CA4B_CONOB
ID CA4B_CONOB Reviewed; 19 AA.
AC P0C1W8;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Alpha-conotoxin OIVB;
DE Short=Alpha-A-O4b;
DE Short=Alpha-A-OIVB;
OS Conus obscurus (Obscure cone) (Conus halitropus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Gastridium.
OX NCBI_TaxID=89447;
RN [1]
RP PROTEIN SEQUENCE, SYNTHESIS, HYDROXYLATION AT PRO-5 AND PRO-11, AMIDATION
RP AT GLY-19, DISULFIDE BONDS, MASS SPECTROMETRY, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=15659611; DOI=10.1523/jneurosci.4065-04.2005;
RA Teichert R.W., Rivier J., Torres J., Dykert J., Miller C., Olivera B.M.;
RT "A uniquely selective inhibitor of the mammalian fetal neuromuscular
RT nicotinic acetylcholine receptor.";
RL J. Neurosci. 25:732-736(2005).
RN [2]
RP SYNTHESIS, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=16430227; DOI=10.1021/bi052016d;
RA Teichert R.W., Lopez-Vera E., Gulyas J., Watkins M., Rivier J.,
RA Olivera B.M.;
RT "Definition and characterization of the short alphaA-conotoxins: a single
RT residue determines dissociation kinetics from the fetal muscle nicotinic
RT acetylcholine receptor.";
RL Biochemistry 45:1304-1312(2006).
CC -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC This toxin blocks the fetal muscle subtype (alpha-1/beta-1/gamma/delta
CC subunits) (IC(50)=66 nM) with 1500/2000-fold greater affinity than the
CC adult (alpha-1/beta-1/epsilon/delta) subtype (IC(50)=96000 nM). It
CC blocks the currents completely and dissociates rapidly from the fetal
CC muscle receptor. Has no inhibitory activity on various neuronal nAChRs.
CC This toxin causes a reversible paralysis upon injection into gold fish.
CC {ECO:0000269|PubMed:15659611, ECO:0000269|PubMed:16430227}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC -!- DOMAIN: The cysteine framework is IV (CC-C-C-C-C).
CC -!- MASS SPECTROMETRY: Mass=1866.5; Method=FAB;
CC Evidence={ECO:0000269|PubMed:15659611};
CC -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0C1W8; -.
DR ConoServer; 1688; OIVB.
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.
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..19
FT /note="Alpha-conotoxin OIVB"
FT /id="PRO_0000249797"
FT MOD_RES 5
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:15659611"
FT MOD_RES 11
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:15659611"
FT MOD_RES 19
FT /note="Glycine amide"
FT /evidence="ECO:0000269|PubMed:15659611"
FT DISULFID 1..9
FT /evidence="ECO:0000269|PubMed:15659611"
FT DISULFID 2..14
FT /evidence="ECO:0000269|PubMed:15659611"
FT DISULFID 12..18
FT /evidence="ECO:0000269|PubMed:15659611"
SQ SEQUENCE 19 AA; 1840 MW; 21A3765DF117119C CRC64;
CCGVPNAACP PCVCNKTCG
