ID   I2B2_CONSR              Reviewed;          70 AA.
AC   P0C258;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Kappa-conotoxin-like Sx11.2;
DE   Flags: Precursor;
OS   Conus striolatus (Cone snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX   NCBI_TaxID=101315;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=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   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: Modulator of potassium channels, specifically up-modulates
CC       the calcium and voltage-gated BK channels, has no effect on single
CC       channel conductance, but increases the open probability of BK channels.
CC       {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 I2 superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C258; -.
DR   SMR; P0C258; -.
DR   ConoServer; 1452; Sx11.2 precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR013141; Conotoxin-I_CS.
DR   InterPro; IPR020242; Conotoxin_I2-superfamily.
DR   Pfam; PF17557; Conotoxin_I2; 1.
DR   PROSITE; PS60019; I_CONOTOXIN; 1.
PE   2: Evidence at transcript level;
KW   Amidation; Cleavage on pair of basic residues; Disulfide bond;
KW   Gamma-carboxyglutamic acid; Hydroxylation; Ion channel impairing toxin;
KW   Neurotoxin; Potassium channel impairing toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..57
FT                   /note="Kappa-conotoxin-like Sx11.2"
FT                   /id="PRO_0000262687"
FT   PROPEP          61..70
FT                   /id="PRO_0000262688"
FT   MOD_RES         30
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         35
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         44
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         53
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         57
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        27..41
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT   DISULFID        34..46
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT   DISULFID        40..50
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT   DISULFID        45..54
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
SQ   SEQUENCE   70 AA;  7900 MW;  F6575A2E830AD903 CRC64;
     MMFRVTSVGC LLLVIVFLNL VVPTSACRAE GTYCENDSQC CLNECCWGGC GHPCRHPGKR
     SKLQEFFRQR