CA19_CONLE
ID CA19_CONLE Reviewed; 37 AA.
AC A1X8D6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Alpha-conotoxin-like Lp1.9 {ECO:0000303|PubMed:17400270};
DE Flags: Precursor; Fragment;
OS Conus leopardus (Leopard cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Lithoconus.
OX NCBI_TaxID=101306;
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).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ311076; ABD33868.1; -; Genomic_DNA.
DR AlphaFoldDB; A1X8D6; -.
DR ConoServer; 566; Lp1.9 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 Toxin.
FT PROPEP <1..21
FT /evidence="ECO:0000305|PubMed:17400270"
FT /id="PRO_0000370657"
FT PEPTIDE 22..37
FT /note="Alpha-conotoxin-like Lp1.9"
FT /evidence="ECO:0000305|PubMed:17400270"
FT /id="PRO_0000370658"
FT REGION 24..26
FT /note="Lacks the Ser-Xaa-Pro motif that is crucial for
FT potent interaction with nAChR"
FT /evidence="ECO:0000305"
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 37 AA; 3822 MW; ADB310FD421EFB85 CRC64;
SDDNDVAAEM MSGLIALAID SCCSDSDCNA NHPDMCS