ID   I22_CONVX               Reviewed;          67 AA.
AC   P69501; Q59AA2;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Kappa-conotoxin-like 2;
DE   Flags: Precursor;
OS   Conus vexillum (Flag cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Rhizoconus.
OX   NCBI_TaxID=89431;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=15450929; DOI=10.1016/j.toxicon.2004.07.006;
RA   Kauferstein S., Huys I., Kuch U., Melaun C., Tytgat J., Mebs D.;
RT   "Novel conopeptides of the I-superfamily occur in several clades of cone
RT   snails.";
RL   Toxicon 44:539-548(2004).
CC   -!- FUNCTION: Inhibits the vertebrate voltage-gated potassium channels
CC       Kv1.1/KCNA1 and Kv1.3/KCNA3. {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}.
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; AJ748255; CAG38082.1; -; mRNA.
DR   AlphaFoldDB; P69501; -.
DR   ConoServer; 1086; Vx11.2 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   Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW   Secreted; Signal; Toxin; Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..59
FT                   /note="Kappa-conotoxin-like 2"
FT                   /id="PRO_0000035120"
FT   PROPEP          63..67
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000035121"
FT   MOD_RES         59
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        29..43
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT   DISULFID        36..48
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT   DISULFID        42..51
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT   DISULFID        47..55
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
SQ   SEQUENCE   67 AA;  7691 MW;  4A941F6CB446F62D CRC64;
     MMFRLTSVSC FLLVIACLNL FQVVLTSRCF PPGIYCTPYL PCCWGICCDT CRNVCHLRFG
     KRATFQE