CP91_CONGL
ID CP91_CONGL Reviewed; 88 AA.
AC Q9GU57;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Conotoxin Gm9.1 {ECO:0000303|PubMed:10677206};
DE AltName: Full=Conotoxin Gm9a {ECO:0000303|PubMed:12193600};
DE AltName: Full=Spasmodic peptide {ECO:0000303|PubMed:10677206, ECO:0000303|PubMed:12193600};
DE Flags: Precursor;
OS Conus gloriamaris (Glory-of-the-Sea cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Cylinder.
OX NCBI_TaxID=37336;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT ASN-87.
RC TISSUE=Venom duct;
RX PubMed=10677206; DOI=10.1021/bi9923712;
RA Lirazan M.B., Hooper D., Corpuz G.P., Ramilo C.A., Bandyopadhyay P.,
RA Cruz L.J., Olivera B.M.;
RT "The spasmodic peptide defines a new conotoxin superfamily.";
RL Biochemistry 39:1583-1588(2000).
RN [2]
RP SYNTHESIS OF 61-87, FUNCTION, STRUCTURE BY NMR OF 61-87, AND DISULFIDE
RP BONDS.
RX PubMed=12193600; DOI=10.1074/jbc.m206690200;
RA Miles L.A., Dy C.Y., Nielsen J., Barnham K.J., Hinds M.G., Olivera B.M.,
RA Bulaj G., Norton R.S.;
RT "Structure of a novel P-superfamily spasmodic conotoxin reveals an
RT inhibitory cystine knot motif.";
RL J. Biol. Chem. 277:43033-43040(2002).
CC -!- FUNCTION: Neurotoxin. In vivo, elicits 'spasmodic' symptomatology.
CC {ECO:0000269|PubMed:12193600}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:10677206}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:10677206}.
CC -!- DOMAIN: The cysteine framework is IX (C-C-C-C-C-C). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the conotoxin P superfamily. {ECO:0000305}.
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DR EMBL; AF193511; AAG28407.1; -; mRNA.
DR PDB; 1IXT; NMR; -; A=61-87.
DR PDB; 2MSO; NMR; -; A=61-88.
DR PDBsum; 1IXT; -.
DR PDBsum; 2MSO; -.
DR AlphaFoldDB; Q9GU57; -.
DR BMRB; Q9GU57; -.
DR SMR; Q9GU57; -.
DR TCDB; 8.B.22.1.1; the p-conotoxin cystine knot (p-cck) family.
DR ConoServer; 609; GmIXA precursor.
DR EvolutionaryTrace; Q9GU57; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR010012; Toxin_11.
DR Pfam; PF07473; Toxin_11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amidation; Cleavage on pair of basic residues;
KW Disulfide bond; Neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..58
FT /evidence="ECO:0000305"
FT /id="PRO_0000035013"
FT PEPTIDE 61..87
FT /note="Conotoxin Gm9.1"
FT /evidence="ECO:0000305|PubMed:12193600"
FT /id="PRO_0000035014"
FT MOD_RES 87
FT /note="Asparagine amide"
FT /evidence="ECO:0000269|PubMed:10677206"
FT DISULFID 62..76
FT /evidence="ECO:0000269|PubMed:12193600,
FT ECO:0007744|PDB:1IXT, ECO:0007744|PDB:2MSO"
FT DISULFID 66..78
FT /evidence="ECO:0000269|PubMed:12193600,
FT ECO:0007744|PDB:1IXT, ECO:0007744|PDB:2MSO"
FT DISULFID 72..83
FT /evidence="ECO:0000269|PubMed:12193600,
FT ECO:0007744|PDB:1IXT, ECO:0007744|PDB:2MSO"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1IXT"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:1IXT"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:1IXT"
SQ SEQUENCE 88 AA; 9687 MW; C82818A55CBC44E7 CRC64;
MHLSLARSAV LMLLLLFALG NFVVVQSGLI TRDVDNGQLT DNRRNLQTEW NPLSLFMSRR
SCNNSCQSHS DCASHCICTF RGCGAVNG
