ID   CA11B_CONQU             Reviewed;          67 AA.
AC   Q6PPB3; A1X8C4;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Alpha-conotoxin-like Qc1.1b;
DE   AltName: Full=Qc1.3;
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 [GENOMIC DNA / MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=17400270; DOI=10.1016/j.toxicon.2007.02.011;
RA   Yuan D.-D., Han Y.-H., Wang C.-G., Chi C.-W.;
RT   "From the identification of gene organization of alpha conotoxins to the
RT   cloning of novel toxins.";
RL   Toxicon 49:1135-1149(2007).
CC   -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC       the nicotinic acetylcholine receptors (nAChR) and thus inhibit them (By
CC       similarity). Has possibly a distinct nAChR binding mode from other
CC       alpha-conotoxins, due to a different three residue motif (lacks the
CC       Ser-Xaa-Pro motif) (By similarity). {ECO:0000250|UniProtKB:Q2I2R8}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:17400270}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:17400270}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR   EMBL; AY588972; AAS99932.1; -; mRNA.
DR   EMBL; DQ311061; ABD33853.1; -; mRNA.
DR   EMBL; DQ311064; ABD33856.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6PPB3; -.
DR   SMR; Q6PPB3; -.
DR   ConoServer; 551; Qc1.1b precursor.
DR   ConoServer; 554; Qc1.1b precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0035792; C:host cell postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR009958; Conotoxin_a-typ.
DR   Pfam; PF07365; Toxin_8; 1.
PE   3: Inferred from homology;
KW   Acetylcholine receptor inhibiting toxin; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..46
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000377449"
FT   PEPTIDE         47..67
FT                   /note="Alpha-conotoxin-like Qc1.1b"
FT                   /id="PRO_0000377450"
FT   REGION          51..53
FT                   /note="Lacks the Ser-Xaa-Pro motif that is crucial for
FT                   potent interaction with nAChR"
FT                   /evidence="ECO:0000305"
FT   DISULFID        49..55
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   DISULFID        50..63
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
SQ   SEQUENCE   67 AA;  7417 MW;  D3D776AA38BBBCCD CRC64;
     MGMRMMFTMF LLVVLAITVV SFTSDHASDG RNTAANDKAS KLMALRNECC DNPPCKSSNP
     DLCDWRS