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 22-NOV-2017, entry version 33. DE RecName: Full=Alpha-conotoxin-like Ca1.2; DE Flags: Precursor; OS Conus caracteristicus (Characteristic cone). OC Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda; OC Caenogastropoda; Hypsogastropoda; Neogastropoda; Conoidea; Conidae; OC 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 RT divergence."; RL J. Biol. Chem. 279:17596-17606(2004). CC -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they CC bind to the nicotinic acetylcholine receptors (nAChR) and thus CC inhibit them. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed by the venom duct. CC -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern. 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 ProteinModelPortal; P0C1W0; -. DR ConoServer; 13; Ca1.2 precursor. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0035792; C:other organism postsynaptic membrane; IEA:UniProtKB-KW. DR GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:InterPro. DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW. DR InterPro; IPR009958; Conotoxin_a-typ. DR Pfam; PF07365; Toxin_8; 1. PE 2: Evidence at transcript level; KW Acetylcholine receptor inhibiting toxin; Amidation; Disulfide bond; KW Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; KW Secreted; Signal; Sulfation; Toxin. FT SIGNAL 1 21 {ECO:0000255}. FT PROPEP 22 48 {ECO:0000250}. FT /FTId=PRO_0000249785. FT PEPTIDE 49 64 Alpha-conotoxin-like Ca1.2. FT /FTId=PRO_0000249786. FT PROPEP 65 68 {ECO:0000250}. FT /FTId=PRO_0000249787. FT MOD_RES 63 63 Sulfotyrosine. {ECO:0000250}. FT MOD_RES 64 64 Cysteine amide. {ECO:0000250}. FT DISULFID 50 56 {ECO:0000250}. FT DISULFID 51 64 {ECO:0000250}. SQ SEQUENCE 68 AA; 7326 MW; 618E8912BC5BE7AF CRC64; MGMRMMFTVF LLVVLATTVV SFTSDRASEG RNAAAKDKAS DLVALTVRGC CAIRECRLQN AAYCGGIY //