ID CA12_CONCB Reviewed; 68 AA. AC P0C1W0; DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 19-SEP-2006, sequence version 1. DT 25-MAY-2022, entry version 43. DE RecName: Full=Alpha-conotoxin-like Ca1.2; DE Flags: Precursor; OS Conus caracteristicus (Characteristic cone). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda; OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus. OX NCBI_TaxID=89440; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Venom duct; RX PubMed=14701840; DOI=10.1074/jbc.m309654200; RA Santos A.D., McIntosh J.M., Hillyard D.R., Cruz L.J., Olivera B.M.; RT "The A-superfamily of conotoxins: structural and functional divergence."; RL J. Biol. Chem. 279:17596-17606(2004). CC -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to CC the nicotinic acetylcholine receptors (nAChR) and thus inhibit them (By CC similarity). Has possibly a distinct nAChR binding mode from other CC alpha-conotoxins, due to a different three residue motif (lacks the CC Ser-Xaa-Pro motif) (By similarity). {ECO:0000250|UniProtKB:Q2I2R8}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305}. CC -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; P0C1W0; -. DR ConoServer; 13; Ca1.2 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. DR InterPro; IPR009958; Conotoxin_a-typ. DR Pfam; PF07365; Toxin_8; 1. PE 3: Inferred from homology; KW Acetylcholine receptor inhibiting toxin; Amidation; Disulfide bond; KW Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted; KW Signal; Sulfation; Toxin. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT PROPEP 22..48 FT /evidence="ECO:0000250" FT /id="PRO_0000249785" FT PEPTIDE 49..64 FT /note="Alpha-conotoxin-like Ca1.2" FT /id="PRO_0000249786" FT PROPEP 65..68 FT /evidence="ECO:0000250" FT /id="PRO_0000249787" FT REGION 52..54 FT /note="Lacks the Ser-Xaa-Pro motif that is crucial for FT potent interaction with nAChR" FT /evidence="ECO:0000305" FT MOD_RES 63 FT /note="Sulfotyrosine" FT /evidence="ECO:0000250" FT MOD_RES 64 FT /note="Cysteine amide" FT /evidence="ECO:0000250" FT DISULFID 50..56 FT /evidence="ECO:0000250|UniProtKB:P56636" FT DISULFID 51..64 FT /evidence="ECO:0000250|UniProtKB:P56636" SQ SEQUENCE 68 AA; 7326 MW; 618E8912BC5BE7AF CRC64; MGMRMMFTVF LLVVLATTVV SFTSDRASEG RNAAAKDKAS DLVALTVRGC CAIRECRLQN AAYCGGIY //