ID   I1BC_CONRA              Reviewed;          80 AA.
AC   Q7Z096;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Iota-conotoxin-like r11c;
DE   AltName: Full=R11.4;
DE   Flags: Precursor;
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], SYNTHESIS OF 37-79, AND D-AMINO ACID AT LEU-78.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=16098199; DOI=10.1111/j.1742-4658.2005.04830.x;
RA   Buczek O., Yoshikami D., Watkins M., Bulaj G., Jimenez E.C., Olivera B.M.;
RT   "Characterization of D-amino-acid-containing excitatory conotoxins and
RT   redefinition of the I-conotoxin superfamily.";
RL   FEBS J. 272:4178-4188(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 37-80, PROTEIN SEQUENCE OF 37-79,
RP   HYDROXYLATION AT PRO-38; PRO-47 AND PRO-65, AND MASS SPECTROMETRY.
RC   TISSUE=Venom, and 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).
RN   [3]
RP   ERRATUM OF PUBMED:12694387.
RA   Buczek O., Yoshikami D., Watkins M., Bulaj G., Jimenez E.C., Olivera B.M.;
RL   FEBS J. 272:4839-4839(2005).
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 (By similarity). Causes circular motion,
CC       convulsions, copious urination, rigid paralysis and death upon
CC       intracranial injection into mice. Causes unbalanced swimming, swimming
CC       in diagonal and vertical motion and death, when injected
CC       intraperitoneally into goldfish. L-Leu and D-Leu forms are active on
CC       both nerve and muscle. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The cysteine framework is XI (C-C-CC-CC-C-C).
CC   -!- PTM: The natural D-Leu form of the peptide is more potent than the
CC       synthetic L-Leu form.
CC   -!- MASS SPECTROMETRY: Mass=4632.68; Method=MALDI; Note=With hydroxyPro.;
CC       Evidence={ECO:0000269|PubMed:12694387};
CC   -!- MASS SPECTROMETRY: Mass=4616.62; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12694387};
CC   -!- SIMILARITY: Belongs to the conotoxin I1 superfamily. {ECO:0000305}.
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DR   EMBL; AY208957; AAP41539.1; -; mRNA.
DR   AlphaFoldDB; Q7Z096; -.
DR   SMR; Q7Z096; -.
DR   ConoServer; 1409; RXIC precursor.
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   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; D-amino acid;
KW   Direct protein sequencing; Disulfide bond; Hydroxylation;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..35
FT                   /id="PRO_0000262448"
FT   CHAIN           37..79
FT                   /note="Iota-conotoxin-like r11c"
FT                   /id="PRO_0000035100"
FT   PROPEP          80
FT                   /note="Removed by a carboxypeptidase"
FT                   /id="PRO_0000035101"
FT   MOD_RES         38
FT                   /note="4-hydroxyproline; partial"
FT                   /evidence="ECO:0000269|PubMed:12694387"
FT   MOD_RES         47
FT                   /note="4-hydroxyproline; partial"
FT                   /evidence="ECO:0000269|PubMed:12694387"
FT   MOD_RES         65
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:12694387"
FT   MOD_RES         78
FT                   /note="D-leucine"
FT                   /evidence="ECO:0000269|PubMed:16098199"
FT   DISULFID        41..55
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT   DISULFID        48..58
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT   DISULFID        54..63
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT   DISULFID        57..72
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
SQ   SEQUENCE   80 AA;  8744 MW;  12A793215AA85418 CRC64;
     MKLCLTFLLV LMILASVTGE KSSKHTLSRA ARVKNRGPSF CKADEKPCKY HADCCNCCLG
     GICKPSTSWI GCSTNVFLTR