CA14A_CONQU
ID CA14A_CONQU Reviewed; 40 AA.
AC P0CAQ8; A1X8C8; A1X8C9; H9N3V4;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Alpha-conotoxin-like Qc1.4a {ECO:0000303|PubMed:17400270};
DE AltName: Full=Qu-5 {ECO:0000303|PubMed:30917600};
DE Flags: Precursor; Fragment;
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].
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 NUCLEOTIDE SEQUENCE [MRNA] OF 7-40.
RX PubMed=22337864; DOI=10.1093/molbev/mss068;
RA Chang D., Duda T.F. Jr.;
RT "Extensive and continuous duplication facilitates rapid evolution and
RT diversification of gene families.";
RL Mol. Biol. Evol. 29:2019-2029(2012).
CC -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305}.
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; DQ311068; ABD33860.1; -; Genomic_DNA.
DR EMBL; JF723456; AFD18521.1; -; Genomic_DNA.
DR AlphaFoldDB; P0CAQ8; -.
DR ConoServer; 558; Qc1.4a 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 2: Evidence at transcript level;
KW Acetylcholine receptor inhibiting toxin; Amidation; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW Toxin.
FT PROPEP <1..19
FT /evidence="ECO:0000250"
FT /id="PRO_0000370673"
FT PEPTIDE 20..36
FT /note="Alpha-conotoxin-like Qc1.4a"
FT /id="PRO_0000370674"
FT PROPEP 37..40
FT /evidence="ECO:0000250"
FT /id="PRO_0000370675"
FT REGION 24..26
FT /note="Ser-Xaa-Pro motif, crucial for potent interaction
FT with nAChR"
FT /evidence="ECO:0000250|UniProtKB:P56636"
FT MOD_RES 36
FT /note="Cysteine amide"
FT /evidence="ECO:0000250"
FT DISULFID 22..28
FT /evidence="ECO:0000250|UniProtKB:P56636"
FT DISULFID 23..36
FT /evidence="ECO:0000250|UniProtKB:P56636"
FT NON_TER 1
SQ SEQUENCE 40 AA; 4043 MW; 699222C37061EE62 CRC64;
SDGRNTAAND KASDLMALRD GCCSNPSCSV NNPDICGGGR
