ID   CA1A_CONAL              Reviewed;          56 AA.
AC   P56639;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Alpha-conotoxin AuIA;
DE   Flags: Precursor;
OS   Conus aulicus (Princely cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Darioconus.
OX   NCBI_TaxID=89437;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Watkins M., Olivera B.M., Hillyard D.R., Mcintosh M.J., Jones R.M.;
RT   "Alpha-conotoxin peptides.";
RL   Patent number JP2002534996, 22-OCT-2002.
RN   [2]
RP   PROTEIN SEQUENCE OF 40-55, SYNTHESIS OF 40-55, AMIDATION AT CYS-55, MASS
RP   SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=9786965; DOI=10.1523/jneurosci.18-21-08571.1998;
RA   Luo S., Kulak J.M., Cartier G.E., Jacobsen R.B., Yoshikami D.,
RA   Olivera B.M., McIntosh J.M.;
RT   "Alpha-conotoxin AuIB selectively blocks alpha3 beta4 nicotinic
RT   acetylcholine receptors and nicotine-evoked norepinephrine release.";
RL   J. Neurosci. 18:8571-8579(1998).
CC   -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC       the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC       This toxin blocks mammalian nAChR alpha-3/beta-4 subunits.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9786965}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:9786965}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
CC   -!- MASS SPECTROMETRY: Mass=1725.6; Method=LSI;
CC       Evidence={ECO:0000269|PubMed:9786965};
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR   EMBL; BD261396; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR   PIR; A59045; A59045.
DR   AlphaFoldDB; P56639; -.
DR   ConoServer; 404; AuIA.
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   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;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..39
FT                   /evidence="ECO:0000269|PubMed:9786965"
FT                   /id="PRO_0000392689"
FT   PEPTIDE         40..55
FT                   /note="Alpha-conotoxin AuIA"
FT                   /id="PRO_0000044454"
FT   REGION          43..45
FT                   /note="Ser-Xaa-Pro motif, crucial for potent interaction
FT                   with nAChR"
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   MOD_RES         55
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:9786965"
FT   DISULFID        41..47
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   DISULFID        42..55
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
SQ   SEQUENCE   56 AA;  5886 MW;  B3BBFF7426007635 CRC64;
     MFTVFLLVVL ATTVVSFTSD RASDGRKDAA SGLIALTIKG CCSYPPCFAT NSDYCG