O162_CONAE
ID O162_CONAE Reviewed; 78 AA.
AC Q9BH84;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Omega-conotoxin-like ArMKLT1-011;
DE AltName: Full=Conotoxin ArMKLT1-0131;
DE Flags: Precursor;
OS Conus arenatus (Sand-dusted cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus.
OX NCBI_TaxID=89451;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom duct;
RX PubMed=11158371; DOI=10.1093/oxfordjournals.molbev.a003786;
RA Conticello S.G., Gilad Y., Avidan N., Ben-Asher E., Levy Z., Fainzilber M.;
RT "Mechanisms for evolving hypervariability: the case of conopeptides.";
RL Mol. Biol. Evol. 18:120-131(2001).
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:0000250}.
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. {ECO:0000250}.
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; AF215038; AAG60466.1; -; mRNA.
DR EMBL; AF215106; AAG60527.1; -; mRNA.
DR AlphaFoldDB; Q9BH84; -.
DR SMR; Q9BH84; -.
DR ConoServer; 725; Ar6.2 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; IPR004214; Conotoxin.
DR InterPro; IPR012321; Conotoxin_omega-typ_CS.
DR Pfam; PF02950; Conotoxin; 1.
DR PROSITE; PS60004; OMEGA_CONOTOXIN; 1.
PE 2: Evidence at transcript level;
KW Calcium channel impairing toxin; Cleavage on pair of basic residues;
KW Disulfide bond; Ion channel impairing toxin; Knottin; Neurotoxin;
KW Presynaptic neurotoxin; Secreted; Signal; Toxin;
KW Voltage-gated calcium channel impairing toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..48
FT /evidence="ECO:0000250"
FT /id="PRO_0000404762"
FT PEPTIDE 51..78
FT /note="Omega-conotoxin-like ArMKLT1-011"
FT /id="PRO_0000404763"
FT DISULFID 52..69
FT /evidence="ECO:0000250|UniProtKB:Q26443"
FT DISULFID 59..73
FT /evidence="ECO:0000250|UniProtKB:Q26443"
FT DISULFID 68..77
FT /evidence="ECO:0000250|UniProtKB:Q26443"
SQ SEQUENCE 78 AA; 8482 MW; 4D6E59F180D8B327 CRC64;
MKLTCMMIVA VLFLTAWTSV TAVNTRGELE NLFLRASHEM NSEASKLDKK VCVDGGTFCG
FPKIGGPCCS GWCIFVCL