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DR   AlphaFoldDB; P0DKN8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Toxin.
FT   CHAIN           1..82
FT                   /note="Turripeptide OL139"
FT                   /id="PRO_0000419854"
FT   REGION          58..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   82 AA;  8859 MW;  D146F80FBC0BDE4A CRC64;
     QEGNVCHRPC FRCHVCGETI AACAACSICI GCEEVVEDAC AGNPCYWCDN CGVNDGSHRT
     TRDTADKTHG GSQRDRFFQS IA