ID   O17D_CONMA              Reviewed;          29 AA.
AC   Q26350;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Omega-conotoxin MVIID {ECO:0000303|PubMed:9920728};
DE   AltName: Full=SNX-238;
DE   Flags: Precursor; Fragment;
OS   Conus magus (Magical cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX   NCBI_TaxID=6492;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AMIDATION AT CYS-28, AND SYNTHESIS OF 4-28.
RX   PubMed=8107968; DOI=10.1016/0028-3908(93)90008-q;
RA   Monje V.D., Haack J.A., Naisbitt S.R., Miljanich G.P., Ramachandran J.,
RA   Nasdasdi L., Olivera B.M., Hillyard D.R., Gray W.R.;
RT   "A new Conus peptide ligand for Ca channel subtypes.";
RL   Neuropharmacology 32:1141-1149(1993).
RN   [2]
RP   STRUCTURE BY NMR OF 4-28, DISULFIDE BOND, AND SYNTHESIS OF 4-28.
RX   PubMed=9920728; DOI=10.1006/bbrc.1998.9878;
RA   Civera C., Vazquez A., Sevilla J.M., Bruix M., Gago F., Garcia A.G.,
RA   Sevilla P.;
RT   "Solution structure determination by two-dimensional 1H NMR of omega-
RT   conotoxin MVIID, a calcium channel blocker peptide.";
RL   Biochem. Biophys. Res. Commun. 254:32-35(1999).
CC   -!- FUNCTION: Omega-conotoxins act at presynaptic membranes, they bind and
CC       block voltage-gated calcium channels (Cav). This toxin blocks channels
CC       of the N-type as well as other types.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
CC   -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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DR   EMBL; S69322; AAB29902.1; -; mRNA.
DR   PIR; A58537; A58537.
DR   AlphaFoldDB; Q26350; -.
DR   SMR; Q26350; -.
DR   ConoServer; 878; MVIID precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012321; Conotoxin_omega-typ_CS.
DR   PROSITE; PS60004; OMEGA_CONOTOXIN; 1.
PE   1: Evidence at protein level;
KW   Amidation; Calcium channel impairing toxin; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Neurotoxin; Presynaptic neurotoxin;
KW   Secreted; Toxin; Voltage-gated calcium channel impairing toxin.
FT   PROPEP          <1..3
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000034918"
FT   PEPTIDE         4..28
FT                   /note="Omega-conotoxin MVIID"
FT                   /evidence="ECO:0000305|PubMed:8107968,
FT                   ECO:0000305|PubMed:9920728"
FT                   /id="PRO_0000034919"
FT   MOD_RES         28
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000305|PubMed:8107968"
FT   DISULFID        4..19
FT                   /evidence="ECO:0000269|PubMed:9920728"
FT   DISULFID        11..23
FT                   /evidence="ECO:0000269|PubMed:9920728"
FT   DISULFID        18..28
FT                   /evidence="ECO:0000269|PubMed:9920728"
FT   NON_TER         1
SQ   SEQUENCE   29 AA;  3104 MW;  9E04B2EA3779CB22 CRC64;
     STRCQGRGAS CRKTMYNCCS GSCNRGRCG