ID   CM34_CONAA              Reviewed;          70 AA.
AC   A0A3G3C7U9;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   13-FEB-2019, sequence version 1.
DT   23-FEB-2022, entry version 12.
DE   RecName: Full=Mu-conotoxin-like Am3.4 {ECO:0000305};
DE   AltName: Full=Conotoxin Ama1805 {ECO:0000303|PubMed:31203793};
DE   AltName: Full=Conotoxin Ama1821 {ECO:0000303|PubMed:31203793};
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 54-69, SUBCELLULAR
RP   LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, PARTIAL HYDROXYLATION AT
RP   PRO-67, AND AMIDATION AT CYS-69.
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).
RN   [2]
RP   PROTEIN SEQUENCE OF 54-69, SUBCELLULAR LOCATION, MASS SPECTROMETRY, PARTIAL
RP   HYDROXYLATION AT PRO-67, AND AMIDATION AT CYS-69.
RC   TISSUE=Venom;
RX   PubMed=31203793; DOI=10.2174/0929866526666190614144006;
RA   Rajesh R.P., Franklin J.B., Badsha I., Arjun P., Jain R.P., Vignesh M.S.,
RA   Kannan R.R.;
RT   "Proteome based de novo sequencing of novel conotoxins from marine
RT   molluscivorous cone snail Conus amadis and neurological activities of its
RT   natural venom in zebrafish model.";
RL   Protein Pept. Lett. 26:819-833(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       ECO:0000269|PubMed:31203793}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:30593932, ECO:0000305|PubMed:31203793}.
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: Contains 3 disulfide bonds. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=1805.6; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:31203793};
CC   -!- MASS SPECTROMETRY: Mass=1821.6; Method=MALDI; Note=with hydroxyPro-67.;
CC       Evidence={ECO:0000269|PubMed:31203793};
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR   EMBL; MH282820; AYP73027.1; -; 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; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Hydroxylation; Ion channel impairing toxin; Secreted;
KW   Signal; Toxin; Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..53
FT                   /evidence="ECO:0000305|PubMed:30593932"
FT                   /id="PRO_0000453593"
FT   PEPTIDE         54..69
FT                   /note="Mu-conotoxin-like Am3.4"
FT                   /evidence="ECO:0000269|PubMed:30593932,
FT                   ECO:0000269|PubMed:31203793"
FT                   /id="PRO_5018251283"
FT   MOD_RES         67
FT                   /note="4-hydroxyproline; partial; in major form"
FT                   /evidence="ECO:0000269|PubMed:30593932,
FT                   ECO:0000269|PubMed:31203793"
FT   MOD_RES         69
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:30593932,
FT                   ECO:0000269|PubMed:31203793"
FT   DISULFID        54..69
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
FT   DISULFID        55..65
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
FT   DISULFID        61..68
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
SQ   SEQUENCE   70 AA;  8015 MW;  6FB0F61DC521FE30 CRC64;
     MMYKLGVLLI ICLLLFPLTA VPQDGDQPAD RPAERMQDDI SFEHDRFFDP VKRCCKYGWT
     CWLGCSPCCG