ID   CAL12_CONPE             Reviewed;          61 AA.
AC   Q9BP56;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Alpha-conotoxin-like PnMGMR-02;
DE   Flags: Precursor;
OS   Conus pennaceus (Feathered cone) (Conus episcopus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Darioconus.
OX   NCBI_TaxID=37335;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=11158371; DOI=10.1093/oxfordjournals.molbev.a003786;
RA   Conticello S.G., Gilad Y., Avidan N., Ben-Asher E., Levy Z., Fainzilber M.;
RT   "Mechanisms for evolving hypervariability: the case of conopeptides.";
RL   Mol. Biol. Evol. 18:120-131(2001).
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 nAChRs (alpha-7 > alpha-3/beta-2) (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:11158371}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:11158371}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR   EMBL; AF215089; AAG60510.1; -; mRNA.
DR   AlphaFoldDB; Q9BP56; -.
DR   ConoServer; 37; PnMGMR-02 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   InterPro; IPR018072; Conotoxin_a-typ_CS.
DR   Pfam; PF07365; Toxin_8; 1.
DR   PROSITE; PS60014; ALPHA_CONOTOXIN; 1.
PE   3: Inferred from homology;
KW   Acetylcholine receptor inhibiting toxin; Amidation; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW   Signal; Sulfation; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..44
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000404874"
FT   PEPTIDE         45..60
FT                   /note="Alpha-conotoxin-like PnMGMR-02"
FT                   /id="PRO_0000404875"
FT   REGION          48..50
FT                   /note="Ser-Xaa-Pro motif, crucial for potent interaction
FT                   with nAChR"
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   SITE            54
FT                   /note="Direct interaction with nAChR alpha-7 subunit"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         60
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        46..52
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   DISULFID        47..60
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
SQ   SEQUENCE   61 AA;  6348 MW;  6FCFD3333D306921 CRC64;
     MGMRMMFTVF LLVVLATTVV SFTSDRASDG GNAAASDLIA LTIKGCCSRP PCALSNPDYC
     G