CM3A_CONTE
ID CM3A_CONTE Reviewed; 70 AA.
AC Q9BH73;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Conotoxin elongated-tx3a-a {ECO:0000305};
DE Contains:
DE RecName: Full=Conotoxin tx3a-b {ECO:0000305};
DE AltName: Full=Tx3a {ECO:0000303|PubMed:15924437, ECO:0000303|PubMed:17042781, ECO:0000303|PubMed:23031820};
DE Contains:
DE RecName: Full=Conotoxin tx3a-a {ECO:0000305};
DE AltName: Full=Tx3.2 {ECO:0000303|PubMed:15924437, ECO:0000303|PubMed:17042781};
DE AltName: Full=Tx3a {ECO:0000303|PubMed:15924437, ECO:0000303|PubMed:17042781, ECO:0000303|PubMed:23031820};
DE Contains:
DE RecName: Full=Conotoxin elongated-tx3a-b {ECO:0000305};
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 NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 55-70, MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, BIOASSAY, AND FUNCTION.
RC TISSUE=Venom, and Venom duct;
RX PubMed=15924437; DOI=10.1021/bi047541b;
RA Corpuz G.P., Jacobsen R.B., Jimenez E.C., Watkins M., Walker C.,
RA Colledge C., Garrett J.E., McDougal O., Li W., Gray W.R., Hillyard D.R.,
RA Rivier J., McIntosh J.M., Cruz L.J., Olivera B.M.;
RT "Definition of the M-conotoxin superfamily: characterization of novel
RT peptides from molluscivorous Conus venoms.";
RL Biochemistry 44:8176-8186(2005).
RN [3]
RP PROTEIN SEQUENCE OF 55-70, DISULFIDE BONDS, AND SYNTHESIS OF 55-70.
RC TISSUE=Venom;
RX PubMed=17042781; DOI=10.1111/j.1742-4658.2006.05493.x;
RA Han Y.-H., Wang Q., Jiang H., Liu L., Xiao C., Yuan D.-D., Shao X.-X.,
RA Dai Q.-Y., Cheng J.-S., Chi C.-W.;
RT "Characterization of novel M-superfamily conotoxins with new disulfide
RT linkage.";
RL FEBS J. 273:4972-4982(2006).
RN [4]
RP PROTEIN SEQUENCE OF 55-70, SUBCELLULAR LOCATION, MASS SPECTROMETRY,
RP DISULFIDE BONDS, AND AMIDATION AT CYS-69.
RC TISSUE=Venom;
RX PubMed=19380747; DOI=10.1073/pnas.0900745106;
RA Ueberheide B.M., Fenyo D., Alewood P.F., Chait B.T.;
RT "Rapid sensitive analysis of cysteine rich peptide venom components.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:6910-6915(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, BROMINATION AT
RP TRP-58, AND AMIDATION AT CYS-69.
RC TISSUE=Venom;
RX PubMed=22709442; DOI=10.1021/pr300312h;
RA Bhatia S., Kil Y.J., Ueberheide B., Chait B.T., Tayo L., Cruz L., Lu B.,
RA Yates J.R. III, Bern M.;
RT "Constrained de novo sequencing of conotoxins.";
RL J. Proteome Res. 11:4191-4200(2012).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, POSITION IN VENOM
RP DUCT, AND AMIDATION AT CYS-69.
RC TISSUE=Venom;
RX PubMed=23031820; DOI=10.1016/j.toxicon.2012.09.013;
RA Dobson R., Collodoro M., Gilles N., Turtoi A., De Pauw E., Quinton L.;
RT "Secretion and maturation of conotoxins in the venom ducts of Conus
RT textile.";
RL Toxicon 60:1370-1379(2012).
RN [7]
RP STRUCTURE BY NMR OF 55-69, AND DISULFIDE BONDS.
RX PubMed=18205318; DOI=10.1021/bi702388b;
RA McDougal O.M., Turner M.W., Ormond A.J., Poulter C.D.;
RT "Three-dimensional structure of conotoxin tx3a: an m-1 branch peptide of
RT the M-superfamily.";
RL Biochemistry 47:2826-2832(2008).
CC -!- FUNCTION: Intracranial injection into mice causes scratching and
CC hyperactivity. {ECO:0000269|PubMed:15924437}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15924437}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct. Is present in all duct
CC parts with a highest content in part 2 (proximal of the venom bulb) and
CC then decreases in concentration toward the end of the duct.
CC {ECO:0000305|PubMed:19380747, ECO:0000305|PubMed:23031820}.
CC -!- DOMAIN: The cysteine framework is III (CC-C-C-CC). Classified in the M-
CC 1 branch, since 1 residue stands between the fourth and the fifth
CC cysteine residues.
CC -!- PTM: Two short peptides are produced from this precursor; Conotoxin
CC tx3a-b is amidated at Cys-69 (but has no bromotryptophan), whereas
CC conotoxin tx3a-a has an unmodified Gly-70 and a bromotryptophan
CC (PubMed:15924437, PubMed:17042781, PubMed:19380747, PubMed:22709442).
CC Two elongated peptides are also produced; Conotoxin elongated-tx3a-b is
CC amidated at Cys-69 (but has no bromotryptophan), whereas conotoxin
CC elongated tx3a-a has an unmodified Gly-70 (but has no bromotryptophan)
CC (PubMed:22709442). {ECO:0000269|PubMed:15924437,
CC ECO:0000269|PubMed:17042781, ECO:0000269|PubMed:19380747,
CC ECO:0000269|PubMed:22709442}.
CC -!- MASS SPECTROMETRY: [Conotoxin tx3a-b]: Mass=1653.455; Mass_error=0.02;
CC Method=Electrospray; Note=With amidation at Cys-69.;
CC Evidence={ECO:0000269|PubMed:19380747};
CC -!- MASS SPECTROMETRY: [Conotoxin tx3a-a]: Mass=1712.5;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:15924437};
CC -!- MASS SPECTROMETRY: [Conotoxin tx3a-a]: Mass=1711.458; Mass_error=0.02;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:19380747};
CC -!- SIMILARITY: Belongs to the conotoxin M 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; AF215090; AAG60511.1; -; mRNA.
DR EMBL; AF214953; AAG60381.1; -; mRNA.
DR AlphaFoldDB; Q9BH73; -.
DR ConoServer; 640; TxIIIA precursor.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR004214; Conotoxin.
DR Pfam; PF02950; Conotoxin; 1.
PE 1: Evidence at protein level;
KW Amidation; Bromination; Direct protein sequencing; Disulfide bond;
KW Neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..44
FT /evidence="ECO:0000305|PubMed:22709442"
FT /id="PRO_0000246053"
FT PEPTIDE 45..70
FT /note="Conotoxin elongated-tx3a-a"
FT /evidence="ECO:0000305|PubMed:23031820"
FT /id="PRO_0000445119"
FT PEPTIDE 45..69
FT /note="Conotoxin elongated-tx3a-b"
FT /evidence="ECO:0000305|PubMed:23031820"
FT /id="PRO_0000445120"
FT PEPTIDE 55..70
FT /note="Conotoxin tx3a-a"
FT /evidence="ECO:0000269|PubMed:15924437,
FT ECO:0000269|PubMed:17042781, ECO:0000269|PubMed:19380747,
FT ECO:0000305|PubMed:22709442"
FT /id="PRO_0000371305"
FT PEPTIDE 55..69
FT /note="Conotoxin tx3a-b"
FT /evidence="ECO:0000269|PubMed:19380747,
FT ECO:0000305|PubMed:22709442, ECO:0000305|PubMed:23031820"
FT /id="PRO_0000246054"
FT MOD_RES 58
FT /note="6'-bromotryptophan; partial"
FT /evidence="ECO:0000269|PubMed:22709442"
FT MOD_RES 69
FT /note="Cysteine amide; partial"
FT /evidence="ECO:0000269|PubMed:15924437,
FT ECO:0000269|PubMed:17042781, ECO:0000269|PubMed:19380747,
FT ECO:0000269|PubMed:22709442, ECO:0000269|PubMed:23031820"
FT DISULFID 55..68
FT /evidence="ECO:0000269|PubMed:17042781,
FT ECO:0000269|PubMed:18205318, ECO:0000269|PubMed:19380747"
FT DISULFID 56..66
FT /evidence="ECO:0000269|PubMed:17042781,
FT ECO:0000269|PubMed:18205318, ECO:0000269|PubMed:19380747"
FT DISULFID 61..69
FT /evidence="ECO:0000269|PubMed:17042781,
FT ECO:0000269|PubMed:18205318, ECO:0000269|PubMed:19380747"
SQ SEQUENCE 70 AA; 7924 MW; 74DC2714B1AD15A2 CRC64;
MLKMGVVLFI FLVLFPLATL QLDADQPVER YAENKQLLSP DERREIILHA LGTRCCSWDV
CDHPSCTCCG
