CDK3_CONMS
ID CDK3_CONMS Reviewed; 94 AA.
AC C3VVN5;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Alpha-conotoxin Ms20.3;
DE AltName: Full=Conopeptide alpha-D Ms;
DE Flags: Precursor;
OS Conus mustelinus (Weasel cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Rhizoconus.
OX NCBI_TaxID=101309;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-64,
RP GAMMA-CARBOXYGLUTAMATION AT GLU-49, HYDROXYLATION AT PRO-55, AND SUBUNIT.
RC TISSUE=Venom, and Venom duct;
RX PubMed=19275168; DOI=10.1021/bi9000326;
RA Loughnan M.L., Nicke A., Lawrence N., Lewis R.J.;
RT "Novel alpha D-conopeptides and their precursors identified by cDNA cloning
RT define the D-conotoxin superfamily.";
RL Biochemistry 48:3717-3729(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-54 AND 56-57, FUNCTION,
RP SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Venom, and Venom duct;
RX PubMed=19393680; DOI=10.1016/j.toxicon.2009.04.016;
RA Kauferstein S., Kendel Y., Nicke A., Coronas F.I.V., Possani L.D.,
RA Favreau P., Krizaj I., Wunder C., Kauert G., Mebs D.;
RT "New conopeptides of the D-superfamily selectively inhibiting neuronal
RT nicotinic acetylcholine receptors.";
RL Toxicon 54:295-301(2009).
CC -!- FUNCTION: Alpha-D-conopeptides act on postsynaptic membranes, they bind
CC to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC This toxin specifically blocks mammalian neuronal nAChR of the alpha-
CC 7/CHRNA7 (IC(50)=0.12 nM), alpha-3-beta-2/CHRNA3-CHRNB2 (IC(50)=1.08
CC nM), and alpha-4-beta-2/CHRNA4-CHRNB2 (IC(50)=4.5 nM) subtypes. Has no
CC effect on alpha-3-beta-4/CHRNA3-CHRNB4, alpha-4-beta-4/CHRNA4-CHRNB4
CC and alpha-1-beta-1-epsilon-delta/CHRNA1-CHRNB1-CHRNE-CHRND subtypes of
CC nAChRs. {ECO:0000269|PubMed:19393680}.
CC -!- SUBUNIT: Hetero-, homo- or pseudo-homodimers (identical sequence,
CC different post-translational modifications). Homodimer of [carboxyGlu-
CC 49, hydroxyPro-55]Ms20.3, and heterodimer of [carboxyGlu-49,
CC hydroxyPro-55]Ms20.3 and [carboxy'Glu-50', hydroxy'Pro-56']Ms20.5 may
CC exist. {ECO:0000269|PubMed:19275168, ECO:0000269|PubMed:19393680}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19393680}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000269|PubMed:19393680}.
CC -!- DOMAIN: The cysteine framework is XX (C-CC-C-CC-C-C-C-C).
CC -!- PTM: Contains 5 disulfide bonds. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the conotoxin D superfamily. {ECO:0000305}.
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DR EMBL; FJ896005; ACP50600.1; -; mRNA.
DR AlphaFoldDB; C3VVN5; -.
DR SMR; C3VVN5; -.
DR ConoServer; 3728; Ms20.3 precursor.
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; Direct protein sequencing;
KW Disulfide bond; Gamma-carboxyglutamic acid; Hydroxylation;
KW Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..45
FT /evidence="ECO:0000269|PubMed:19275168,
FT ECO:0000269|PubMed:19393680"
FT /id="PRO_0000388731"
FT CHAIN 46..94
FT /note="Alpha-conotoxin Ms20.3"
FT /id="PRO_0000388732"
FT MOD_RES 49
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:19275168"
FT MOD_RES 55
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:19275168"
FT CONFLICT 58
FT /note="S -> K (in Ref. 2; ACP50600)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 94 AA; 10256 MW; 571CDB3BB5CB36DB CRC64;
MPKLAVVLLV LLILPLSYFD AAGGQVVQGD RRGNGLARYL QRGDRDVREC QVNTPGSSWG
KCCMTRMCGT MCCARSGCTC VYHWRRGHGC SCPG
