CA12_CONQU
ID CA12_CONQU Reviewed; 62 AA.
AC Q6PTD6; A1X8C7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Alpha-conotoxin-like Qc1.2 {ECO:0000303|PubMed:19779652};
DE AltName: Full=Qu-3 {ECO:0000303|PubMed:30917600};
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom duct;
RX PubMed=30917600; DOI=10.3390/md17030193;
RA Yao G., Peng C., Zhu Y., Fan C., Jiang H., Chen J., Cao Y., Shi Q.;
RT "High-throughput identification and analysis of novel conotoxins from three
RT vermivorous cone snails by transcriptome sequencing.";
RL Mar. Drugs 17:0-0(2019).
RN [3]
RP FUNCTION, SYNTHESIS OF 49-62, AND PYROGLUTAMATE FORMATION AT GLN-49.
RX PubMed=19779652; DOI=10.1093/abbs/gmp077;
RA Peng C., Chen W., Han Y., Sanders T., Chew G., Liu J., Hawrot E.,
RA Chi C.-W., Wang C.-G.;
RT "Characterization of a novel alpha4/4-conotoxin, Qc1.2, from vermivorous
RT Conus quercinus.";
RL Acta Biochim. Biophys. Sin. 41:858-864(2009).
CC -!- FUNCTION: Alpha-conotoxins bind to the nicotinic acetylcholine
CC receptors (nAChR) and inhibit them. This synthetic peptide (10 uM)
CC selectively, but weakly inhibits both rat neuronal alpha-3-beta-
CC 2/CHRNA3-CHRNB2 (63%) and alpha-3-beta-4/CHRNA3-CHRNB4 (37%) subtypes
CC of nAChR. {ECO:0000269|PubMed:19779652}.
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). Alpha4/4 pattern.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR EMBL; AY580320; AAS93423.1; -; mRNA.
DR EMBL; DQ311067; ABD33859.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6PTD6; -.
DR ConoServer; 118; Qc1.2 precursor.
DR ConoServer; 557; Qc1.2 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 1: Evidence at protein level;
KW Acetylcholine receptor inhibiting toxin; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin;
KW Pyrrolidone carboxylic acid; Secreted; Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..48
FT /evidence="ECO:0000305|PubMed:19779652"
FT /id="PRO_0000370671"
FT PEPTIDE 49..62
FT /note="Alpha-conotoxin-like Qc1.2"
FT /evidence="ECO:0000305|PubMed:19779652"
FT /id="PRO_0000370672"
FT MOD_RES 49
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000305|PubMed:19779652"
FT DISULFID 50..56
FT /evidence="ECO:0000250|UniProtKB:P69657"
FT DISULFID 51..61
FT /evidence="ECO:0000250|UniProtKB:P69657"
FT CONFLICT 6
FT /note="M -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 62 AA; 6745 MW; 2081153B1FADFDD4 CRC64;
MGMRMMFTVF LLVALATTVA SFTLDRASNG RNAAADDKPS DWIALAIKQC CANPPCKHVN
CR
