ID   I1BB_CONRA              Reviewed;          46 AA.
AC   Q7Z092;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Iota-conotoxin-like r11b;
DE   AltName: Full=I-superfamily conotoxin R11.14;
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], PROTEIN SEQUENCE, HYDROXYLATION AT PRO-2;
RP   PRO-11 AND PRO-29, 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   [2]
RP   SYNTHESIS, AND D-AMINO ACID AT PHE-44.
RC   TISSUE=Venom;
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   [3]
RP   ERRATUM OF PUBMED:16098199.
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). Produces excitatory
CC       symptoms when injected intracranially into mice and is lethal at higher
CC       doses. Exposure to frog cutaneous pectoris induces spontaneous and
CC       repetitive action potentials. This effect is slowly reversible. Natural
CC       peptide (with D-Phe) is active on nerve, but not on muscle. Synthetic
CC       peptide (with L-Phe) is not active on both nerve and muscle.
CC       {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-Phe form of the peptide is more potent than the
CC       synthetic L-Phe form.
CC   -!- MASS SPECTROMETRY: Mass=4857.6; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12694387};
CC   -!- SIMILARITY: Belongs to the conotoxin I1 superfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY208961; AAP41543.1; -; mRNA.
DR   AlphaFoldDB; Q7Z092; -.
DR   ConoServer; 842; RXIB.
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   D-amino acid; Direct protein sequencing; Disulfide bond; Hydroxylation;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..46
FT                   /note="Iota-conotoxin-like r11b"
FT                   /id="PRO_0000086871"
FT   MOD_RES         2
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:12694387"
FT   MOD_RES         11
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:12694387"
FT   MOD_RES         29
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:12694387"
FT   MOD_RES         44
FT                   /note="D-phenylalanine"
FT                   /evidence="ECO:0000269|PubMed:16098199"
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"
SQ   SEQUENCE   46 AA;  4819 MW;  EA48F7B3E4DA3B4E CRC64;
     GPSFCKANGK PCSYHADCCN CCLSGICKPS TNVILPGCST SSFFRI