CM3H_CONTE
ID CM3H_CONTE Reviewed; 71 AA.
AC P0C1N6; Q9BPI2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=Conotoxin tx3h {ECO:0000303|PubMed:23031820};
DE AltName: Full=Conotoxin Tx3.1 {ECO:0000303|PubMed:23031820};
DE AltName: Full=TxMLKM-011 {ECO:0000312|EMBL:AAG60370.1};
DE Contains:
DE RecName: Full=Truncated conotoxin tx3h {ECO:0000305|PubMed:22709442};
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].
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].
RC TISSUE=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 53-70, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP AMIDATION AT TYR-70.
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, BROMINATION AT
RP TRP-60, AND AMIDATION AT TYR-70.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, POSITION IN VENOM
RP DUCT, AND AMIDATION AT TYR-70.
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 1 branch, since 1 residue stands between the fourth and the fifth
CC cysteine residues. {ECO:0000305}.
CC -!- PTM: Contains 3 disulfide bonds. {ECO:0000269|PubMed:19380747}.
CC -!- PTM: The truncated conotoxin tx3h exists in two forms, one is amidated,
CC whereas the other is non-amidated. The conotoxin tx3h also exists in
CC two forms, one is amidated and the other is brominated but not
CC amidated. {ECO:0000269|PubMed:22709442}.
CC -!- MASS SPECTROMETRY: [Conotoxin tx3h]: Mass=2150.684; Mass_error=0.02;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:19380747};
CC -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR EMBL; AF214942; AAG60370.1; -; mRNA.
DR AlphaFoldDB; P0C1N6; -.
DR SMR; P0C1N6; -.
DR ConoServer; 1472; Tx3h precursor.
DR ConoServer; 629; Tx3h 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; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Secreted; Signal; Toxin.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..52
FT /evidence="ECO:0000305"
FT /id="PRO_0000246049"
FT PEPTIDE 53..70
FT /note="Conotoxin tx3h"
FT /evidence="ECO:0000269|PubMed:19380747"
FT /id="PRO_0000246050"
FT PEPTIDE 54..70
FT /note="Truncated conotoxin tx3h"
FT /evidence="ECO:0000269|PubMed:22709442"
FT /id="PRO_0000445117"
FT MOD_RES 60
FT /note="6'-bromotryptophan; partial"
FT /evidence="ECO:0000269|PubMed:22709442"
FT MOD_RES 70
FT /note="Tyrosine amide; partial"
FT /evidence="ECO:0000269|PubMed:19380747,
FT ECO:0000269|PubMed:22709442, ECO:0000269|PubMed:23031820"
FT DISULFID 55..68
FT /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT DISULFID 56..66
FT /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT DISULFID 61..69
FT /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT CONFLICT 1
FT /note="M -> MM (in Ref. 1; AAG60370)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="E -> G (in Ref. 1; AAG60370)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 71 AA; 8251 MW; E6F957619216A7E0 CRC64;
MLKMGVVLFI FLVLFPLATL QLDADQPVER YAENKQLLNP DERREILLPA LRKFCCDSNW
CHISDCECCY G
