CA14_CONLI
ID CA14_CONLI Reviewed; 65 AA.
AC S4UJV1;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Alpha-conotoxin-like Lv1.4 {ECO:0000312|EMBL:AGK23159.1};
DE AltName: Full=Conotoxin Lv1d {ECO:0000303|PubMed:33610632};
DE Flags: Precursor;
OS Conus lividus (Livid cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Lividoconus.
OX NCBI_TaxID=89426;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SYNTHESIS OF 49-65.
RC TISSUE=Venom duct;
RX PubMed=33610632; DOI=10.1016/j.toxicon.2021.02.003;
RA Qiang Y., Wu Y., Zhao D., Zhao B., Wang F., Ren S., Wen Y., Gu J.,
RA Zhang L., Liu K., Niu J., Wang L.;
RT "Discovery and characterization of the novel conotoxin Lv1d from Conus
RT lividus that presents analgesic activity.";
RL Toxicon 194:70-78(2021).
CC -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC the nicotinic acetylcholine receptors (nAChR) and thus inhibit them (By
CC similarity). At high doses (10 uM), the synthetic non-amidated toxin
CC (residues 49-65) completely inhibits frog sciatic nerve-gastrocnemius
CC muscle contractility (PubMed:33610632). It also inhibit the cholinergic
CC miniature excitatory postsynaptic currents (mEPSCs) frequency and
CC amplitude of projection neurons in insects (D.melanogaster)
CC (PubMed:33610632). In vivo, the toxin (100 ug/kg) shows good analgesic
CC effects in mouse hot plate model and formalin test (PubMed:33610632).
CC {ECO:0000250|UniProtKB:K4RNX9, ECO:0000269|PubMed:33610632}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33610632}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:33610632}.
CC -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
CC {ECO:0000305}.
CC -!- PTM: Possibly amidated at Cys-64. {ECO:0000305|PubMed:33610632}.
CC -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
CC -!- CAUTION: The C-terminal Gly suggests that the peptide is amidated and
CC is one residue shorter (residues 49-64) than that synthesized by Qiang
CC et al., 2021. {ECO:0000305|PubMed:33610632}.
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DR EMBL; JX293419; AGK23159.1; -; mRNA.
DR AlphaFoldDB; S4UJV1; -.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR009958; Conotoxin_a-typ.
DR InterPro; IPR018072; Conotoxin_a-typ_CS.
DR Pfam; PF07365; Toxin_8; 1.
DR PROSITE; PS60014; ALPHA_CONOTOXIN; 1.
PE 3: Inferred from homology;
KW Acetylcholine receptor inhibiting toxin; Amidation; Disulfide bond;
KW Neurotoxin; Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..48
FT /evidence="ECO:0000305|PubMed:33610632"
FT /id="PRO_0000453023"
FT PEPTIDE 49..65
FT /note="Alpha-conotoxin-like Lv1.4"
FT /evidence="ECO:0000305|PubMed:33610632"
FT /id="PRO_5004533440"
FT REGION 52..54
FT /note="Ser-Xaa-Pro motif, crucial for potent interaction
FT with nAChR"
FT /evidence="ECO:0000250|UniProtKB:P56636"
FT DISULFID 50..56
FT /evidence="ECO:0000250|UniProtKB:K4RNX9"
FT DISULFID 51..64
FT /evidence="ECO:0000250|UniProtKB:K4RNX9"
SQ SEQUENCE 65 AA; 7125 MW; 5CFC0C20AEA86BC1 CRC64;
MGMRMMFTML LLVVLATTVV SFTLDHAFDG RNTAANNKAT DLMALPVRGC CSDPPCRHKH
QDLCG
