ID   CX07_CONZO              Reviewed;          10 AA.
AC   P0DQM9;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-OCT-2020, sequence version 1.
DT   23-FEB-2022, entry version 3.
DE   RecName: Full=Conotoxin Czon1107 {ECO:0000303|PubMed:32234761};
OS   Conus zonatus (Zoned cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Stephanoconus.
OX   NCBI_TaxID=754466;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AMIDATION AT CYS-10, AND MUTAGENESIS OF PRO-5
RP   AND PRO-7.
RX   PubMed=32234761; DOI=10.1074/jbc.ra119.012098;
RA   Mohan M.K., Abraham N., Rajesh P.R., Jayaseelan B.F., Ragnarsson L.,
RA   Lewis R.J., Sarma S.P.;
RT   "Structure and allosteric activity of a single-disulfide conopeptide from
RT   Conus zonatus at human alpha3beta4 and alpha7 nicotinic acetylcholine
RT   receptors.";
RL   J. Biol. Chem. 295:7096-7112(2020).
CC   -!- FUNCTION: Strongly inhibits the human alpha-3-beta-4/CHRNA3-CHRNB4
CC       (IC(50)=15.7 uM) and alpha-7/CHRNA7 (IC(50)=77.2 uM) nicotinic
CC       acetylcholine receptor (nAChR). Incomplete inhibition of responses is
CC       observed for both subtypes, indicating a potential non-competitive mode
CC       of action. {ECO:0000269|PubMed:32234761}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32234761}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:32234761}.
CC   -!- DOMAIN: The cysteine framework is C-C. {ECO:0000305}.
CC   -!- MISCELLANEOUS: Does not modulate oxytocin (OXTR), vasopressin (AVPR1A
CC       and AVPR1B), NMDA (GRIN1 and GRIN2A), and muscarinic (CHRM1 and CHRM3)
CC       receptors, and voltage-gated calcium (Cav) and sodium channels (Nav).
CC       {ECO:0000269|PubMed:32234761}.
CC   -!- MISCELLANEOUS: Exists in two forms, due to cis-trans isomerization at
CC       4-Ser-Pro-5. The conformer with the trans conformation is the most
CC       abundant (~65:30). 6-Cys-Pro-7 and the 7-Pro-Pro-8 peptide bonds are in
CC       the cis conformation. {ECO:0000269|PubMed:32234761}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0035792; C:host cell postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Acetylcholine receptor inhibiting toxin; Amidation;
KW   Direct protein sequencing; Disulfide bond; Neurotoxin;
KW   Postsynaptic neurotoxin; Secreted; Toxin.
FT   PEPTIDE         1..10
FT                   /note="Conotoxin Czon1107"
FT                   /evidence="ECO:0000269|PubMed:32234761"
FT                   /id="PRO_0000450818"
FT   MOD_RES         10
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:32234761"
FT   DISULFID        6..10
FT                   /evidence="ECO:0000269|PubMed:32234761"
FT   MUTAGEN         5
FT                   /note="P->A: Increase in activity for alpha-7 and decrease
FT                   in activity for alpha-3-beta-4. Exists only in cis
FT                   conformation."
FT                   /evidence="ECO:0000269|PubMed:32234761"
FT   MUTAGEN         7
FT                   /note="P->A: Gain of selectivity for alpha-7 nAChR.
FT                   Increase in activity for alpha-7 and important decrease in
FT                   activity for alpha-3-beta-4. Exists in both cis and trans
FT                   conformation."
FT                   /evidence="ECO:0000269|PubMed:32234761"
SQ   SEQUENCE   10 AA;  1110 MW;  62304C776EA775A4 CRC64;
     GFRSPCPPFC