ID   CA12_CONMR              Reviewed;          68 AA.
AC   A6M934;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Alpha-conotoxin-like Mr1.2;
DE   Flags: Precursor;
OS   Conus marmoreus (Marble cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Conus.
OX   NCBI_TaxID=42752;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
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.
CC       {ECO:0000250}.
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}.
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DR   EMBL; DQ359140; ABD48791.1; -; mRNA.
DR   AlphaFoldDB; A6M934; -.
DR   ConoServer; 127; Mr1.2 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; 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:0000250"
FT                   /id="PRO_0000370661"
FT   PEPTIDE         49..65
FT                   /note="Alpha-conotoxin-like Mr1.2"
FT                   /id="PRO_0000370662"
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="Asparagine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        50..56
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   DISULFID        51..64
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
SQ   SEQUENCE   68 AA;  7296 MW;  31C166F007FC1439 CRC64;
     MGMRMMFTVF LLVVLATTVV SFTSDRGSDG RNAAAKDKAS DLVALTVKGC CSNPPCYANN
     QAYCNGRR