O161_CONQU
ID O161_CONQU Reviewed; 94 AA.
AC P0DJC6;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=Conotoxin Qc6.1;
DE Flags: Precursor;
OS Conus quercinus (Oak cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Lividoconus.
OX NCBI_TaxID=101313;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RA Hillyard D.R., Mcintosh M.J., Jones R.M., Cartier E.G., Watkins M.,
RA Olivera B.M., Layer R.T.;
RT "O-Superfamily conotoxin peptides.";
RL Patent number JP2003533178, 05-NOV-2002.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000250}.
CC -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
CC -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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DR EMBL; DJ379477; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR AlphaFoldDB; P0DJC6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR004214; Conotoxin.
DR Pfam; PF02950; Conotoxin; 1.
PE 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Disulfide bond; Knottin; Neurotoxin;
KW Secreted; Signal; Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..62
FT /evidence="ECO:0000250"
FT /id="PRO_0000415313"
FT PEPTIDE 65..94
FT /note="Conotoxin Qc6.1"
FT /id="PRO_0000415314"
FT DISULFID 66..84
FT /evidence="ECO:0000250"
FT DISULFID 73..88
FT /evidence="ECO:0000250"
FT DISULFID 83..92
FT /evidence="ECO:0000250"
SQ SEQUENCE 94 AA; 10302 MW; EC0CDF050F50FCAA CRC64;
MKLTCMMIVA LLFLTAWTFV TAVDSKNELE NRGGWGQAGG WGKLFPMARD EMKNSEVSKL
DNKRKCAAAG EACVIPIIGN VFCCKGYCLF VCIS