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CA11A_CONAH
ID   CA11A_CONAH             Reviewed;          64 AA.
AC   P0CAQ4; A1X8B5; A3DT43; A6M932; A6M933;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Alpha-conotoxin-like Ac1.1a;
DE   Flags: Precursor;
OS   Conus achatinus (Little frog cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX   NCBI_TaxID=369967;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
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:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha3/5 pattern.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR   EMBL; DQ359138; ABD48789.1; -; mRNA.
DR   EMBL; DQ311072; ABD33864.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0CAQ4; -.
DR   ConoServer; 562; Ac1.1a precursor.
DR   ConoServer; 570; Ac1.1a 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   2: Evidence at transcript level;
KW   Acetylcholine receptor inhibiting toxin; Amidation;
KW   Cleavage on pair of basic residues; 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..47
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000370640"
FT   PEPTIDE         48..62
FT                   /note="Alpha-conotoxin-like Ac1.1a"
FT                   /id="PRO_0000370641"
FT   MOD_RES         62
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        51..56
FT                   /evidence="ECO:0000250|UniProtKB:P01519"
FT   DISULFID        52..62
FT                   /evidence="ECO:0000250|UniProtKB:P01519"
FT   CONFLICT        36
FT                   /note="K -> I (in Ref. 1; ABD33864)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   64 AA;  7251 MW;  C4F700FF1FB18F6E CRC64;
     MGMRMMFTLF LLVVLTTTVV SYPSDSASDG RDDEAKDERS DMYELKRNGR CCHPACGKHF
     NCGR
 
 
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