CDS1_CONLT
ID CDS1_CONLT Reviewed; 85 AA.
AC F6JWU7;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 25-MAY-2022, entry version 13.
DE RecName: Full=Alpha-conotoxin Lt28.1 {ECO:0000305|PubMed:28666820};
DE AltName: Full=Conotoxin Lt15.2 {ECO:0000312|EMBL:ADZ76484.1};
DE AltName: Full=Conotoxin Lt28.1 {ECO:0000303|PubMed:28666820};
DE Flags: Precursor;
OS Conus litteratus (Lettered cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Elisaconus.
OX NCBI_TaxID=89445;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND RECOMBINANT EXPRESSION.
RC TISSUE=Venom duct;
RX PubMed=28666820; DOI=10.1016/j.peptides.2017.06.008;
RA Lu J., Zhang K., Wang S., Sun T., Yu S., Dai Q., Liu Z.;
RT "Cloning, expression and functional characterization of a D-superfamily
RT conotoxin Lt28.1 with previously undescribed cysteine pattern.";
RL Peptides 94:64-70(2017).
CC -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC This toxin weakly inhibits alpha-9-alpha-10/CHRNA9-CHRNA10 nAChRs
CC (IC(50)=3 uM). {ECO:0000269|PubMed:28666820}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:28666820}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:28666820}.
CC -!- DOMAIN: The cysteine framework is XXVIII (C-C-C-CC-C-C-C-C-C).
CC {ECO:0000305}.
CC -!- PTM: Contains 5 disulfide bonds. {ECO:0000305}.
CC -!- MISCELLANEOUS: Very weakly inhibits alpha-3-beta-2/CHRNA3-CHRNB2 (19.4%
CC when 10 uM of toxin is tested) and alpha-4-beta-2/CHRNA4-CHRNB2 (18% at
CC 10 uM) nAChRs subtypes. Has no effect on alpha-3-beta-4/CHRNA3-CHRNB4,
CC alpha-4-beta-4/CHRNA4-CHRNB4, alpha-2-beta-2/CHRNA2-CHRNB2, alpha-2-
CC beta-4/CHRNA2-CHRNB4, alpha-7/CHRNA7 and alpha-6/alpha-3-beta-2-beta-3
CC (CHRNA6/CHRNA3-CHRNB2-CHRNB3) nAChRs subtypes.
CC {ECO:0000269|PubMed:28666820}.
CC -!- SIMILARITY: Belongs to the conotoxin D 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; HM003926; ADZ76484.1; -; mRNA.
DR AlphaFoldDB; F6JWU7; -.
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.
PE 3: Inferred from homology;
KW Acetylcholine receptor inhibiting toxin; Disulfide bond; Neurotoxin;
KW Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..40
FT /evidence="ECO:0000305|PubMed:28666820"
FT /id="PRO_0000451012"
FT CHAIN 41..85
FT /note="Alpha-conotoxin Lt28.1"
FT /evidence="ECO:0000305|PubMed:28666820"
FT /id="PRO_5003337452"
SQ SEQUENCE 85 AA; 9391 MW; 84F7AAB262566FFF CRC64;
MPKLEMMLLV LLILPLCYID AVGPPPPWNM EDEIIEHWQK LHCHEISDLT PWILCSPEPL
CGGKGCCAQE VCDCSGPACT CPPCL