O166_CONAA
ID O166_CONAA Reviewed; 26 AA.
AC P60179;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Delta-conotoxin Am2766 {ECO:0000305|PubMed:17192003};
DE Short=Am 2766 {ECO:0000303|PubMed:14550575};
DE Short=Delta-Am2766 {ECO:0000303|PubMed:17192003};
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 PROTEIN SEQUENCE, FUNCTION, AMIDATION AT GLU-26, MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=14550575; DOI=10.1016/s0014-5793(03)01016-0;
RA Sudarslal S., Majumdar S., Ramasamy P., Dhawan R., Pal P.P., Ramaswami M.,
RA Lala A.K., Sikdar S.K., Sarma S.P., Krishnan K.S., Balaram P.;
RT "Sodium channel modulating activity in a delta-conotoxin from an Indian
RT marine snail.";
RL FEBS Lett. 553:209-212(2003).
RN [2]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=17192003; DOI=10.1002/cbdv.200590035;
RA Sarma S.P., Kumar G.S., Sudarslal S., Iengar P., Ramasamy P., Sikdar S.K.,
RA Krishnan K.S., Balaram P.;
RT "Solution structure of delta-Am2766: a highly hydrophobic delta-conotoxin
RT from Conus amadis that inhibits inactivation of neuronal voltage-gated
RT sodium channels.";
RL Chem. Biodivers. 2:535-556(2005).
CC -!- FUNCTION: Delta-conotoxins bind to site 6 of voltage-gated sodium
CC channels (Nav) and inhibit the inactivation process.
CC {ECO:0000269|PubMed:14550575}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14550575}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:14550575}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000305}.
CC -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C). {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=2766; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:14550575};
CC -!- MASS SPECTROMETRY: Mass=2766; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:14550575};
CC -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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DR PDB; 1YZ2; NMR; -; A=1-26.
DR PDBsum; 1YZ2; -.
DR AlphaFoldDB; P60179; -.
DR SMR; P60179; -.
DR ConoServer; 1630; Am2766.
DR EvolutionaryTrace; P60179; -.
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; IPR012322; Conotoxin_d-typ_CS.
DR PROSITE; PS60005; DELTA_CONOTOXIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amidation; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Knottin; Neurotoxin; Secreted; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT PEPTIDE 1..26
FT /note="Delta-conotoxin Am2766"
FT /evidence="ECO:0000269|PubMed:14550575"
FT /id="PRO_0000044474"
FT MOD_RES 26
FT /note="Glutamic acid 1-amide"
FT /evidence="ECO:0000269|PubMed:14550575"
FT DISULFID 1..16
FT /evidence="ECO:0000269|PubMed:17192003"
FT DISULFID 8..20
FT /evidence="ECO:0000269|PubMed:17192003"
FT DISULFID 15..24
FT /evidence="ECO:0000269|PubMed:17192003"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:1YZ2"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1YZ2"
SQ SEQUENCE 26 AA; 2773 MW; ADF678066CF6D615 CRC64;
CKQAGESCDI FSQNCCVGTC AFICIE
