ID   CM31_CONFG              Reviewed;          69 AA.
AC   A0A2D1P890;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2018, sequence version 1.
DT   03-AUG-2022, entry version 17.
DE   RecName: Full=Conotoxin Fr3.1 {ECO:0000305};
DE   AltName: Full=Conotoxin Fr2091 {ECO:0000303|PubMed:29947227};
DE   Flags: Precursor;
OS   Conus frigidus (Frigid cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Virgiconus.
OX   NCBI_TaxID=101755;
RN   [1] {ECO:0000312|EMBL:ATO88041.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 52-69, PYROGLUTAMATE
RP   FORMATION AT GLN-52, GAMMA-CARBOXYGLUTAMATION AT GLU-54, HYDROXYLATION AT
RP   PRO-58, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=29947227; DOI=10.1021/acs.jproteome.8b00132;
RA   Vijayasarathy M., Basheer S.M., Balaram P.;
RT   "Cone Snail Glutaminyl Cyclase Sequences from Transcriptomic Analysis and
RT   Mass Spectrometric Characterization of Two Pyroglutamyl Conotoxins.";
RL   J. Proteome Res. 17:2695-2703(2018).
CC   -!- FUNCTION: Probable toxin. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29947227}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:29947227}.
CC   -!- DOMAIN: The cysteine framework is III (CC-C-C-CC). Classified in the M-
CC       2 branch, since 2 residues stand between the fourth and the fifth
CC       cysteine residues. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR   EMBL; MF362622; ATO88041.1; -; mRNA.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Gamma-carboxyglutamic acid; Hydroxylation;
KW   Pyrrolidone carboxylic acid; Secreted; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..51
FT                   /evidence="ECO:0000305|PubMed:29947227"
FT                   /id="PRO_0000454999"
FT   PEPTIDE         52..69
FT                   /note="Conotoxin Fr3.1"
FT                   /evidence="ECO:0000269|PubMed:29947227"
FT                   /id="PRO_5013884406"
FT   MOD_RES         52
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:29947227"
FT   MOD_RES         54
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:29947227"
FT   MOD_RES         58
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:29947227"
SQ   SEQUENCE   69 AA;  7915 MW;  119953EB66274DE9 CRC64;
     MLKTGVLLLI FLVLFPLATL QDADQPVERN VENKQDLNLD KRRGMKLLAQ RQQECCDPDW
     CDGACYNCC