ID   CTA1B_CONMR             Reviewed;          13 AA.
AC   P58810;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2002, sequence version 1.
DT   02-JUN-2021, entry version 64.
DE   RecName: Full=Chi-conotoxin MrIB;
DE   AltName: Full=Conotoxin MrIB;
DE   AltName: Full=Lambda/chi-conotoxin MrIB;
DE            Short=Chi-MrIB;
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, SYNTHESIS, FUNCTION, HYDROXYLATION AT PRO-12, DISULFIDE
RP   BONDS, STRUCTURE BY NMR, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=11528421; DOI=10.1038/nn0901-902;
RA   Sharpe I.A., Gehrmann J., Loughnan M.L., Thomas L., Adams D.A., Atkins A.,
RA   Palant E., Craik D.J., Adams D.J., Alewood P.F., Lewis R.J.;
RT   "Two new classes of conopeptides inhibit the alpha1-adrenoceptor and
RT   noradrenaline transporter.";
RL   Nat. Neurosci. 4:902-907(2001).
CC   -!- FUNCTION: Chi-conotoxins inhibit the neuronal noradrenaline transporter
CC       (NET/SLC6A2). {ECO:0000269|PubMed:11528421}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11528421}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:11528421}.
CC   -!- DOMAIN: The cysteine framework is X (CC-CX[hydroxyPro]C).
CC       {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=1393.52; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11528421};
CC   -!- MISCELLANEOUS: Exists in two forms, due to cis-trans isomerization at
CC       11-His-Hyp-12.
CC   -!- SIMILARITY: Belongs to the conotoxin T superfamily. {ECO:0000305}.
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DR   PDB; 1IEO; NMR; -; A=1-13.
DR   PDBsum; 1IEO; -.
DR   SMR; P58810; -.
DR   ConoServer; 1737; MrIB.
DR   EvolutionaryTrace; P58810; -.
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..13
FT                   /note="Chi-conotoxin MrIB"
FT                   /id="PRO_0000044509"
FT   MOD_RES         12
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:11528421"
FT   DISULFID        4..13
FT                   /evidence="ECO:0000269|PubMed:11528421"
FT   DISULFID        5..10
FT                   /evidence="ECO:0000269|PubMed:11528421"
FT   STRAND          6..8
FT                   /evidence="ECO:0007829|PDB:1IEO"
SQ   SEQUENCE   13 AA;  1382 MW;  277AAC376EAD2B58 CRC64;
     VGVCCGYKLC HPC