ID   CA12_CONAA              Reviewed;          61 AA.
AC   A0A3G3C7S9;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   13-FEB-2019, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Alpha-conotoxine-like Am1.2 {ECO:0000305};
DE   Flags: Precursor;
OS   Conus amadis (Amadis cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Leptoconus.
OX   NCBI_TaxID=198732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND AMIDATION AT CYS-60.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=30593932; DOI=10.1016/j.jprot.2018.12.028;
RA   Vijayasarathy M., Balaram P.;
RT   "Cone snail prolyl-4-hydroxylase alpha-subunit sequences derived from
RT   transcriptomic data and mass spectrometric analysis of variable proline
RT   hydroxylation in C. amadis venom.";
RL   J. Proteomics 194:37-48(2019).
CC   -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC       the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC       {ECO:0000250|UniProtKB:E2DIH5}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30593932}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:30593932}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
CC       {ECO:0000305}.
CC   -!- PTM: Contains 2 disulfide bonds. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR   EMBL; MH282816; AYP73023.1; -; mRNA.
DR   SMR; A0A3G3C7S9; -.
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   1: Evidence at protein level;
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..44
FT                   /evidence="ECO:0000250|UniProtKB:A0A3G3C7V0"
FT                   /id="PRO_0000453585"
FT   PEPTIDE         45..60
FT                   /note="Alpha-conotoxine-like Am1.2"
FT                   /evidence="ECO:0000250|UniProtKB:A0A3G3C7V0"
FT                   /id="PRO_5018047427"
FT   REGION          48..50
FT                   /note="Ser-Xaa-Pro motif, crucial for potent interaction
FT                   with nAChR"
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   MOD_RES         60
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000250|UniProtKB:A0A3G3C7V0"
SQ   SEQUENCE   61 AA;  6387 MW;  DAA770028ADCF518 CRC64;
     MGMRMMFTVF LLVVLATTVV SFMSGRASHG RNAAASDLIA LTIKGCCSVP PCTANHPELC
     G