ID   TU179_LOPOL             Reviewed;          70 AA.
AC   P0DKM2;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Turripeptide OL179;
DE   Flags: Precursor;
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   -!- MISCELLANEOUS: The mature peptide does not contain cysteine residues.
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DR   AlphaFoldDB; P0DKM2; -.
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   Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..32
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000419834"
FT   CHAIN           33..70
FT                   /note="Turripeptide OL179"
FT                   /id="PRO_0000419835"
SQ   SEQUENCE   70 AA;  7916 MW;  3F8848736F405096 CRC64;
     MMAKQVVVLL ALLLLLPIVT ASMGDASGRT GRIYMYGTSI QDLFRYLQLD YQRNVFLLRF
     LLGRGGLLLH