ID   CA12_CONGE              Reviewed;          13 AA.
AC   P01520;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Alpha-conotoxin GII;
OS   Conus geographus (Geography cone) (Nubecula geographus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Gastridium.
OX   NCBI_TaxID=6491;
RN   [1]
RP   PROTEIN SEQUENCE, AND AMIDATION AT CYS-13.
RC   TISSUE=Venom;
RX   PubMed=7014556; DOI=10.1016/s0021-9258(19)69313-0;
RA   Gray W.R., Luque A., Olivera B.M., Barrett J., Cruz L.J.;
RT   "Peptide toxins from Conus geographus venom.";
RL   J. Biol. Chem. 256:4734-4740(1981).
CC   -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC       the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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   PIR; A01783; NTKN2G.
DR   ConoServer; 24; GII.
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; Toxin.
FT   PEPTIDE         1..13
FT                   /note="Alpha-conotoxin GII"
FT                   /id="PRO_0000044460"
FT   MOD_RES         13
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:7014556"
FT   DISULFID        2..7
FT                   /evidence="ECO:0000250|UniProtKB:P01519"
FT   DISULFID        3..13
FT                   /evidence="ECO:0000250|UniProtKB:P01519"
SQ   SEQUENCE   13 AA;  1422 MW;  DEEE831C39297EBD CRC64;
     ECCHPACGKH FSC