ID   CA878_CONIN             Reviewed;          17 AA.
AC   P0DUR1;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 1.
DT   23-FEB-2022, entry version 2.
DE   RecName: Full=Alpha-conotoxin In1878 {ECO:0000303|PubMed:33732044};
OS   Conus inscriptus (Engraved cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Phasmoconus.
OX   NCBI_TaxID=257329;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, MASS SPECTROMETRY, HYDROXYLATION AT
RP   PRO-8, AND AMIDATION AT CYS-17.
RC   TISSUE=Venom;
RX   PubMed=33732044; DOI=10.1016/j.sjbs.2020.12.032;
RA   Jain R.P., Jayaseelan B.F., Wilson Alphonse C.R., Mahmoud A.H.,
RA   Mohammed O.B., Ahmed Almunqedhi B.M., Rajaian Pushpabai R.;
RT   "Mass spectrometric identification and denovo sequencing of novel
RT   conotoxins from vermivorous cone snail (Conus inscriptus), and preliminary
RT   screening of its venom for biological activities in vitro and in vivo.";
RL   Saudi J. Biol. Sci. 28:1582-1595(2021).
CC   -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC       the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC       {ECO:0000250|UniProtKB:X1WB75}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:33732044}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:33732044}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
CC       {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=1878.7; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:33732044};
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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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:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR009958; Conotoxin_a-typ.
DR   InterPro; IPR018072; Conotoxin_a-typ_CS.
DR   Pfam; PF07365; Toxin_8; 1.
PE   1: Evidence at protein level;
KW   Acetylcholine receptor inhibiting toxin; Amidation;
KW   Direct protein sequencing; Disulfide bond; Hydroxylation;
KW   Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW   Toxin.
FT   PEPTIDE         1..17
FT                   /note="Alpha-conotoxin In1878"
FT                   /evidence="ECO:0000269|PubMed:33732044"
FT                   /id="PRO_0000453223"
FT   REGION          5..7
FT                   /note="Ser-Xaa-Pro motif, crucial for potent interaction
FT                   with nAChR"
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   MOD_RES         8
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:33732044"
FT   MOD_RES         17
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:33732044"
FT   DISULFID        3..9
FT                   /evidence="ECO:0000250|UniProtKB:X1WB75"
FT   DISULFID        4..17
FT                   /evidence="ECO:0000250|UniProtKB:X1WB75"
SQ   SEQUENCE   17 AA;  1869 MW;  DA522E4BD17C7C2C CRC64;
     EGCCSNPPCR HTHPEVC