ID   TUB1_LOPOL              Reviewed;          83 AA.
AC   P0DKN2;
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 Lol11.1;
DE   AltName: Full=OL105;
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 voltage-gated potassium
CC       channels (Kv). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The cysteine framework is XI (C-C-CC-CC-C-C).
CC   -!- PTM: Contains 4 disulfide bonds. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the conopeptide I2-like superfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P0DKN2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015459; F:potassium 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;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..83
FT                   /note="Turripeptide Lol11.1"
FT                   /id="PRO_0000419848"
SQ   SEQUENCE   83 AA;  9162 MW;  A0142EE0BD661D88 CRC64;
     MARQMMTVGC LILIVVLLDM MVPVFNTCPG QYDECGNGPE EGECCGTHNY CCKNACTTYH
     HCHGGRDAGK LLRSLKKLKL TTH