ID   CM31_CONAA              Reviewed;          69 AA.
AC   A0A3G3C7T5;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   13-FEB-2019, sequence version 1.
DT   23-FEB-2022, entry version 14.
DE   RecName: Full=Mu-conotoxin-like Am3.1 {ECO:0000305};
DE   Flags: Precursor;
OS   Conus amadis (Amadis cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Leptoconus.
OX   NCBI_TaxID=198732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 53-68, SUBCELLULAR
RP   LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, HYDROXYLATION AT PRO-66, AND
RP   AMIDATION AT CYS-68.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=30593932; DOI=10.1016/j.jprot.2018.12.028;
RA   Vijayasarathy M., Balaram P.;
RT   "Cone snail prolyl-4-hydroxylase alpha-subunit sequences derived from
RT   transcriptomic data and mass spectrometric analysis of variable proline
RT   hydroxylation in C. amadis venom.";
RL   J. Proteomics 194:37-48(2019).
CC   -!- FUNCTION: Mu-conotoxins block voltage-gated sodium channels (Nav).
CC       {ECO:0000250|UniProtKB:P58927}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30593932}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:30593932}.
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   -!- PTM: Mostly non-hydroxylated. {ECO:0000269|PubMed:30593932}.
CC   -!- PTM: Contains 3 disulfide bonds. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin M family. {ECO:0000305}.
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DR   EMBL; MH282814; AYP73021.1; -; 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:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
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   Amidation; Direct protein sequencing; Disulfide bond; Hydroxylation;
KW   Ion channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..52
FT                   /evidence="ECO:0000305|PubMed:30593932"
FT                   /id="PRO_0000453590"
FT   PEPTIDE         53..68
FT                   /note="Mu-conotoxin-like Am3.1"
FT                   /evidence="ECO:0000269|PubMed:30593932"
FT                   /id="PRO_5018084468"
FT   REGION          22..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         66
FT                   /note="4-hydroxyproline; partial; in minor form"
FT                   /evidence="ECO:0000269|PubMed:30593932"
FT   MOD_RES         68
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:30593932"
SQ   SEQUENCE   69 AA;  7472 MW;  8D4037CE8F16B18A CRC64;
     MMSKLRVLLI ICLLLFPLTA VPLDGDQPAD RPAERTQDDI SSEHHPMFDA VRGCCPALAC
     AMGCRPCCG