CI2_CONVR
ID CI2_CONVR Reviewed; 67 AA.
AC Q7YZS9;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Kappa-conotoxin ViTx {ECO:0000303|PubMed:12893060};
DE Short=Kappa-ViTx;
DE AltName: Full=I2-superfamily conotoxin ViTx;
DE Flags: Precursor;
GN Name=VITX;
OS Conus virgo (Virgin cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Virgiconus.
OX NCBI_TaxID=89427;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-53, SYNTHESIS OF 27-60,
RP FUNCTION, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom duct;
RX PubMed=12893060; DOI=10.1016/s0041-0101(03)00099-0;
RA Kauferstein S., Huys I., Lamthanh H., Stoecklin R., Sotto F., Menez A.,
RA Tytgat J., Mebs D.;
RT "A novel conotoxin inhibiting vertebrate voltage-sensitive potassium
RT channels.";
RL Toxicon 42:43-52(2003).
RN [2]
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).
RN [3]
RP 3D-STRUCTURE MODELING, AND DISULFIDE BONDS.
RX PubMed=16268797;
RA Mondal S., Vijayan R., Shichina K., Babu R.M., Ramakumar S.;
RT "I-superfamily conotoxins: sequence and structure analysis.";
RL In Silico Biol. 5:557-571(2005).
CC -!- FUNCTION: Kappa-conotoxins bind and inhibit voltage-gated potassium
CC channels. This toxin inhibits the mammalian potassium channels
CC Kv1.1/KCNA1 and Kv1.3/KCNA3. {ECO:0000269|PubMed:12893060}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12893060}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:12893060}.
CC -!- DOMAIN: The cysteine framework is XI (C-C-CC-CC-C-C). {ECO:0000305}.
CC -!- PTM: Contains 4 disulfide bonds. Here are reported disulfide bonds
CC proposed in [PubMed:16268797], even if the connectivity known for the
CC framework XI is I-IV, II-VI, III-VII, V-VIII.
CC -!- MASS SPECTROMETRY: Mass=3933.3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12893060};
CC -!- MISCELLANEOUS: This toxin has no effects on Kv1.2/KCNA2, Kv11/KCNH, and
CC Kir2.1/KCNJ2 potassium channels, and on Nav1.5/SCN5A sodium channels.
CC {ECO:0000305|PubMed:12893060}.
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; AJ560778; CAD90965.1; -; mRNA.
DR AlphaFoldDB; Q7YZS9; -.
DR TCDB; 8.B.21.1.8; the spider insecticidal neurotoxin cyrtautoxin (cyrautoxin) family.
DR ConoServer; 845; ViTx 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 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW Voltage-gated potassium channel impairing toxin.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:12893060"
FT CHAIN 27..59
FT /note="Kappa-conotoxin ViTx"
FT /id="PRO_0000035116"
FT PROPEP 63..67
FT /id="PRO_0000035117"
FT MOD_RES 59
FT /note="Isoleucine amide"
FT /evidence="ECO:0000305"
FT DISULFID 29..48
FT /evidence="ECO:0000305|PubMed:16268797"
FT DISULFID 36..51
FT /evidence="ECO:0000305|PubMed:16268797"
FT DISULFID 42..43
FT /evidence="ECO:0000305|PubMed:16268797"
FT DISULFID 47..55
FT /evidence="ECO:0000305|PubMed:16268797"
FT CONFLICT 38
FT /note="P -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="G -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 67 AA; 7599 MW; 46671D012446F62D CRC64;
MMFRLTSVSC FLLVIACLNL FQVVLTSRCF PPGIYCTPYL PCCWGICCGT CRNVCHLRIG
KRATFQE
