TU61_LOPOL
ID TU61_LOPOL Reviewed; 82 AA.
AC P0DKM3;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 23-FEB-2022, entry version 15.
DE RecName: Full=Turripeptide Lol6.1;
DE AltName: Full=OL38;
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 -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000250}.
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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; Knottin; Neurotoxin; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..48
FT /evidence="ECO:0000255"
FT /id="PRO_0000419836"
FT CHAIN 49..82
FT /note="Turripeptide Lol6.1"
FT /id="PRO_0000419837"
FT DISULFID 54..66
FT /evidence="ECO:0000250"
FT DISULFID 58..71
FT /evidence="ECO:0000250"
FT DISULFID 65..77
FT /evidence="ECO:0000250"
SQ SEQUENCE 82 AA; 9170 MW; CF44E8CE67F28C6C CRC64;
MRFHWIPTLT VLLVLSMSFG TEAIPXXXXX XXXXXXXXXX XXXXXXXXSE VLECYFECGN
WEGTCCDTGI CVGIHNCKIP EN