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Epsilon-conotoxin TxVA (Tx-012) (Tx5.2) (TxIX) (tx5a)

 CT5A_CONTE              Reviewed;          67 AA.
P81755; Q9U6Z7;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
06-JUN-2002, sequence version 2.
23-MAY-2018, entry version 88.
RecName: Full=Epsilon-conotoxin TxVA {ECO:0000305};
AltName: Full=Epsilon-TxIX {ECO:0000303|PubMed:10318957, ECO:0000303|PubMed:10679974};
AltName: Full=Tx-012 {ECO:0000312|EMBL:AAG60386.1};
AltName: Full=Tx5.2 {ECO:0000303|PubMed:10521453};
AltName: Full=tx5a {ECO:0000303|PubMed:10521453};
Flags: Precursor;
Conus textile (Cloth-of-gold cone).
Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda;
Caenogastropoda; Hypsogastropoda; Neogastropoda; Conoidea; Conidae;
Conus; Cylinder.
NCBI_TaxID=6494;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 51-63, MASS
SPECTROMETRY, SUBCELLULAR LOCATION, GAMMA-CARBOXYGLUTAMATION AT GLU-51
AND GLU-54, BROMINATION AT TRP-57, HYDROXYLATION AT PRO-63, AND
GLYCOSYLATION AT THR-60.
TISSUE=Venom, and Venom duct;
PubMed=10521453; DOI=10.1074/jbc.274.43.30664;
Walker C.S., Steel D., Jacobsen R.B., Lirazan M.B., Cruz L.J.,
Hooper D., Shetty R., DelaCruz R.C., Nielsen J.S., Zhou L.M.,
Bandyopadhyay P., Craig A.G., Olivera B.M.;
"The T-superfamily of conotoxins.";
J. Biol. Chem. 274:30664-30671(1999).
[2]
ERRATUM.
Walker C.S., Steel D., Jacobsen R.B., Lirazan M.B., Cruz L.J.,
Hooper D., Shetty R., DelaCruz R.C., Nielsen J.S., Zhou L.M.,
Bandyopadhyay P., Craig A.G., Olivera B.M.;
J. Biol. Chem. 274:36030-36030(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom duct;
PubMed=11158371; DOI=10.1093/oxfordjournals.molbev.a003786;
Conticello S.G., Gilad Y., Avidan N., Ben-Asher E., Levy Z.,
Fainzilber M.;
"Mechanisms for evolving hypervariability: the case of conopeptides.";
Mol. Biol. Evol. 18:120-131(2001).
[4]
PROTEIN SEQUENCE OF 51-63, FUNCTION, GLYCOSYLATION AT THR-60,
GAMMA-CARBOXYGLUTAMATION AT GLU-51 AND GLU-54, BROMINATION AT TRP-57,
HYDROXYLATION AT PRO-63, STRUCTURE BY NMR OF 51-63, AND DISULFIDE
BONDS.
TISSUE=Venom;
PubMed=10318957; DOI=10.1073/pnas.96.10.5758;
Rigby A.C., Lucas-Meunier E., Kalume D.E., Czerwiec E., Hambe B.,
Dahlqvist I., Fossier P., Baux G., Roepstorff P., Baleja J.D.,
Furie B.C., Furie B., Stenflo J.P.;
"A conotoxin from Conus textile with unusual posttranslational
modifications reduces presynaptic Ca2+ influx.";
Proc. Natl. Acad. Sci. U.S.A. 96:5758-5763(1999).
[5]
PROTEIN SEQUENCE OF 51-63, AND MASS SPECTROMETRY.
TISSUE=Venom;
PubMed=10679974;
DOI=10.1002/(SICI)1096-9888(200002)35:2<145::AID-JMS922>3.0.CO;2-I;
Kalume D.E., Stenflo J.P., Czerwiec E., Hambe B., Furie B.C.,
Furie B., Roepstorff P.;
"Structure determination of two conotoxins from Conus textile by a
combination of matrix-assisted laser desorption/ionization time-of-
flight and electrospray ionization mass spectrometry and biochemical
methods.";
J. Mass Spectrom. 35:145-156(2000).
-!- FUNCTION: Epsilon-conotoxins act at presynaptic membranes,
blocking the calcium channels or G protein-coupled receptors.
Causes hyperactivity upon intracranial injection into mice. Causes
dorsal fins drooping in fish. {ECO:0000269|PubMed:10318957}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10521453}.
-!- TISSUE SPECIFICITY: Expressed by the venom duct.
{ECO:0000305|PubMed:10521453}.
-!- DOMAIN: The cysteine framework is V (CC-CC). {ECO:0000305}.
-!- PTM: O-glycan consists of the disaccharide Gal-GalNAc.
{ECO:0000269|PubMed:10318957}.
-!- MASS SPECTROMETRY: Mass=1929.4; Method=Electrospray; Range=51-63;
Evidence={ECO:0000269|PubMed:10521453,
ECO:0000269|PubMed:10679974};
-!- MASS SPECTROMETRY: Mass=1929.43; Method=MALDI; Range=51-63;
Evidence={ECO:0000269|PubMed:10521453,
ECO:0000269|PubMed:10679974};
-!- SIMILARITY: Belongs to the conotoxin T superfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF167167; AAF03687.1; -; mRNA.
EMBL; AF214958; AAG60386.1; -; mRNA.
PIR; E59147; E59147.
PDB; 1WCT; NMR; -; A=51-63.
PDBsum; 1WCT; -.
SMR; P81755; -.
iPTMnet; P81755; -.
ConoServer; 645; TxVA precursor.
EvolutionaryTrace; P81755; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0072556; C:other organism presynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
InterPro; IPR031565; T-conotoxin.
Pfam; PF16981; Chi-conotoxin; 1.
1: Evidence at protein level;
3D-structure; Bromination; Calcium channel impairing toxin;
Direct protein sequencing; Disulfide bond; Gamma-carboxyglutamic acid;
Glycoprotein; Hydroxylation; Ion channel impairing toxin; Neurotoxin;
Presynaptic neurotoxin; Secreted; Signal; Toxin.
SIGNAL 1 19 {ECO:0000255}.
PROPEP 20 50 {ECO:0000269|PubMed:10318957,
ECO:0000269|PubMed:10521453,
ECO:0000269|PubMed:10679974}.
/FTId=PRO_0000035016.
PEPTIDE 51 63 Epsilon-conotoxin TxVA.
{ECO:0000269|PubMed:10318957,
ECO:0000269|PubMed:10521453,
ECO:0000269|PubMed:10679974}.
/FTId=PRO_0000035017.
PROPEP 64 67 {ECO:0000269|PubMed:10318957,
ECO:0000269|PubMed:10521453,
ECO:0000269|PubMed:10679974}.
/FTId=PRO_0000035018.
MOD_RES 51 51 4-carboxyglutamate.
{ECO:0000269|PubMed:10318957,
ECO:0000269|PubMed:10521453}.
MOD_RES 54 54 4-carboxyglutamate.
{ECO:0000269|PubMed:10318957,
ECO:0000269|PubMed:10521453}.
MOD_RES 57 57 6'-bromotryptophan.
{ECO:0000269|PubMed:10318957,
ECO:0000269|PubMed:10521453}.
MOD_RES 63 63 4-hydroxyproline.
{ECO:0000269|PubMed:10318957,
ECO:0000269|PubMed:10521453}.
CARBOHYD 60 60 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:10318957,
ECO:0000269|PubMed:10521453}.
DISULFID 52 58 {ECO:0000269|PubMed:10318957}.
DISULFID 53 59 {ECO:0000269|PubMed:10318957}.
TURN 53 56 {ECO:0000244|PDB:1WCT}.
SEQUENCE 67 AA; 7587 MW; 7270505504D6BB3D CRC64;
MRCFPVFIIL LLLIASAPCF DARTKTDDDV PLSSLRDNLK RTIRTRLNIR ECCEDGWCCT
AAPLTGR


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