ID   CT5AP_CONTE             Reviewed;          67 AA.
AC   Q9BPG6;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Epsilon-conotoxin TxVA {ECO:0000305};
DE   AltName: Full=Conotoxin TxMRCL-011 {ECO:0000312|EMBL:AAG60390.1};
DE   AltName: Full=Epsilon-conotoxin TxIX {ECO:0000303|PubMed:10318957, ECO:0000303|PubMed:10679974};
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].
RC   TISSUE=Venom duct;
RX   PubMed=11158371; DOI=10.1093/oxfordjournals.molbev.a003786;
RA   Conticello S.G., Gilad Y., Avidan N., Ben-Asher E., Levy Z., Fainzilber M.;
RT   "Mechanisms for evolving hypervariability: the case of conopeptides.";
RL   Mol. Biol. Evol. 18:120-131(2001).
RN   [2]
RP   PROTEIN SEQUENCE OF 51-63, FUNCTION, GAMMA-CARBOXYGLUTAMATION AT GLU-51 AND
RP   GLU-54, BROMINATION AT TRP-57, HYDROXYLATION AT PRO-63, GLYCOSYLATION AT
RP   THR-60, STRUCTURE BY NMR OF 51-63, DISULFIDE BONDS, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Venom;
RX   PubMed=10318957; DOI=10.1073/pnas.96.10.5758;
RA   Rigby A.C., Lucas-Meunier E., Kalume D.E., Czerwiec E., Hambe B.,
RA   Dahlqvist I., Fossier P., Baux G., Roepstorff P., Baleja J.D., Furie B.C.,
RA   Furie B., Stenflo J.P.;
RT   "A conotoxin from Conus textile with unusual posttranslational
RT   modifications reduces presynaptic Ca2+ influx.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:5758-5763(1999).
RN   [3]
RP   PROTEIN SEQUENCE OF 51-63, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=10679974;
RX   DOI=10.1002/(sici)1096-9888(200002)35:2<145::aid-jms922>3.0.co;2-i;
RA   Kalume D.E., Stenflo J.P., Czerwiec E., Hambe B., Furie B.C., Furie B.,
RA   Roepstorff P.;
RT   "Structure determination of two conotoxins from Conus textile by a
RT   combination of matrix-assisted laser desorption/ionization time-of-flight
RT   and electrospray ionization mass spectrometry and biochemical methods.";
RL   J. Mass Spectrom. 35:145-156(2000).
CC   -!- FUNCTION: Epsilon-conotoxins act at presynaptic membranes, blocking the
CC       calcium channels or G protein-coupled receptors. Causes hyperactivity
CC       upon intracranial injection into mice. Causes dorsal fins drooping in
CC       fish. {ECO:0000269|PubMed:10318957}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10318957}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:10318957}.
CC   -!- DOMAIN: The cysteine framework is V (CC-CC). {ECO:0000305}.
CC   -!- PTM: O-glycan consists of the disaccharide Gal-GalNAc.
CC       {ECO:0000269|PubMed:10318957}.
CC   -!- MASS SPECTROMETRY: Mass=1929.43; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10679974};
CC   -!- SIMILARITY: Belongs to the conotoxin T superfamily. {ECO:0000305}.
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DR   EMBL; AF214962; AAG60390.1; -; mRNA.
DR   AlphaFoldDB; Q9BPG6; -.
DR   iPTMnet; Q9BPG6; -.
DR   ConoServer; 649; TxVA precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR031565; T-conotoxin.
DR   Pfam; PF16981; Chi-conotoxin; 1.
PE   1: Evidence at protein level;
KW   Bromination; Calcium channel impairing toxin; Direct protein sequencing;
KW   Disulfide bond; Gamma-carboxyglutamic acid; Glycoprotein; Hydroxylation;
KW   Ion channel impairing toxin; Neurotoxin; Presynaptic neurotoxin; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..50
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000404970"
FT   PEPTIDE         51..63
FT                   /note="Epsilon-conotoxin TxVA"
FT                   /evidence="ECO:0000269|PubMed:10318957,
FT                   ECO:0000269|PubMed:10679974"
FT                   /id="PRO_0000404971"
FT   PROPEP          64..67
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000404972"
FT   MOD_RES         51
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:10318957"
FT   MOD_RES         54
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:10318957"
FT   MOD_RES         57
FT                   /note="6'-bromotryptophan"
FT                   /evidence="ECO:0000269|PubMed:10318957"
FT   MOD_RES         63
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:10318957"
FT   CARBOHYD        60
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:10318957"
FT   DISULFID        52..58
FT                   /evidence="ECO:0000269|PubMed:10318957"
FT   DISULFID        53..59
FT                   /evidence="ECO:0000269|PubMed:10318957"
SQ   SEQUENCE   67 AA;  7597 MW;  7272AD7AD4D6BB3D CRC64;
     MRCFPVFIIL LLLIASAPCF DARTKTDDDV PLSPLRDNLK RTIRTRLNIR ECCEDGWCCT
     AAPLTGR