ID   O17H_CONCN              Reviewed;          28 AA.
AC   P58916;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 2.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Omega-conotoxin-like CnVIIH {ECO:0000303|PubMed:22705119};
DE   Contains:
DE     RecName: Full=Omega-conotoxin CnVIIA {ECO:0000303|PubMed:11724570};
OS   Conus consors (Singed cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX   NCBI_TaxID=101297;
RN   [1]
RP   PROTEIN SEQUENCE, SYNTHESIS, FUNCTION, MASS SPECTROMETRY, SUBCELLULAR
RP   LOCATION, AND AMIDATION AT CYS-27.
RC   TISSUE=Venom;
RX   PubMed=11724570; DOI=10.1021/bi002871r;
RA   Favreau P., Gilles N., Lamthanh H., Bournaud R., Shimahara T., Bouet F.,
RA   Laboute P., Letourneux Y., Menez A., Molgo J., Le Gall F.;
RT   "A new omega-conotoxin that targets N-type voltage-sensitive calcium
RT   channels with unusual specificity.";
RL   Biochemistry 40:14567-14575(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], HYDROXYLATION AT PRO-7, OXIDATION AT MET-12,
RP   AMIDATION AT CYS-27, MASS SPECTROMETRY, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=22705119; DOI=10.1016/j.jprot.2012.06.001;
RA   Violette A., Biass D., Dutertre S., Koua D., Piquemal D., Pierrat F.,
RA   Stocklin R., Favreau P.;
RT   "Large-scale discovery of conopeptides and conoproteins in the injectable
RT   venom of a fish-hunting cone snail using a combined proteomic and
RT   transcriptomic approach.";
RL   J. Proteomics 75:5215-5225(2012).
CC   -!- FUNCTION: Omega-conotoxins act at presynaptic membranes, they bind and
CC       block voltage-gated calcium channels (Cav). This toxin blocks N-type
CC       calcium channels (Cav2.2/CACNA1B) with high potency. Unexpectedly, it
CC       does not show any blocking activity at amphibian neuromuscular
CC       junction. In vivo, when intracerebroventricularly injected into mice
CC       causes shaking activity, and, at higher doses, causes mild tremors.
CC       When injected intramuscularly into fish, it causes paralysis, and, at
CC       higher doses, causes death. {ECO:0000269|PubMed:11724570}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11724570}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:11724570}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
CC   -!- MASS SPECTROMETRY: [Omega-conotoxin CnVIIA]: Mass=2847.74;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:11724570};
CC   -!- MASS SPECTROMETRY: [Omega-conotoxin-like CnVIIH]: Mass=2904.17;
CC       Method=Electrospray; Note=CnVIIH.;
CC       Evidence={ECO:0000269|PubMed:22705119};
CC   -!- MASS SPECTROMETRY: [Omega-conotoxin CnVIIA]: Mass=2846.14;
CC       Method=Electrospray; Note=[Hyp7]-CnVIIA and [Pro7, oxMet12]-CnVIIA.;
CC       Evidence={ECO:0000269|PubMed:22705119};
CC   -!- MASS SPECTROMETRY: [Omega-conotoxin CnVIIA]: Mass=2830.19;
CC       Method=Electrospray; Note=[Pro7]CnVIIA.;
CC       Evidence={ECO:0000269|PubMed:22705119};
CC   -!- MISCELLANEOUS: Found in injectable (milked) (IV) venom.
CC       {ECO:0000305|PubMed:22705119}.
CC   -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P58916; -.
DR   SMR; P58916; -.
DR   ConoServer; 1632; CnVIIA.
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; Direct protein sequencing;
KW   Disulfide bond; Hydroxylation; Ion channel impairing toxin; Knottin;
KW   Neurotoxin; Oxidation; Presynaptic neurotoxin; Secreted; Toxin;
KW   Voltage-gated calcium channel impairing toxin.
FT   PEPTIDE         1..28
FT                   /note="Omega-conotoxin-like CnVIIH"
FT                   /evidence="ECO:0000269|PubMed:22705119"
FT                   /id="PRO_0000419828"
FT   PEPTIDE         1..27
FT                   /note="Omega-conotoxin CnVIIA"
FT                   /evidence="ECO:0000269|PubMed:11724570"
FT                   /id="PRO_0000044481"
FT   SITE            13
FT                   /note="Essential for calcium channel binding"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         7
FT                   /note="4-hydroxyproline; partial"
FT                   /evidence="ECO:0000269|PubMed:22705119"
FT   MOD_RES         12
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000269|PubMed:22705119"
FT   MOD_RES         27
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:11724570,
FT                   ECO:0000269|PubMed:22705119"
FT   DISULFID        1..16
FT                   /evidence="ECO:0000250"
FT   DISULFID        8..20
FT                   /evidence="ECO:0000250"
FT   DISULFID        15..27
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   28 AA;  2896 MW;  0A49DEFD1491F2CB CRC64;
     CKGKGAPCTR LMYDCCHGSC SSSKGRCG