I2B_CONBE
ID I2B_CONBE Reviewed; 70 AA.
AC Q9U3Z3;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Kappa-conotoxin BtX {ECO:0000303|PubMed:12547831};
DE AltName: Full=BeTx {ECO:0000312|EMBL:AAF23167.1};
DE Flags: Precursor;
OS Conus betulinus (Beech cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Dendroconus.
OX NCBI_TaxID=89764;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-43, FUNCTION, MASS
RP SPECTROMETRY, HYDROXYLATION AT PRO-53, GAMMA-CARBOXYGLUTAMATION AT GLU-30;
RP GLU-35 AND GLU-44, AMIDATION AT PRO-57, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom duct;
RX PubMed=12547831; DOI=10.1074/jbc.m210200200;
RA Fan C.-X., Chen X.-K., Zhang C., Wang L.-X., Duan K.-L., He L.-L., Cao Y.,
RA Liu S.-Y., Zhong M.-N., Ulens C., Tytgat J., Chen J.-S., Chi C.-W.,
RA Zhou Z.;
RT "A novel conotoxin from Conus betulinus, kappa-BtX, unique in cysteine
RT pattern and in function as a specific BK channel modulator.";
RL J. Biol. Chem. 278:12624-12633(2003).
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:0000269|PubMed:12547831}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12547831}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:12547831}.
CC -!- DOMAIN: The cysteine framework is XI (C-C-CC-CC-C-C). {ECO:0000305}.
CC -!- PTM: Contains 4 disulfide bonds. {ECO:0000269|PubMed:12547831}.
CC -!- MASS SPECTROMETRY: Mass=3569; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12547831};
CC -!- SIMILARITY: Belongs to the conotoxin I2 superfamily. {ECO:0000305}.
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DR EMBL; AF208661; AAF23167.1; -; mRNA.
DR AlphaFoldDB; Q9U3Z3; -.
DR SMR; Q9U3Z3; -.
DR TCDB; 8.B.21.1.9; the spider insecticidal neurotoxin cyrtautoxin (cyrautoxin) family.
DR ConoServer; 1106; BtX 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; Gamma-carboxyglutamic acid; Hydroxylation;
KW Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW Secreted; Signal; Toxin.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:12547831"
FT PEPTIDE 27..57
FT /note="Kappa-conotoxin BtX"
FT /id="PRO_0000035086"
FT PROPEP 61..70
FT /id="PRO_0000035087"
FT MOD_RES 30
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12547831"
FT MOD_RES 35
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12547831"
FT MOD_RES 44
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:12547831"
FT MOD_RES 53
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:12547831"
FT MOD_RES 57
FT /note="Proline amide"
FT /evidence="ECO:0000269|PubMed:12547831"
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