ID   O165_CONAH              Reviewed;          78 AA.
AC   P0C8V9;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Omega-conotoxin-like Ac6.5;
DE   Flags: Precursor;
OS   Conus achatinus (Little frog cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX   NCBI_TaxID=369967;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 43-78, HYDROXYLATION AT
RP   PRO-55 AND PRO-67, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=18286662; DOI=10.1002/jms.1377;
RA   Gowd K.H., Dewan K.K., Iengar P., Krishnan K.S., Balaram P.;
RT   "Probing peptide libraries from Conus achatinus using mass spectrometry and
RT   cDNA sequencing: identification of delta and omega-conotoxins.";
RL   J. Mass Spectrom. 43:791-805(2008).
CC   -!- FUNCTION: Omega-conotoxins act at presynaptic membranes, they bind and
CC       block voltage-gated calcium channels (Cav). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
CC   -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C8V9; -.
DR   SMR; P0C8V9; -.
DR   ConoServer; 3702; Ac6.5 precursor.
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   Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Hydroxylation; Ion channel impairing toxin; Knottin; Neurotoxin;
KW   Presynaptic neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated calcium channel impairing toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..42
FT                   /evidence="ECO:0000269|PubMed:18286662"
FT                   /id="PRO_0000366091"
FT   PEPTIDE         43..78
FT                   /note="Omega-conotoxin-like Ac6.5"
FT                   /id="PRO_0000366092"
FT   MOD_RES         55
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:18286662"
FT   MOD_RES         67
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:18286662"
FT   DISULFID        46..62
FT                   /evidence="ECO:0000250"
FT   DISULFID        53..65
FT                   /evidence="ECO:0000250"
FT   DISULFID        61..72
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   78 AA;  8479 MW;  BE2EAB5438A2C3C8 CRC64;
     MKLTCVVIVA VLLLTACQLL TADDSRGTQK HRSLRSTTKV SKATDCIEAG NYCGPTVMKI
     CCGFCSPFSK ICMNYPQN