ID   CEX_CONCN               Reviewed;          30 AA.
AC   P58928;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   12-OCT-2022, entry version 64.
DE   RecName: Full=Conotoxin CcTx;
DE   AltName: Full=Excitotoxin CcTx;
OS   Conus consors (Singed cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX   NCBI_TaxID=101297;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, HYDROXYLATION AT PRO-2; PRO-17 AND PRO-22, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=10510177; DOI=10.1046/j.1460-9568.1999.00732.x;
RA   Le Gall F., Favreau P., Benoit E., Mattei C., Bouet F., Menou J.-L.,
RA   Menez A., Letourneux Y., Molgo J.;
RT   "A new conotoxin isolated from Conus consors venom acting selectively on
RT   axons and motor nerve terminals through a Na+-dependent mechanism.";
RL   Eur. J. Neurosci. 11:3134-3142(1999).
RN   [2]
RP   SEQUENCE REVISION TO 7, AND GLYCOSYLATION AT SER-7.
RX   PubMed=19457347; DOI=10.1016/j.jprot.2009.01.019;
RA   Biass D., Dutertre S., Gerbault A., Menou J.L., Offord R., Favreau P.,
RA   Stocklin R.;
RT   "Comparative proteomic study of the venom of the piscivorous cone snail
RT   Conus consors.";
RL   J. Proteomics 72:210-218(2009).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY OF GLYCOSYLATED AND NON-GLYCOSYLATED
RP   FORMS.
RC   TISSUE=Venom;
RX   PubMed=22705119; DOI=10.1016/j.jprot.2012.06.001;
RA   Violette A., Biass D., Dutertre S., Koua D., Piquemal D., Pierrat F.,
RA   Stocklin R., Favreau P.;
RT   "Large-scale discovery of conopeptides and conoproteins in the injectable
RT   venom of a fish-hunting cone snail using a combined proteomic and
RT   transcriptomic approach.";
RL   J. Proteomics 75:5215-5225(2012).
RN   [4] {ECO:0007744|PDB:4B1Q}
RP   STRUCTURE BY NMR, MASS SPECTROMETRY, DISULFIDE BONDS, AND GLYCOSYLATION AT
RP   SER-7.
RX   PubMed=23281027; DOI=10.1002/chem.201202713;
RA   Hocking H.G., Gerwig G.J., Dutertre S., Violette A., Favreau P.,
RA   Stocklin R., Kamerling J.P., Boelens R.;
RT   "Structure of the O-glycosylated conopeptide CcTx from Conus consors
RT   venom.";
RL   Chemistry 19:870-879(2013).
CC   -!- FUNCTION: May specifically activate neuronal voltage-gated sodium
CC       channels (Nav) at the resting membrane potential. Causes a marked
CC       contraction and extension of the caudal and dorsal fins in fish and
CC       noticeable spontaneous contractions of isolated frog neuromuscular
CC       preparations. {ECO:0000269|PubMed:10510177}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10510177}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000269|PubMed:10510177}.
CC   -!- DOMAIN: The cysteine framework is IV (CC-C-C-C-C).
CC   -!- PTM: O-glycosylated at Ser-7 by a core type 9 glycan, containing both
CC       D- and L-galactose units (alpha-L-Galp-(1->4)-alpha-D- GlcpNAc-(1->6)-
CC       [alpha-L-Galp-(1->2)-bets-D-Galp-(1->3)-]alpha-D-GalpNAc-(1->O)).
CC       {ECO:0000269|PubMed:23281027}.
CC   -!- MASS SPECTROMETRY: Mass=3223; Method=Electrospray; Note=Non-
CC       glycosylated form.; Evidence={ECO:0000269|PubMed:23281027};
CC   -!- MASS SPECTROMETRY: Mass=4156; Method=Electrospray; Note=Glycosylated
CC       form.; Evidence={ECO:0000269|PubMed:10510177};
CC   -!- MISCELLANEOUS: Found in both injectable (milked) (IV) and dissected
CC       venom (DV). {ECO:0000305|PubMed:19457347}.
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DR   PDB; 4B1Q; NMR; -; P=1-30.
DR   PDBsum; 4B1Q; -.
DR   AlphaFoldDB; P58928; -.
DR   BMRB; P58928; -.
DR   SMR; P58928; -.
DR   iPTMnet; P58928; -.
DR   ConoServer; 1510; CcTx.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0044231; C:host cell presynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hydroxylation; Ion channel impairing toxin; Neurotoxin;
KW   Presynaptic neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   PEPTIDE         1..30
FT                   /note="Conotoxin CcTx"
FT                   /id="PRO_0000044514"
FT   MOD_RES         2
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:10510177"
FT   MOD_RES         17
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:10510177"
FT   MOD_RES         22
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:10510177"
FT   CARBOHYD        7
FT                   /note="O-linked (HexNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:19457347,
FT                   ECO:0000269|PubMed:23281027"
FT   DISULFID        12..21
FT                   /evidence="ECO:0000269|PubMed:23281027,
FT                   ECO:0007744|PDB:4B1Q"
FT   DISULFID        13..26
FT                   /evidence="ECO:0000269|PubMed:23281027,
FT                   ECO:0007744|PDB:4B1Q"
FT   DISULFID        24..30
FT                   /evidence="ECO:0000269|PubMed:23281027,
FT                   ECO:0007744|PDB:4B1Q"
FT   HELIX           23..26
FT                   /evidence="ECO:0007829|PDB:4B1Q"
SQ   SEQUENCE   30 AA;  3184 MW;  AD8E9CC5ABB0E065 CRC64;
     APWLVPSQIT TCCGYNPGTM CPSCMCTNTC
//