ID   CA1E_CONRE              Reviewed;          12 AA.
AC   P85011;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   23-FEB-2022, entry version 37.
DE   RecName: Full=Alpha-conotoxin-like Reg1e {ECO:0000303|PubMed:17153339};
OS   Conus regius (Crown cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Stephanoconus.
OX   NCBI_TaxID=101314;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, HYDROXYLATION
RP   AT PRO-6, AND AMIDATION AT CYS-12.
RC   TISSUE=Venom;
RX   PubMed=17153339; DOI=10.1007/978-3-540-30880-5_4;
RA   Franco A., Pisarewicz K., Moller C., Mora D., Fields G.B., Mari F.;
RT   "Hyperhydroxylation: a new strategy for neuronal targeting by venomous
RT   marine molluscs.";
RL   Prog. Mol. Subcell. Biol. 43:83-103(2006).
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:P50983}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17153339}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000269|PubMed:17153339}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/3 pattern.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
CC   -!- CAUTION: Has the same mature sequence than RgIA (AC P0C1D0). RgIA could
CC       therefore be the precursor of Reg1e, except that RgIA does not have the
CC       C-terminal Gly residue required for C-terminal amidation of Reg1e.
CC       {ECO:0000305}.
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DR   ConoServer; 30; RgIA [P6O,del13].
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; Hydroxylation;
KW   Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW   Toxin.
FT   PEPTIDE         1..12
FT                   /note="Alpha-conotoxin-like Reg1e"
FT                   /evidence="ECO:0000269|PubMed:17153339"
FT                   /id="PRO_0000259387"
FT   MOD_RES         6
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:17153339"
FT   MOD_RES         12
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:17153339"
FT   DISULFID        2..8
FT                   /evidence="ECO:0000250|UniProtKB:P0C1D0"
FT   DISULFID        3..12
FT                   /evidence="ECO:0000250|UniProtKB:P0C1D0"
SQ   SEQUENCE   12 AA;  1419 MW;  9C29C69C95A4176A CRC64;
     GCCSDPRCRY RC