ID   O162_CONAH              Reviewed;          83 AA.
AC   P0C8V6;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Delta-conotoxin-like Ac6.2;
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 52-83, HYDROXYLATION AT
RP   PRO-57 AND PRO-65, 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: Delta-conotoxins bind to site 6 of voltage-gated sodium
CC       channels (Nav) and inhibit the inactivation process. {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; P0C8V6; -.
DR   SMR; P0C8V6; -.
DR   ConoServer; 3707; Ac6.2 precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004214; Conotoxin.
DR   InterPro; IPR012322; Conotoxin_d-typ_CS.
DR   Pfam; PF02950; Conotoxin; 1.
DR   PROSITE; PS60005; DELTA_CONOTOXIN; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Hydroxylation; Ion channel impairing toxin; Knottin;
KW   Neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..51
FT                   /evidence="ECO:0000269|PubMed:18286662"
FT                   /id="PRO_0000366085"
FT   PEPTIDE         52..83
FT                   /note="Delta-conotoxin-like Ac6.2"
FT                   /id="PRO_0000366086"
FT   MOD_RES         57
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:18286662"
FT   MOD_RES         65
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:18286662"
FT   DISULFID        54..69
FT                   /evidence="ECO:0000250"
FT   DISULFID        61..73
FT                   /evidence="ECO:0000250"
FT   DISULFID        68..78
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   83 AA;  9397 MW;  6EB438879F6BABFB CRC64;
     MKLTCVVIVA VLFLTAWTFV TADDSRYGLK NLFPKARHEM KNPEASKLNK RDECYPPGTF
     CGIKPGLCCS ERCFPFVCLS LEF