M7F_CONCN
ID M7F_CONCN Reviewed; 71 AA.
AC P0DKQ4; S6CPX8;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 2.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Omega-conotoxin-like CnVIIF {ECO:0000303|PubMed:22705119};
DE Contains:
DE RecName: Full=Omega-conotoxin-like CnVIID {ECO:0000303|PubMed:22705119};
DE Flags: Precursor;
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 NUCLEOTIDE SEQUENCE [MRNA], AMIDATION AT CYS-70, MASS SPECTROMETRY,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
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). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22705119}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000250|UniProtKB:P05484}.
CC -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
CC -!- MASS SPECTROMETRY: [Omega-conotoxin-like CnVIIF]: Mass=2653.96;
CC Method=Electrospray; Note=CnVIIF.;
CC Evidence={ECO:0000269|PubMed:22705119};
CC -!- MASS SPECTROMETRY: [Omega-conotoxin-like CnVIID]: Mass=2595.99;
CC Method=Electrospray; Note=CnVIID.;
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 M superfamily. {ECO:0000305}.
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DR EMBL; HE856386; CCI55499.1; -; mRNA.
DR AlphaFoldDB; P0DKQ4; -.
DR SMR; P0DKQ4; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR004214; Conotoxin.
DR InterPro; IPR012321; Conotoxin_omega-typ_CS.
DR Pfam; PF02950; Conotoxin; 1.
DR PROSITE; PS60004; OMEGA_CONOTOXIN; 1.
PE 1: Evidence at protein level;
KW Amidation; Disulfide bond; Neurotoxin; Secreted; Toxin.
FT PEPTIDE 1..71
FT /note="Omega-conotoxin-like CnVIIF"
FT /evidence="ECO:0000269|PubMed:22705119"
FT /id="PRO_0000419885"
FT PEPTIDE 1..70
FT /note="Omega-conotoxin-like CnVIID"
FT /evidence="ECO:0000269|PubMed:22705119"
FT /id="PRO_0000419886"
FT MOD_RES 70
FT /note="Cysteine amide; in CnVIID"
FT /evidence="ECO:0000269|PubMed:22705119"
FT DISULFID 46..61
FT /evidence="ECO:0000250|UniProtKB:P05484"
FT DISULFID 53..65
FT /evidence="ECO:0000250|UniProtKB:P05484"
FT DISULFID 60..70
FT /evidence="ECO:0000250|UniProtKB:P05484"
SQ SEQUENCE 71 AA; 7618 MW; AE3B29BBEB80228A CRC64;
MKLTCVVIVA VLLLTACQLI TADDSRGTQR HRALRSDTKL SMSTRCKGKG ASCSRTMYNC
CSGSCNRGKC G