EM1_CONMR
ID EM1_CONMR Reviewed; 90 AA.
AC P0DM16;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 1.
DT 25-MAY-2022, entry version 8.
DE RecName: Full=Conotoxin Mr22.1 {ECO:0000305};
DE AltName: Full=Mr104 {ECO:0000303|PubMed:23152539};
DE Flags: Precursor;
OS Conus marmoreus (Marble cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Conus.
OX NCBI_TaxID=42752;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY,
RP BROMINATION AT TRP-75, AND SUBCELLULAR LOCATION.
RX PubMed=23152539; DOI=10.1074/mcp.m112.021469;
RA Dutertre S., Jin A.H., Kaas Q., Jones A., Alewood P.F., Lewis R.J.;
RT "Deep venomics reveals the mechanism for expanded peptide diversity in cone
RT snail venom.";
RL Mol. Cell. Proteomics 12:312-329(2013).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23152539}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:23152539}.
CC -!- DOMAIN: The cysteine framework is XXII (C-C-C-C-C-C-C-C).
CC {ECO:0000305}.
CC -!- PTM: Contains 4 disulfide bonds. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the E superfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DM16; -.
DR TCDB; 8.B.1.4.1; the long (4c-c) scorpion toxin (l-st) superfamily.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Bromination; Cleavage on pair of basic residues; Disulfide bond; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..49
FT /evidence="ECO:0000305"
FT /id="PRO_0000444678"
FT CHAIN 50..90
FT /note="Conotoxin Mr22.1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000444679"
FT MOD_RES 75
FT /note="6'-bromotryptophan"
FT /evidence="ECO:0000305|PubMed:23152539"
SQ SEQUENCE 90 AA; 10546 MW; E42FFFA4F6A44142 CRC64;
MMTRVFFAMF FLMALTEGWP RLYDSDCVRG RNMHITCFKD QTCGLTVKRN GRLNCSLTCS
CRRGESCLHG EYIDWDSRGL KVHICPKPWF