ID   I1B6_CONFI              Reviewed;          43 AA.
AC   P0C610;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Iota-conotoxin-like Fi11.6;
OS   Conus figulinus (Fig cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Dendroconus.
OX   NCBI_TaxID=101301;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=17996262; DOI=10.1016/j.toxicon.2007.09.006;
RA   Buczek O., Jimenez E.C., Yoshikami D., Imperial J.S., Watkins M.,
RA   Morrison A., Olivera B.M.;
RT   "I(1)-superfamily conotoxins and prediction of single D-amino acid
RT   occurrence.";
RL   Toxicon 51:218-229(2008).
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}.
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   AlphaFoldDB; P0C610; -.
DR   ConoServer; 2809; Fi11.6.
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   Bromination; D-amino acid; Disulfide bond; Hydroxylation;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..43
FT                   /note="Iota-conotoxin-like Fi11.6"
FT                   /id="PRO_0000314086"
FT   MOD_RES         8
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         26
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         30
FT                   /note="6'-bromotryptophan"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         41
FT                   /note="D-phenylalanine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        2..16
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT   DISULFID        9..19
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT   DISULFID        15..24
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT   DISULFID        18..35
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
SQ   SEQUENCE   43 AA;  4646 MW;  182F49CD361F1A1B CRC64;
     GCKKDRKPCS YHADCCNCCL SGICAPSTNW ILPGCSTSSF FKI