CA14_CONLE
ID CA14_CONLE Reviewed; 68 AA.
AC A1X8B6; Q6PTD2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=Alpha-conotoxin Lp1.4 {ECO:0000303|PubMed:17400270};
DE Flags: Precursor;
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 / MRNA], AND AMIDATION AT ASP-65.
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 FUNCTION, AND SYNTHESIS OF 49-65.
RX PubMed=20801929; DOI=10.1093/abbs/gmq074;
RA Peng C., Chen W., Sanders T., Chew G., Liu J., Hawrot E., Chi C.;
RT "Chemical synthesis and characterization of two alpha4/7-conotoxins.";
RL Acta Biochim. Biophys. Sin. 42:745-753(2010).
CC -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC This toxin inhibits mouse muscle alpha-1-beta-1-gamma-delta (CHRNA1-
CC CHRNB1-CHRNG-CHRND), and weakly rat neuronal alpha-6/alpha-3-beta-2
CC (CHRNA6/CHRNA3-CHRNB2). {ECO:0000269|PubMed:20801929}.
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 -!- MISCELLANEOUS: Does not or very weakly inhibits rat neuronal alpha-7
CC (CHRNA7), alpha-3-beta-2 (CHRNA3-CHRNB2), alpha-6/alpha-3-beta-4
CC (CHRNA6/CHRNA3-CHRNB4), alpha-3-beta-4 (CHRNA3-CHRNB4), alpha-4-beta-4
CC (CHRNA4-CHRNB4) and alpha-4-beta-2 (CHRNA4-CHRNB2) nAChR.
CC {ECO:0000269|PubMed:20801929}.
CC -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR EMBL; DQ311056; ABD33848.1; -; Genomic_DNA.
DR EMBL; AY580324; AAS93427.1; -; mRNA.
DR AlphaFoldDB; A1X8B6; -.
DR SMR; A1X8B6; -.
DR ConoServer; 122; Lp1.4 precursor.
DR ConoServer; 546; Lp1.4 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; Amidation; 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|PubMed:17400270"
FT /id="PRO_0000370650"
FT PEPTIDE 49..65
FT /note="Alpha-conotoxin Lp1.4"
FT /evidence="ECO:0000305|PubMed:17400270"
FT /id="PRO_0000370651"
FT REGION 52..54
FT /note="Ser-Xaa-Pro motif, crucial for potent interaction
FT with nAChR"
FT /evidence="ECO:0000250|UniProtKB:P56636"
FT MOD_RES 65
FT /note="Aspartic acid 1-amide"
FT /evidence="ECO:0000305|PubMed:17400270"
FT DISULFID 50..56
FT /evidence="ECO:0000305|PubMed:20801929"
FT DISULFID 51..64
FT /evidence="ECO:0000305|PubMed:20801929"
FT CONFLICT 7
FT /note="S -> F (in Ref. 1; AAS93427)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 68 AA; 7292 MW; 2FD44A064F2E2F37 CRC64;
MGMRMMSIMF MLVVLATTVV SFTSDRALDA MNAAASKKAS RLIALAVRGC CSHPACSGNH
QELCDGRR
