ID   CTAX_CONMR              Reviewed;          61 AA.
AC   P58809; H8Y1U2;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 2.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Chi-conotoxin CMrX;
DE   AltName: Full=Conotoxin CMrX;
DE   AltName: Full=Conotoxin Mr1.6;
DE   AltName: Full=Lambda-conotoxin CMrX;
DE   Flags: Precursor;
OS   Conus marmoreus (Marble cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Conus.
OX   NCBI_TaxID=42752;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=22781954; DOI=10.1016/j.toxicon.2012.06.011;
RA   Liu Z., Li H., Liu N., Wu C., Jiang J., Yue J., Jing Y., Dai Q.;
RT   "Diversity and evolution of conotoxins in Conus virgo, Conus eburneus,
RT   Conus imperialis and Conus marmoreus from the South China Sea.";
RL   Toxicon 60:982-989(2012).
RN   [2]
RP   PROTEIN SEQUENCE OF 50-61, SYNTHESIS OF 50-61, FUNCTION, HYDROXYLATION AT
RP   PRO-60, DISULFIDE BONDS, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=10988292; DOI=10.1074/jbc.m006354200;
RA   Balaji R.A., Ohtake A., Sato K., Gopalakrishnakone P., Kini R.M.,
RA   Seow K.T., Bay B.-H.;
RT   "Lambda-conotoxins, a new family of conotoxins with unique disulfide
RT   pattern and protein folding. Isolation and characterization from the venom
RT   of Conus marmoreus.";
RL   J. Biol. Chem. 275:39516-39522(2000).
CC   -!- FUNCTION: Chi-conotoxins inhibit the neuronal noradrenaline transporter
CC       (NET/SLC6A2) (By similarity). Induces flaccid paralysis, when injected
CC       intra-cerebroventricularly into mice. {ECO:0000250|UniProtKB:P58808,
CC       ECO:0000269|PubMed:10988292}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10988292}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:10988292}.
CC   -!- DOMAIN: The cysteine framework is X (CC-CX[hydroxyPro]C).
CC       {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=1262.77; Mass_error=0.07; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10988292};
CC   -!- SIMILARITY: Belongs to the conotoxin T superfamily. {ECO:0000305}.
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DR   EMBL; JF322915; ADZ74144.1; -; mRNA.
DR   AlphaFoldDB; P58809; -.
DR   ConoServer; 1738; CMrX.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR031565; T-conotoxin.
DR   Pfam; PF16981; Chi-conotoxin; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydroxylation; Neurotoxin;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..49
FT                   /evidence="ECO:0000269|PubMed:10988292"
FT                   /id="PRO_0000425738"
FT   PEPTIDE         50..61
FT                   /note="Chi-conotoxin CMrX"
FT                   /evidence="ECO:0000269|PubMed:10988292"
FT                   /id="PRO_0000044508"
FT   MOD_RES         60
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:10988292"
FT   DISULFID        52..61
FT                   /evidence="ECO:0000269|PubMed:10988292"
FT   DISULFID        53..58
FT                   /evidence="ECO:0000269|PubMed:10988292"
SQ   SEQUENCE   61 AA;  6480 MW;  E36882339D4D143B CRC64;
     MRCLPVLIIL LLLTASAPGV DVLPKTEDDV PLSSVYGNGK SILRGILRKG ICCGVSFCYP
     C