I2B_CONTE
ID I2B_CONTE Reviewed; 69 AA.
AC Q5I4E5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Conotoxin Gla-TxXI;
DE Flags: Precursor;
OS Conus textile (Cloth-of-gold cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Cylinder.
OX NCBI_TaxID=6494;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-56,
RP GAMMA-CARBOXYGLUTAMATION AT GLU-29, AMIDATION AT PRO-56, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom, and Venom duct;
RX PubMed=15966739; DOI=10.1021/bi0503293;
RA Brown M.A., Begley G.S., Czerwiec E., Stenberg L.M., Jacobs M.,
RA Kalume D.E., Roepstorff P., Stenflo J., Furie B.C., Furie B.;
RT "Precursors of novel Gla-containing conotoxins contain a carboxy-terminal
RT recognition site that directs gamma-carboxylation.";
RL Biochemistry 44:9150-9159(2005).
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: Contains 4 disulfide bonds.
CC -!- MASS SPECTROMETRY: Mass=3313.4; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15966739};
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; AY856070; AAW50950.1; -; mRNA.
DR AlphaFoldDB; Q5I4E5; -.
DR SMR; Q5I4E5; -.
DR ConoServer; 1057; TxXI precursor.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Secreted; Signal; Toxin.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..56
FT /note="Conotoxin Gla-TxXI"
FT /id="PRO_0000262449"
FT PROPEP 60..69
FT /id="PRO_0000262450"
FT MOD_RES 29
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:15966739"
FT MOD_RES 56
FT /note="Proline amide"
FT /evidence="ECO:0000269|PubMed:15966739"
FT DISULFID 26..40
FT /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT DISULFID 33..45
FT /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT DISULFID 39..49
FT /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT DISULFID 44..53
FT /evidence="ECO:0000250|UniProtKB:Q7Z094"
SQ SEQUENCE 69 AA; 7552 MW; 51BEA105E65A5DEE CRC64;
MVRVTSVGCF LLVIVSLNLV VLTNACIPEG SSCSSSGSCC HKSCCRWTCN QPCLIPGKRA
KLLEFFRQR