ID   O162_CONAA              Reviewed;          82 AA.
AC   A0A2L2P6T9;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   25-APR-2018, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=Omega-conotoxin-like Am6.2 {ECO:0000305};
DE   AltName: Full=Am3136 {ECO:0000303|PubMed:29447903};
DE   AltName: Full=Am3214 {ECO:0000303|PubMed:29447903};
DE   AltName: Full=Am6.2a {ECO:0000303|PubMed:29447903};
DE   AltName: Full=Am6.2b {ECO:0000303|PubMed:29447903};
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 [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 53-82,
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 53-82,
RP   PARTIAL BROMINATION AT TRP-76, SUBCELLULAR LOCATION, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=29447903; DOI=10.1016/j.toxicon.2018.02.005;
RA   Vijayasarathy M., Balaram P.;
RT   "Mass spectrometric identification of bromotryptophan containing conotoxin
RT   sequences from the venom of C.amadis.";
RL   Toxicon 144:68-74(2018).
CC   -!- FUNCTION: Omega-conotoxins act at presynaptic membranes, they bind and
CC       block voltage-gated calcium channels (Cav).
CC       {ECO:0000250|UniProtKB:P56713}.
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 VI/VII (C-C-CC-C-C). {ECO:0000305}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000305}.
CC   -!- PTM: Mostly non-hydroxylated. {ECO:0000269|PubMed:30593932}.
CC   -!- PTM: Two forms of this peptides have been described. Am6.2a (Am3136) is
CC       not unmodified, while Am6.2b (Am3214) is Trp-76 brominated. Both forms
CC       are found in venom with a much more abundant brominated form.
CC       {ECO:0000269|PubMed:29447903}.
CC   -!- SIMILARITY: Belongs to the conotoxin O1 family. {ECO:0000305}.
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DR   EMBL; MG721536; AVH76829.1; -; Genomic_DNA.
DR   SMR; A0A2L2P6T9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
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   InterPro; IPR012321; Conotoxin_omega-typ_CS.
DR   Pfam; PF02950; Conotoxin; 1.
DR   PROSITE; PS60004; OMEGA_CONOTOXIN; 1.
PE   1: Evidence at protein level;
KW   Bromination; Calcium channel impairing toxin; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Knottin; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..52
FT                   /evidence="ECO:0000305|PubMed:29447903,
FT                   ECO:0000305|PubMed:30593932"
FT                   /id="PRO_0000453599"
FT   PEPTIDE         53..82
FT                   /note="Omega-conotoxin-like Am6.2"
FT                   /evidence="ECO:0000269|PubMed:29447903,
FT                   ECO:0000269|PubMed:30593932"
FT                   /id="PRO_5014869467"
FT   MOD_RES         76
FT                   /note="6'-bromotryptophan; partial; in Am6.2b (major form)"
FT                   /evidence="ECO:0000269|PubMed:29447903"
FT   DISULFID        56..73
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        63..77
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        72..81
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
SQ   SEQUENCE   82 AA;  9139 MW;  8AF3F42A7FA0F87D CRC64;
     MKLTCMMIVA VLFLTAWTFV TAVPHSSNVL ENLYLKARHE MENQEASKLN MRDDDCEPPG
     NFCGFPKIGG PCCSGWCFFA CA