ID   TU172_LOPOL             Reviewed;         127 AA.
AC   P0DKP4;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=Turripeptide OL172;
DE   Contains:
DE     RecName: Full=Turripeptide OL172 1;
DE   Contains:
DE     RecName: Full=Turripeptide OL172 2;
DE   Contains:
DE     RecName: Full=Turripeptide OL172 3;
DE   Contains:
DE     RecName: Full=Turripeptide OL172 conotoxin-like;
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], AND PYROGLUTAMATE FORMATION AT GLN-44; GLN-76
RP   AND GLN-107.
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 of the turripeptide OL172 conotoxin-like
CC       is C-CC-C.
CC   -!- PTM: The turripeptide OL172 conotoxin-like contains 2 disulfide bonds.
CC       {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P0DKP4; -.
DR   SMR; P0DKP4; -.
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   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Pyrrolidone carboxylic acid;
KW   Repeat; Secreted; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000305"
FT   PEPTIDE         21..41
FT                   /note="Turripeptide OL172 1"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000419860"
FT   PROPEP          42..43
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000419861"
FT   PEPTIDE         44..72
FT                   /note="Turripeptide OL172 2"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000419862"
FT   PROPEP          73..75
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000419863"
FT   PEPTIDE         76..103
FT                   /note="Turripeptide OL172 3"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000419864"
FT   PROPEP          104..106
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000419865"
FT   PEPTIDE         107..127
FT                   /note="Turripeptide OL172 conotoxin-like"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000419866"
FT   MOD_RES         44
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000305|PubMed:16477526"
FT   MOD_RES         76
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000305|PubMed:16477526"
FT   MOD_RES         107
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000305|PubMed:16477526"
SQ   SEQUENCE   127 AA;  14340 MW;  69D9EC3230B3531D CRC64;
     MFSTLIFLTA VTLLMMPSQT VPAPLKDVND IRVKGLLPLL RQRQLQIMPS QTIPALKDVN
     DIRVKGLLSL LRQRKQEIMP SQTIPALKDV NDIRVKGLLS LLRQRKQEEC DDPDGLMCCT
     ISEMPTC