ID   CTAC_CONTE              Reviewed;          12 AA.
AC   P86257;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   22-APR-2020, entry version 21.
DE   RecName: Full=Chi-conotoxin-like 2 {ECO:0000305};
DE   AltName: Full=Tx10c {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, DISULFIDE BONDS,
RP   PYROGLUTAMATE FORMATION AT GLN-1, OXIDATION AT MET-8, HYDROXYLATION AT
RP   PRO-11, AND AMIDATION AT CYS-12.
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, HYDROXYLATION AT
RP   PRO-11, AND AMIDATION AT CYS-12.
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).
CC   -!- FUNCTION: Chi-conotoxins inhibit the neuronal noradrenaline transporter
CC       (NET/SLC6A2). {ECO:0000250|UniProtKB:P58808}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19380747,
CC       ECO:0000269|PubMed:22709442}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:19380747, ECO:0000305|PubMed:22709442}.
CC   -!- DOMAIN: The cysteine framework is X (CC-CX[hydroxyPro]C).
CC       {ECO:0000305}.
CC   -!- PTM: Contains 2 disulfide bonds. {ECO:0000269|PubMed:19380747}.
CC   -!- MASS SPECTROMETRY: Mass=1372.449; Mass_error=0.02; Method=Electrospray;
CC       Note=With pyroglutamate at Gln-1.;
CC       Evidence={ECO:0000269|PubMed:19380747};
CC   -!- MASS SPECTROMETRY: Mass=1389.479; Mass_error=0.02; Method=Electrospray;
CC       Note=Without pyroglutamate at Gln-1.;
CC       Evidence={ECO:0000269|PubMed:19380747};
CC   -!- SIMILARITY: Belongs to the conotoxin T superfamily. {ECO:0000305}.
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DR   ConoServer; 3754; Tx10c.
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; Hydroxylation;
KW   Neurotoxin; Oxidation; Pyrrolidone carboxylic acid; Secreted; Toxin.
FT   PEPTIDE         1..12
FT                   /note="Chi-conotoxin-like 2"
FT                   /evidence="ECO:0000269|PubMed:19380747"
FT                   /id="PRO_0000371271"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid; partial"
FT                   /evidence="ECO:0000269|PubMed:19380747, ECO:0000305"
FT   MOD_RES         8
FT                   /note="Methionine sulfoxide; partial"
FT                   /evidence="ECO:0000269|PubMed:19380747"
FT   MOD_RES         11
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:19380747"
FT   MOD_RES         12
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:19380747"
FT   DISULFID        3..12
FT                   /evidence="ECO:0000250|UniProtKB:P58807"
FT   DISULFID        4..9
FT                   /evidence="ECO:0000250|UniProtKB:P58807"
SQ   SEQUENCE   12 AA;  1364 MW;  277ABD8EE3841B58 CRC64;
     QTCCGYRMCV PC