O162_CONMI
ID O162_CONMI Reviewed; 83 AA.
AC Q3YEE3;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=Conotoxin MiEr92;
DE Flags: Precursor;
OS Conus miles (Soldier cone) (Mile cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Rhizoconus.
OX NCBI_TaxID=69564;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom duct;
RX PubMed=17106905; DOI=10.1002/psc.802;
RA Luo S., Zhangsun D., Feng J., Wu Y., Zhu X., Hu Y.;
RT "Diversity of the O-superfamily conotoxins from Conus miles.";
RL J. Pept. Sci. 13:44-53(2007).
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; DQ141170; AAZ83769.1; -; mRNA.
DR AlphaFoldDB; Q3YEE3; -.
DR ConoServer; 1124; MiEr92 precursor.
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 Pfam; PF02950; Conotoxin; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Knottin; Neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..49
FT /evidence="ECO:0000250"
FT /id="PRO_0000273433"
FT PEPTIDE 51..83
FT /note="Conotoxin MiEr92"
FT /id="PRO_0000273434"
FT DISULFID 52..67
FT /evidence="ECO:0000250"
FT DISULFID 59..72
FT /evidence="ECO:0000250"
FT DISULFID 66..81
FT /evidence="ECO:0000250"
SQ SEQUENCE 83 AA; 9400 MW; BFCE4D3788890174 CRC64;
MKLTCVLIVI MLFLTVCPLI TADHSRDKQE HPAMRLKDRI RYLRRGKLTR DCKHQNDSCA
EEGEECCSDL RCMTSGAGAI CVT