ID   I1BD_CONRA              Reviewed;          41 AA.
AC   Q7Z091;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Iota-conotoxin-like r11d;
DE   AltName: Full=R11.8;
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-8 AND
RP   PRO-26, 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   PROTEIN SEQUENCE, SYNTHESIS OF [L-THR-41]R11D AND [D-THR-41]R11D, AND
RP   FUNCTION.
RC   TISSUE=Venom;
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 (By similarity). Both natural (L-Thr form)
CC       and synthetic (D-Thr form) peptides cause paralysis and death following
CC       intracranial injection and grooming and hypersensitivity upon
CC       intraperitoneal injection into mice. The L-Thr form of the peptide is
CC       7-fold more potent than the D-Thr form. Both natural peptide (L-Thr
CC       form) and synthetic peptide (D-Thr form) are active on nerve, and on
CC       muscle. {ECO:0000250, ECO:0000269|PubMed:17996262}.
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: Position 41 corresponds to a L-threonine, and not a D-threonine as
CC       firstly supposed.
CC   -!- MASS SPECTROMETRY: Mass=4399.26; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12694387};
CC   -!- SIMILARITY: Belongs to the conotoxin I1 superfamily. {ECO:0000305}.
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DR   EMBL; AY208962; AAP41544.1; -; mRNA.
DR   AlphaFoldDB; Q7Z091; -.
DR   SMR; Q7Z091; -.
DR   ConoServer; 843; RXID.
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   Direct protein sequencing; Disulfide bond; Hydroxylation;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..41
FT                   /note="Iota-conotoxin-like r11d"
FT                   /id="PRO_0000086870"
FT   MOD_RES         8
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:12694387"
FT   MOD_RES         26
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:12694387"
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   41 AA;  4373 MW;  B1AD320F1A1B5B31 CRC64;
     GCKKDRKPCS YHADCCNCCL SGICAPSTNW ILPGCSTSTF T