ID   CA1C_CONAN              Reviewed;          17 AA.
AC   P0C1V8;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Alpha-conotoxin-like AnIC;
OS   Conus anemone (Anemone cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Floraconus.
OX   NCBI_TaxID=101285;
RN   [1]
RP   PROTEIN SEQUENCE, SULFATION AT TYR-16, AMIDATION AT CYS-17, MASS
RP   SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=14971903; DOI=10.1021/jm031010o;
RA   Loughnan M.L., Nicke A., Jones A., Adams D.J., Alewood P.F., Lewis R.J.;
RT   "Chemical and functional identification and characterization of novel
RT   sulfated alpha-conotoxins from the cone snail Conus anemone.";
RL   J. Med. Chem. 47:1234-1241(2004).
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:0000269|PubMed:14971903}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:14971903}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
CC       {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=1805.4; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:14971903};
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C1V8; -.
DR   ConoServer; 17; AnIC.
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; IPR018072; Conotoxin_a-typ_CS.
DR   PROSITE; PS60014; ALPHA_CONOTOXIN; 1.
PE   1: Evidence at protein level;
KW   Acetylcholine receptor inhibiting toxin; Amidation;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Postsynaptic neurotoxin; Secreted; Sulfation; Toxin.
FT   PEPTIDE         1..17
FT                   /note="Alpha-conotoxin-like AnIC"
FT                   /id="PRO_0000249782"
FT   REGION          5..7
FT                   /note="Ser-Xaa-Pro motif, crucial for potent interaction
FT                   with nAChR"
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   MOD_RES         16
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000269|PubMed:14971903"
FT   MOD_RES         17
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:14971903"
FT   DISULFID        3..9
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   DISULFID        4..17
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
SQ   SEQUENCE   17 AA;  1732 MW;  6DF84AFC4AD86001 CRC64;
     GGCCSHPACF ASNPDYC