ID   O165_CONAA              Reviewed;          85 AA.
AC   A0A3G3C7U7;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   13-FEB-2019, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=Omega-conotoxin-like Am6.5 {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 54-84, SUBCELLULAR
RP   LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND AMIDATION AT GLN-84.
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: Omega-conotoxins act at presynaptic membranes, they bind and
CC       block voltage-gated calcium channels (Cav).
CC       {ECO:0000250|UniProtKB:P56712}.
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: Is not hydroxylated. {ECO:0000269|PubMed:30593932}.
CC   -!- SIMILARITY: Belongs to the conotoxin O1 family. {ECO:0000305}.
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DR   EMBL; MH282825; AYP73032.1; -; mRNA.
DR   SMR; A0A3G3C7U7; -.
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   Amidation; Calcium channel impairing toxin; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Knottin; Secreted; Signal;
KW   Toxin; Voltage-gated calcium channel impairing toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..53
FT                   /evidence="ECO:0000305|PubMed:30593932"
FT                   /id="PRO_0000453602"
FT   PEPTIDE         54..84
FT                   /note="Omega-conotoxin-like Am6.5"
FT                   /evidence="ECO:0000269|PubMed:30593932"
FT                   /id="PRO_5018127180"
FT   MOD_RES         84
FT                   /note="Glutamine amide"
FT                   /evidence="ECO:0000269|PubMed:30593932"
FT   DISULFID        55..73
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        62..77
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        72..81
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
SQ   SEQUENCE   85 AA;  9387 MW;  67FE4478DD27A64C CRC64;
     MCILIVAVLF LTAWTFVMAD DPRDEPDTVV RGGKLFSRAR DEMNPAASKL NERDCVEVDY
     FCGIPFVFNG LCCSGNCVFV CTPQG