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M3F_CONTE
ID   M3F_CONTE               Reviewed;          64 AA.
AC   P0C1N7;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Conotoxin Tx3.5-a {ECO:0000303|PubMed:19380747};
DE   Contains:
DE     RecName: Full=Conotoxin tx3f {ECO:0000305};
DE     AltName: Full=Conotoxin Tx3.5-b {ECO:0000303|PubMed:19380747};
DE   Contains:
DE     RecName: Full=Truncated conotoxin tx3f {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].
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   [2]
RP   PROTEIN SEQUENCE OF 48-64, SUBCELLULAR LOCATION, MASS SPECTROMETRY,
RP   DISULFIDE BONDS, AND AMIDATION AT CYS-63.
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND AMIDATION AT
RP   CYS-63.
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, POSITION IN VENOM
RP   DUCT, AND AMIDATION AT CYS-63.
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:0000250}.
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       3 branch, since 3 residues stand between the fourth and the fifth
CC       cysteine residues.
CC   -!- PTM: Contains 3 disulfide bonds.
CC   -!- PTM: Two peptides are produced from this precursor. Conotoxin Tx3.5-b
CC       is amidated at Cys-63, conotoxin Tx3.5-a has an unmodified C-terminus.
CC       {ECO:0000269|PubMed:19380747}.
CC   -!- MASS SPECTROMETRY: [Conotoxin tx3f]: Mass=1888.707; Mass_error=0.02;
CC       Method=Electrospray; Note=With amidation at Cys-63.;
CC       Evidence={ECO:0000269|PubMed:19380747};
CC   -!- MASS SPECTROMETRY: [Conotoxin Tx3.5-a]: Mass=1946.706; 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   AlphaFoldDB; P0C1N7; -.
DR   PRIDE; P0C1N7; -.
DR   ConoServer; 1467; Tx3f 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; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..47
FT                   /evidence="ECO:0000269|PubMed:19380747"
FT                   /id="PRO_0000246051"
FT   PEPTIDE         48..64
FT                   /note="Conotoxin Tx3.5-a"
FT                   /evidence="ECO:0000269|PubMed:19380747"
FT                   /id="PRO_0000371306"
FT   PEPTIDE         48..63
FT                   /note="Conotoxin tx3f"
FT                   /evidence="ECO:0000269|PubMed:19380747,
FT                   ECO:0000269|PubMed:22709442"
FT                   /id="PRO_0000246052"
FT   PEPTIDE         49..63
FT                   /note="Truncated conotoxin tx3f"
FT                   /evidence="ECO:0000269|PubMed:22709442"
FT                   /id="PRO_0000445118"
FT   MOD_RES         63
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:19380747,
FT                   ECO:0000269|PubMed:22709442"
FT   DISULFID        49..58
FT                   /evidence="ECO:0000250"
FT   DISULFID        50..62
FT                   /evidence="ECO:0000250"
FT   DISULFID        54..63
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   64 AA;  7170 MW;  73B797E92602B541 CRC64;
     MSKLGVLLTI CLLLFPLTAL PLDGDQPADQ AAERMQAEQH PLFDQKRRCC KFPCPDSCRY
     LCCG
 
 
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