ID   CM746_CONIN             Reviewed;          15 AA.
AC   P0DUR4;
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=Conotoxin In1746 {ECO:0000303|PubMed:33732044};
DE   AltName: Full=Conotoxin In1762 {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-5, AND AMIDATION AT TYR-15.
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: Probable neurotoxin with unknown target (Probable). Possibly
CC       targets ion channels (Probable). In vivo, intraperitoneal injection
CC       into fish provokes paralysis after 5 minutes (By similarity).
CC       {ECO:0000250|UniProtKB:P0CH15, ECO:0000305}.
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 III (CC-C-C-CC). Classified in the M-
CC       2 branch, since 2 residues stand between the fourth and the fifth
CC       cysteine residues. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=1746.5; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:33732044};
CC   -!- MASS SPECTROMETRY: Mass=1761.6; Method=MALDI; Note=hydroxylation at
CC       Pro-5 (in In1762).; Evidence={ECO:0000269|PubMed:33732044};
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond; Hydroxylation;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Toxin.
FT   PEPTIDE         1..15
FT                   /note="Conotoxin In1746"
FT                   /evidence="ECO:0000269|PubMed:33732044"
FT                   /id="PRO_0000453226"
FT   MOD_RES         5
FT                   /note="4-hydroxyproline; partial; in In1762"
FT                   /evidence="ECO:0000269|PubMed:33732044"
FT   MOD_RES         15
FT                   /note="Tyrosine amide"
FT                   /evidence="ECO:0000269|PubMed:33732044"
FT   DISULFID        1..14
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
FT   DISULFID        2..10
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
FT   DISULFID        6..13
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
SQ   SEQUENCE   15 AA;  1754 MW;  F86474F4FE1D65FE CRC64;
     CCEWPCHHGC IPCCY