CA1A_CONQU
ID CA1A_CONQU Reviewed; 83 AA.
AC S4UJW3;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Alpha-conotoxin QcIA {ECO:0000305};
DE AltName: Full=A superfamily conotoxin Qc1.11 {ECO:0000312|EMBL:AGK23189.1};
DE AltName: Full=A superfamily conotoxin Qc1.16 {ECO:0000305};
DE AltName: Full=Alpha4/7-conotoxin QuIA {ECO:0000303|PubMed:35200675};
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] {ECO:0000312|EMBL:AGK23189.1}
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 [2]
RP FUNCTION, AND SYNTHESIS OF 49-65 OF AN AMIDATED PEPTIDE.
RX PubMed=35200675; DOI=10.3390/md20020146;
RA Wang L., Wu X., Zhu X., Zhangsun D., Wu Y., Luo S.;
RT "A novel alpha4/7-conotoxin QuIA selectively inhibits alpha3beta2 and
RT alpha6/alpha3beta4 nicotinic acetylcholine receptor subtypes with high
RT efficacy.";
RL Mar. Drugs 20:0-0(2022).
CC -!- FUNCTION: Alpha-conotoxins bind to the nicotinic acetylcholine
CC receptors (nAChR) and inhibit them. A synthetic amidated version of
CC this toxin potently and preferentially antagonizes neuronal rat alpha-
CC 3-beta-2 (IC(50)=55.7 nM) and alpha-6/alpha-3-beta-4 (IC(50)=90.69 nM)
CC nAChRs. {ECO:0000269|PubMed:35200675}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:35200675}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:35200675}.
CC -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: Shows no or weak inhibitory activity on a range of
CC nAChRs subtypes, including human and rat alpha-9-alpha-10, mouse alpha-
CC 1-beta-1-delta-epsilon, rat alpha-7, rat alpha-6/alpha-3-beta-2-beta-3,
CC rat alpha-3-beta-4, rat alpha-4-beta-2, and rat alpha-9-alpha-10.
CC {ECO:0000269|PubMed:35200675}.
CC -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR EMBL; JX293449; AGK23189.1; -; mRNA.
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 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..48
FT /evidence="ECO:0000305"
FT /id="PRO_0000455817"
FT PEPTIDE 49..65
FT /note="Alpha-conotoxin QcIA"
FT /evidence="ECO:0000305|PubMed:35200675"
FT /id="PRO_5004533488"
FT PROPEP 66..83
FT /evidence="ECO:0000305"
FT /id="PRO_0000455818"
FT REGION 53..55
FT /note="Ser-Xaa-Pro motif, crucial for potent interaction
FT with nAChR"
FT /evidence="ECO:0000250|UniProtKB:P56636"
FT DISULFID 51..57
FT /evidence="ECO:0000250|UniProtKB:P56636"
FT DISULFID 52..65
FT /evidence="ECO:0000250|UniProtKB:P56636"
SQ SEQUENCE 83 AA; 9062 MW; A6A4CE30BEA87FC6 CRC64;
MGMRMMFTLF LLAVLSTTVV SFTLDRASNG RDAAADSKAA DQIAQTVRDE CCSNPSCAQT
HPEICRRTLM LQNPLNHDMS PSA
