I3B1_CONGE
ID I3B1_CONGE Reviewed; 77 AA.
AC X5IY26;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Conotoxin G11.1 {ECO:0000305};
DE AltName: Full=Conotoxin G117 {ECO:0000303|PubMed:24662800, ECO:0000303|PubMed:33530397};
DE AltName: Full=Conotoxin GXIA {ECO:0000303|PubMed:33530397};
DE Flags: Precursor;
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] {ECO:0000312|EMBL:BAO65650.1}
RP NUCLEOTIDE SEQUENCE [MRNA], ISOLATION, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom duct;
RX PubMed=24662800; DOI=10.1038/ncomms4521;
RA Dutertre S., Jin A.-H., Vetter I., Hamilton B., Sunagar K., Lavergne V.,
RA Dutertre V., Fry B.G., Antunes A., Venter D.J., Alewood P.F., Lewis R.J.;
RT "Evolution of separate predation- and defence-evoked venoms in carnivorous
RT cone snails.";
RL Nat. Commun. 5:3521-3521(2014).
RN [2] {ECO:0007744|PDB:6CEI}
RP STRUCTURE BY NMR OF 46-77, AND DISULFIDE BONDS.
RX PubMed=33530397; DOI=10.3390/md19020060;
RA Armstrong D.A., Jin A.H., Braga Emidio N., Lewis R.J., Alewood P.F.,
RA Rosengren K.J.;
RT "Chemical synthesis and NMR solution structure of conotoxin GXIA from Conus
RT geographus.";
RL Mar. Drugs 19:0-0(2021).
CC -!- FUNCTION: May embed in the membrane and bind to the voltage sensor
CC domain of a ion channel (PubMed:24662800). Does not induce paralysis
CC when injected in fish, leading to the hypothesis that it may be part of
CC the sedative nirvana cabal (Probable). {ECO:0000269|PubMed:24662800,
CC ECO:0000305|PubMed:33530397}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24662800}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:24662800}.
CC -!- DOMAIN: The cysteine framework is XI (C-C-CC-CC-C-C). {ECO:0000305}.
CC -!- DOMAIN: Adopts an inhibitor cystine knot (ICK) fold. Has 4 disulfide
CC bonds (ICK+1). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the conotoxin I3 superfamily. {ECO:0000305}.
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DR EMBL; AB910882; BAO65650.1; -; mRNA.
DR PDB; 6CEI; NMR; -; A=46-77.
DR PDBsum; 6CEI; -.
DR AlphaFoldDB; X5IY26; -.
DR BMRB; X5IY26; -.
DR SMR; X5IY26; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR013141; Conotoxin-I_CS.
DR PROSITE; PS60019; I_CONOTOXIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues; Disulfide bond;
KW Ion channel impairing toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..45
FT /evidence="ECO:0000250|UniProtKB:D2DGD4"
FT /id="PRO_0000448283"
FT PEPTIDE 46..77
FT /note="Conotoxin G11.1"
FT /id="PRO_5004957649"
FT DISULFID 46..60
FT /evidence="ECO:0000269|PubMed:33530397,
FT ECO:0007744|PDB:6CEI"
FT DISULFID 53..65
FT /evidence="ECO:0000269|PubMed:33530397,
FT ECO:0007744|PDB:6CEI"
FT DISULFID 59..69
FT /evidence="ECO:0000269|PubMed:33530397,
FT ECO:0007744|PDB:6CEI"
FT DISULFID 64..76
FT /evidence="ECO:0000269|PubMed:33530397,
FT ECO:0007744|PDB:6CEI"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:6CEI"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:6CEI"
SQ SEQUENCE 77 AA; 8339 MW; 903EE8056146F82B CRC64;
MKLFLAIVLI LMLQFLSTGA ETSDNHASRS TTALRDWLLG PKAKRCAVTH EKCSDDYDCC
GSLCCVGICA KTIAPCK
