ID   U6GS_CONGE              Reviewed;          34 AA.
AC   P15472;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Mu-conotoxin GS;
DE            Short=CGS;
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, HYDROXYLATION AT PRO-10 AND PRO-11,
RP   GAMMA-CARBOXYGLUTAMATION AT GLU-32, AND FUNCTION.
RX   PubMed=2851318; DOI=10.1021/bi00417a009;
RA   Yanagawa Y., Abe T., Satake M., Odani S., Suzuki J., Ishikawa K.;
RT   "A novel sodium channel inhibitor from Conus geographus: purification,
RT   structure, and pharmacological properties.";
RL   Biochemistry 27:6256-6262(1988).
RN   [2]
RP   STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX   PubMed=9115446; DOI=10.1016/s0969-2126(97)00212-8;
RA   Hill J.M., Alewood P.F., Craik D.J.;
RT   "Solution structure of the sodium channel antagonist conotoxin GS: a new
RT   molecular caliper for probing sodium channel geometry.";
RL   Structure 5:571-583(1997).
CC   -!- FUNCTION: Mu-conotoxins block voltage-gated sodium channels (Nav). No
CC       effect was observed upon injections into mice and goldfish (25 ug).
CC       {ECO:0000269|PubMed:2851318}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
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DR   PIR; A31043; A31043.
DR   PDB; 1AG7; NMR; -; A=1-34.
DR   PDBsum; 1AG7; -.
DR   AlphaFoldDB; P15472; -.
DR   SMR; P15472; -.
DR   ConoServer; 1268; conotoxin-GS.
DR   EvolutionaryTrace; P15472; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012629; Conotoxin_TVIIAGS.
DR   Pfam; PF08094; Toxin_24; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Gamma-carboxyglutamic acid; Hydroxylation; Ion channel impairing toxin;
KW   Knottin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   PEPTIDE         1..34
FT                   /note="Mu-conotoxin GS"
FT                   /id="PRO_0000044878"
FT   MOD_RES         10
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2851318"
FT   MOD_RES         11
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:2851318"
FT   MOD_RES         32
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:2851318"
FT   DISULFID        2..14
FT                   /evidence="ECO:0000269|PubMed:9115446"
FT   DISULFID        9..19
FT                   /evidence="ECO:0000269|PubMed:9115446"
FT   DISULFID        13..27
FT                   /evidence="ECO:0000269|PubMed:9115446"
FT   STRAND          9..11
FT                   /evidence="ECO:0007829|PDB:1AG7"
FT   STRAND          17..20
FT                   /evidence="ECO:0007829|PDB:1AG7"
FT   STRAND          22..24
FT                   /evidence="ECO:0007829|PDB:1AG7"
FT   STRAND          26..29
FT                   /evidence="ECO:0007829|PDB:1AG7"
SQ   SEQUENCE   34 AA;  3548 MW;  16614FD96DB1A78C CRC64;
     ACSGRGSRCP PQCCMGLRCG RGNPQKCIGA HEDV