ID   CTA6A_CONMR             Reviewed;          11 AA.
AC   P58807;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2002, sequence version 1.
DT   02-JUN-2021, entry version 62.
DE   RecName: Full=Chi-conotoxin CMrVIA;
DE   AltName: Full=Conotoxin CMrVIA;
DE   AltName: Full=Lambda-conotoxin CMrVIA;
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   PROTEIN SEQUENCE, HYDROXYLATION AT PRO-10, DISULFIDE BONDS, SYNTHESIS, MASS
RP   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).
RN   [2]
RP   STRUCTURE BY NMR, SYNTHESIS, HYDROXYLATION AT PRO-10, AND DISULFIDE BONDS.
RX   PubMed=16903680; DOI=10.1021/bm060269w;
RA   Kang T.S., Jois S.D.S., Kini R.M.;
RT   "Solution structures of two structural isoforms of CMrVIA chi/lambda-
RT   conotoxin.";
RL   Biomacromolecules 7:2337-2346(2006).
CC   -!- FUNCTION: Chi-conotoxins inhibit the neuronal noradrenaline transporter
CC       (NET/SLC6A2). {ECO:0000250|UniProtKB:P58808}.
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=1237.93; Mass_error=0.21; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10988292};
CC   -!- SIMILARITY: Belongs to the conotoxin T superfamily. {ECO:0000305}.
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DR   PDB; 2B5P; NMR; -; A=1-11.
DR   PDB; 2B5Q; NMR; -; A=1-11.
DR   PDBsum; 2B5P; -.
DR   PDBsum; 2B5Q; -.
DR   SMR; P58807; -.
DR   EvolutionaryTrace; P58807; -.
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   3D-structure; Direct protein sequencing; Disulfide bond; Hydroxylation;
KW   Neurotoxin; Secreted; Toxin.
FT   PEPTIDE         1..11
FT                   /note="Chi-conotoxin CMrVIA"
FT                   /evidence="ECO:0000269|PubMed:10988292"
FT                   /id="PRO_0000044507"
FT   MOD_RES         10
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:10988292,
FT                   ECO:0000269|PubMed:16903680"
FT   DISULFID        2..11
FT                   /evidence="ECO:0000269|PubMed:16903680,
FT                   ECO:0000312|PDB:2B5P, ECO:0000312|PDB:2B5Q"
FT   DISULFID        3..8
FT                   /evidence="ECO:0000269|PubMed:16903680,
FT                   ECO:0000312|PDB:2B5P, ECO:0000312|PDB:2B5Q"
FT   TURN            4..6
FT                   /evidence="ECO:0007829|PDB:2B5Q"
SQ   SEQUENCE   11 AA;  1226 MW;  277AAC60B7232B58 CRC64;
     VCCGYKLCHP C