M3D_CONTE
ID M3D_CONTE Reviewed; 16 AA.
AC P86260;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Conotoxin tx3d {ECO:0000303|PubMed:23031820};
DE AltName: Full=Conotoxin 1 {ECO:0000305};
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 PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, AND POSITION IN
RP VENOM DUCT.
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).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19380747}.
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 2 branch, since 2 residues stand between the fourth and the fifth
CC cysteine residues. {ECO:0000305}.
CC -!- PTM: Contains 3 disulfide bonds. {ECO:0000269|PubMed:19380747}.
CC -!- MASS SPECTROMETRY: Mass=1591.497; Mass_error=0.02; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:19380747};
CC -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR AlphaFoldDB; P86260; -.
DR ConoServer; 3750; Tx3d.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Secreted; Toxin.
FT PEPTIDE 1..16
FT /note="Conotoxin tx3d"
FT /evidence="ECO:0000269|PubMed:19380747"
FT /id="PRO_0000371272"
FT DISULFID 2..16
FT /evidence="ECO:0000250|UniProtKB:P0CI24"
FT DISULFID 3..12
FT /evidence="ECO:0000250|UniProtKB:P0CI24"
FT DISULFID 8..15
FT /evidence="ECO:0000250|UniProtKB:P0CI24"
SQ SEQUENCE 16 AA; 1599 MW; AA31F4FFFC71A40C CRC64;
GCCGAFACRF GCTPCC