ID   CT5B_CONTE              Reviewed;          14 AA.
AC   P86258;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   29-SEP-2021, entry version 23.
DE   RecName: Full=Conotoxin tx5b {ECO:0000305};
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, MASS SPECTROMETRY, AND DISULFIDE
RP   BONDS.
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, SUBCELLULAR LOCATION, AND AMIDATION AT
RP   ILE-14.
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   SYNTHESIS.
RX   PubMed=23567999; DOI=10.1016/j.bcp.2013.03.019;
RA   Petrel C., Hocking H.G., Reynaud M., Upert G., Favreau P., Biass D.,
RA   Paolini-Bertrand M., Peigneur S., Tytgat J., Gilles N., Hartley O.,
RA   Boelens R., Stocklin R., Servent D.;
RT   "Identification, structural and pharmacological characterization of tau-
RT   CnVA, a conopeptide that selectively interacts with somatostatin sst
RT   receptor.";
RL   Biochem. Pharmacol. 85:1663-1671(2013).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19380747}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:19380747}.
CC   -!- DOMAIN: The cysteine framework is V (CC-CC). {ECO:0000305}.
CC   -!- PTM: Contains 2 disulfide bonds. {ECO:0000269|PubMed:19380747}.
CC   -!- PTM: Contains 2 disulfide bonds that can be either 'C1-C3, C2-C4' or
CC       'C1-C4, C2-C3', since these disulfide connectivities have been observed
CC       for conotoxins with cysteine framework V (for examples, see AC P0DQQ7
CC       and AC P81755)... {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=1447.532; Mass_error=0.02; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:19380747};
CC   -!- MISCELLANEOUS: Does not have the ability to interact with the G-protein
CC       coupled somatostatin type 3 receptor (SSTR3).
CC       {ECO:0000305|PubMed:23567999}.
CC   -!- SIMILARITY: Belongs to the conotoxin T superfamily. {ECO:0000305}.
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DR   ConoServer; 3757; Tx5b.
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   Amidation; Direct protein sequencing; Disulfide bond; Secreted; Toxin.
FT   PEPTIDE         1..14
FT                   /note="Conotoxin tx5b"
FT                   /evidence="ECO:0000269|PubMed:19380747,
FT                   ECO:0000269|PubMed:22709442"
FT                   /id="PRO_0000371267"
FT   MOD_RES         14
FT                   /note="Isoleucine amide; partial"
FT                   /evidence="ECO:0000269|PubMed:22709442"
FT   UNSURE          6
FT                   /note="I or L"
FT                   /evidence="ECO:0000305|PubMed:19380747"
FT   UNSURE          14
FT                   /note="I or L"
FT                   /evidence="ECO:0000305|PubMed:19380747"
SQ   SEQUENCE   14 AA;  1453 MW;  E233F3636FED1DA1 CRC64;
     KPCCSIHDSS CCGI