CA907_CONIN
ID CA907_CONIN Reviewed; 17 AA.
AC P0DUR0;
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 In1907 {ECO:0000303|PubMed:33732044};
DE AltName: Full=Alpha-conotoxin In1857 {ECO:0000303|PubMed:33732044};
DE AltName: Full=Alpha-conotoxin In1874 {ECO:0000303|PubMed:33732044};
DE AltName: Full=Alpha-conotoxin In1891 {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, PYROGLUTAMATE
RP FORMATION AT GLU-1, HYDROXYLATION AT PRO-8 AND PRO-14, AND AMIDATION AT
RP 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 -!- PTM: Exists in 4 forms due to different PTMs (In1907, In1891, In1874,
CC and In1857). {ECO:0000305|PubMed:33732044}.
CC -!- MASS SPECTROMETRY: Mass=1907.7; Method=MALDI; Note=Hydroxylation at
CC 'Pro-8' and 'Pro-14' (In1907).; Evidence={ECO:0000269|PubMed:33732044};
CC -!- MASS SPECTROMETRY: Mass=1891.7; Method=MALDI; Note=Hydroxylation at
CC 'Pro-8' (In1891).; Evidence={ECO:0000269|PubMed:33732044};
CC -!- MASS SPECTROMETRY: Mass=1874.7; Method=MALDI; Note=Pyrrolidone
CC carboxylic acid at 'Glu-1' and hydroxylation at 'Pro-8' (In1874).;
CC Evidence={ECO:0000269|PubMed:33732044};
CC -!- MASS SPECTROMETRY: Mass=1857.6; Method=MALDI; Note=Pyrrolidone
CC carboxylic acid at 'Glu-1' (In1857).;
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;
KW Pyrrolidone carboxylic acid; Secreted; Toxin.
FT PEPTIDE 1..17
FT /note="Alpha-conotoxin In1907"
FT /evidence="ECO:0000269|PubMed:33732044"
FT /id="PRO_0000453222"
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 1
FT /note="Pyrrolidone carboxylic acid (Glu); partial; in
FT In1874 and In1857"
FT /evidence="ECO:0000269|PubMed:33732044"
FT MOD_RES 8
FT /note="4-hydroxyproline; partial; in In1907, In1891 and
FT In1874"
FT /evidence="ECO:0000269|PubMed:33732044"
FT MOD_RES 14
FT /note="4-hydroxyproline; partial; in In1907"
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; 1882 MW; DA522E4BD1699C2C CRC64;
EGCCSNPPCR HNHPEVC
