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I1B5_CONRA
ID   I1B5_CONRA              Reviewed;          46 AA.
AC   Q7Z098;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Iota-conotoxin-like R11.5;
DE   Flags: Precursor; Fragment;
OS   Conus radiatus (Rayed cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Phasmoconus.
OX   NCBI_TaxID=61198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=12694387; DOI=10.1046/j.1471-4159.2003.01685.x;
RA   Jimenez E.C., Shetty R.P., Lirazan M., Rivier J., Walker C., Abogadie F.C.,
RA   Yoshikami D., Cruz L.J., Olivera B.M.;
RT   "Novel excitatory Conus peptides define a new conotoxin superfamily.";
RL   J. Neurochem. 85:610-621(2003).
CC   -!- FUNCTION: Iota-conotoxins bind to voltage-gated sodium channels (Nav)
CC       and act as agonists by shifting the voltage-dependence of activation to
CC       more hyperpolarized levels. Produces general excitatory symptoms (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The cysteine framework is XI (C-C-CC-CC-C-C).
CC   -!- SIMILARITY: Belongs to the conotoxin I1 superfamily. {ECO:0000305}.
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DR   EMBL; AY208955; AAP41537.1; -; mRNA.
DR   AlphaFoldDB; Q7Z098; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR013141; Conotoxin-I_CS.
DR   InterPro; IPR012624; Toxin_19.
DR   Pfam; PF08088; Toxin_19; 1.
DR   PROSITE; PS60019; I_CONOTOXIN; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   CHAIN           <1..45
FT                   /note="Iota-conotoxin-like R11.5"
FT                   /id="PRO_0000035102"
FT   PROPEP          46
FT                   /note="Removed by a carboxypeptidase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000035103"
FT   DISULFID        5..19
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT   DISULFID        12..22
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT   DISULFID        18..27
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT   DISULFID        21..38
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT   NON_TER         1
SQ   SEQUENCE   46 AA;  4832 MW;  3ECFBC8E501E11F5 CRC64;
     GAVPCGKDGR QCRNHADCCN CCPIGTCAPS TNWILPGCST GQFMTR
 
 
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